Affinage

MARCO

Macrophage receptor MARCO · UniProt Q9UEW3

Length
520 aa
Mass
52.7 kDa
Annotated
2026-06-10
100 papers in source corpus 47 papers cited in narrative 47 extracted findings
Cross-family judge vs UniProt: tie faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MARCO (SR-A6) is a trimeric class A scavenger receptor of macrophages that mediates the direct, opsonin-independent recognition and clearance of bacteria, environmental particles, modified lipids, and viruses, while doubling as a signaling co-receptor that shapes innate and adaptive immune responses (PMID:10224290, PMID:15263032, PMID:19521507). Its ligand-binding activity resides in the C-terminal SRCR domain (domain V): an arginine-rich basic cluster centered on an RXR motif and a Ca2+-coordinating acidic cluster cooperatively engage diverse ligands, with the trimeric, collagen-stalked architecture conferring high-affinity binding (PMID:11820786, PMID:12097327, PMID:17405873, PMID:16524885). Through this domain MARCO is sufficient to bind and internalize unopsonized bacteria, TiO2, silica, nanoparticles, oxidized lipids, exosomes, and viral ligands including HSV-1 glycoprotein C and the adenovirus hexon hypervariable region, and is required in vivo for alveolar-macrophage clearance of S. pneumoniae and inhaled particles and for splenic marginal-zone capture of bacteria (PMID:10224290, PMID:9916718, PMID:15263032, PMID:16237101, PMID:16984918, PMID:17332894, PMID:18836211, PMID:23739639, PMID:29522575, PMID:33311558, PMID:16524885). Beyond clearance, MARCO functions as a co-receptor: it tethers mycobacterial trehalose dimycolate and pneumococcal ligands to amplify TLR2/CD14- and Nod2-dependent NF-κB and ERK1/2 signaling and costimulates TLR9 responses to CpG, yet by rapidly internalizing surface ligands it dampens TLR4 responses while routing ligands to intracellular sensors (TLR3, NOD2, NALP3, cGAS) (PMID:16882874, PMID:19521507, PMID:21098741, PMID:23197261, PMID:28765216). Ectopic MARCO expression remodels the actin cytoskeleton through Rac1, driving lamellipodia and dendritic processes, focal-adhesion loss, dendritic-cell maturation with reduced antigen uptake, and constraint of DC migration to lymph nodes (PMID:10196178, PMID:12842997, PMID:17442975). MARCO expression is induced by LPS and IL-10/STAT3, by the Akt–TFEB axis, and by Nrf2 (whose p300-dependent acetylation is disrupted by cigarette smoke), and is suppressed by HIF-2α via mitochondrial ROS (PMID:9916718, PMID:27671111, PMID:28408365, PMID:32153580, PMID:32512637). In the circulation, MARCO on liver Kupffer cells and lymph-node lymphatic endothelial cells clears arthritogenic alphaviruses in a species- and SRCR-domain-dependent manner dictated by specific E2 lysine residues, and in adipose-tissue macrophages it drives PI3K-dependent lipid uptake supporting metabolic health (PMID:31596239, PMID:33199895, PMID:34618370, PMID:37083332). Loss of MARCO impairs apoptotic-cell clearance and predisposes to SLE-like autoimmunity, and in tumors MARCO+ macrophages suppress STING/IFN-β responses, linking the receptor to disease (PMID:19201851, PMID:38065400).

Mechanistic history

Synthesis pass · year-by-year structured walk · 22 steps
  1. 1998 High

    Localizing the bacteria-binding region established that MARCO recognizes ligands through its C-terminal SRCR domain rather than its collagenous stalk, defining where engagement occurs.

    Evidence Binding assays with truncated MARCO variants plus disulfide-bond mapping of domain V

    PMID:9468508

    Open questions at the time
    • Atomic basis of binding not resolved at this stage
    • Did not identify which residues contact ligand
  2. 1999 High

    Reconstitution and in vivo blockade showed MARCO is sufficient and required for opsonin-independent capture of bacteria and environmental particles, defining its core scavenging function and LPS-inducible expression.

    Evidence COS-cell transfection, anti-MARCO mAb inhibition, in vivo splenic bacterial capture, LPS upregulation

    PMID:10224290 PMID:9916718

    Open questions at the time
    • Downstream fate of internalized particles not defined
    • Signaling consequences of ligation not addressed
  3. 1999 High

    Ectopic expression revealed that MARCO is not merely a sink but actively remodels the actin cytoskeleton through Rac1, linking the receptor to cell morphology and adhesion.

    Evidence Ectopic expression in multiple cell lines with dominant-negative Rac1/Cdc42 and domain truncations

    PMID:10196178

    Open questions at the time
    • Mechanism coupling SRCR domain to Rac1 not defined
    • No intracellular adaptor identified
  4. 2002 High

    Mutagenesis and biophysical reconstitution pinned ligand binding to an arginine-rich RXR motif and showed high-affinity binding requires the trimeric collagenous architecture, explaining how MARCO differs from related scavenger receptors.

    Evidence Deletion/substitution mutagenesis, circular dichroism, rotary-shadowing EM, cell-free binding of recombinant MARCO

    PMID:11820786 PMID:12097327

    Open questions at the time
    • Three-dimensional structure not yet solved
    • Role of metal ions in binding not yet shown
  5. 2003 High

    Gain- and loss-of-function in dendritic cells and microglia established MARCO as a driver of cytoskeletal remodeling and maturation that simultaneously reduces antigen internalization, bridging scavenging and adaptive-immune regulation.

    Evidence MARCO transfection and knockdown in DCs with actin imaging and antigen-uptake assays

    PMID:12842997

    Open questions at the time
    • Signaling pathway from MARCO to maturation not mapped
    • In vivo relevance to DC function not tested here
  6. 2004 High

    The MARCO-knockout mouse demonstrated a non-redundant in vivo role in clearing S. pneumoniae and inert particles from the lung, with loss causing excess inflammation, establishing physiological importance.

    Evidence MARCO-/- mice in pneumococcal challenge and particle-uptake assays with cytokine readouts

    PMID:15263032

    Open questions at the time
    • Did not dissect signaling versus uptake contributions
    • Other lung pathogens not surveyed
  7. 2005 High

    Studies in alveolar and peritoneal macrophages and KO mice showed MARCO both confers human particle/bacterial binding and costimulates IL-12, and revealed its Th1-biased, SR-A-opposite expression regulation and roles in marginal-zone architecture.

    Evidence Inhibitory mAb mapping, COS-cell reconstitution, MARCO-/- macrophage IL-12 assays, splenic histology, vaccination

    PMID:16237101 PMID:16339540 PMID:16339556

    Open questions at the time
    • Receptor that transduces costimulatory signal not identified
    • Mechanism of marginal-zone maintenance unclear
  8. 2006 High

    Ligand-spectrum mapping (phage display, SPR, KO macrophages) defined the SRCR domain as the dominant binding site distinguishing MARCO from SR-A, and extended ligands to CpG-ODN, nanoparticles, and Neisseria, establishing MARCO as a TLR9 costimulator.

    Evidence Phage display, surface plasmon resonance, chimeric receptor binding, COS-7 nanoparticle uptake, MARCO-/- CpG/IL-12 assays

    PMID:16524885 PMID:16525990 PMID:16882874 PMID:17361018

    Open questions at the time
    • Relative affinities for physiological ligands not fully ranked
    • How MARCO delivers CpG to TLR9 compartment unclear
  9. 2007 High

    The crystal structure of the SRCR domain provided the atomic framework, showing a basic arginine cluster and a Ca2+-binding acidic loop that cooperatively engage ligands, and KO/DC studies extended function to oxidized-lipid scavenging and dampening adaptive responses.

    Evidence X-ray crystallography of mouse SRCR domain with mutagenesis; MARCO-/- mice in ozone/oxidized-lipid and DC-migration models

    PMID:17332894 PMID:17405873 PMID:17442975

    Open questions at the time
    • Full-length trimer structure not determined
    • Structural basis for distinct particle-binding motifs not resolved
  10. 2009 High

    Mechanistic dissection of mycobacterial cord-factor sensing showed MARCO tethers TDM and is required for TLR2/CD14-dependent NF-κB and ERK1/2 activation, defining MARCO as a bona fide signaling co-receptor; KO mice also linked MARCO to apoptotic-cell clearance and autoimmunity.

    Evidence NF-κB reporter, MARCO/TLR2/CD14-/- macrophages, ERK phosphorylation, M. tuberculosis infection; BXSB mouse SLE model

    PMID:19201851 PMID:19521507

    Open questions at the time
    • Physical MARCO-TLR2 contact not directly shown here
    • Adaptor coupling MARCO to MAPK unknown
  11. 2010 High

    Triple-KO studies clarified MARCO's dual signaling logic—internalization attenuates surface TLR4 responses while enhancing intracellular TLR3/NOD2/NALP3 sensing—and a co-IP identified formyl-peptide receptors as physical partners coupling MARCO to ERK/cAMP signaling.

    Evidence SR-A/MARCO single and double KO mice with innate-receptor agonists; co-IP and signaling assays with FPR/FPRL1 in glial cells

    PMID:20141570 PMID:21098741

    Open questions at the time
    • FPRL1 interaction rests on single-lab co-IP without reciprocal in vivo validation
    • Compartmental routing mechanism not molecularly defined
  12. 2011 High

    In vivo colonization studies extended MARCO co-receptor function to Nod2- and TLR2-dependent NF-κB signaling during pneumococcal colonization, and cell studies showed nanotube uptake proceeds via MARCO-induced dendritic structures and macropinocytosis.

    Evidence MARCO/SRA/MR KO mice in nasopharyngeal colonization with NF-κB reporters; CHO-K1 MARCO transfection with live imaging and EM

    PMID:22209804 PMID:23197261

    Open questions at the time
    • Order of Nod2 versus TLR2 engagement not resolved
    • Internalization route generality across ligands unclear
  13. 2013 High

    Direct binding of HSV-1 glycoprotein C to purified MARCO, with KO and overexpression mice, established MARCO as a viral receptor cooperating with heparan sulfate, broadening its role from bacterial to viral recognition.

    Evidence Direct binding assay with purified proteins, MARCO-/- and overexpression infection models, ligand competition

    PMID:23739639

    Open questions at the time
    • Post-binding entry steps not detailed
    • Whether MARCO signals upon HSV-1 binding not addressed
  14. 2014 High

    Vaccinia binding, the SRCR-lacking MARCOII dominant-negative variant, particle-motif mapping, and silica/inflammasome studies together cemented the SRCR domain as essential for binding, phagocytosis, adhesion, and TLR2 signaling, and revealed MARCO restrains NLRP3 activation by limiting lysosomal damage.

    Evidence VV binding/competition; MARCOII co-expression dominant-negative; CHO competitive binding/ion chelation; MARCO-/- AM inflammasome assays

    PMID:18836211 PMID:25054161 PMID:25089661 PMID:26888252

    Open questions at the time
    • Endogenous regulation of MARCOII splicing unknown
    • Link between cholesterol recycling and LMP not fully mechanistic
  15. 2015 Medium

    Live-imaging of GFP-MARCO defined two internalization routes—macropinocytosis and endocytosis to LC3B-positive amphisomes—clarifying the intracellular trafficking that underlies ligand delivery to degradative and sensing compartments.

    Evidence GFP-MARCO stable CHO-K1 cells with co-localization and pharmacological/cytoskeletal dissection

    PMID:26545255

    Open questions at the time
    • Single-lab reconstituted system, not primary macrophages
    • Sorting determinants between the two routes unknown
  16. 2016 Medium

    Transcriptional-regulation studies positioned MARCO downstream of an NRF2-activating, HIF-2α-suppressing axis tuned by mitochondrial ROS, beginning to explain how phagocytic capacity is set by macrophage metabolic state.

    Evidence Hif-2α-/- macrophages, NRF2 ChIP, mitochondrial ROS inhibition, phagocytosis and bacterial-clearance assays

    PMID:27671111

    Open questions at the time
    • Single-lab finding
    • Direct NRF2 occupancy of human MARCO promoter not shown
  17. 2017 High

    Adenovirus studies identified MARCO as a macrophage entry receptor via the negatively charged hexon HVR1, coupling viral uptake to cGAS sensing, while the Akt–TFEB and Nrf2 pathways and free extracellular actin were shown to regulate MARCO expression and ligand binding.

    Evidence MARCO KO/reconstituted cells, soluble SR-A6 domain, hexon HVR1 mutant, cGAS readouts; Akt/Nrf2/TFEB pharmacology and knockdown; actin competition in KO cells/mice

    PMID:28385809 PMID:28408365 PMID:28765216

    Open questions at the time
    • Whether MARCO-cGAS coupling requires specific trafficking step unclear
    • Physiological source of free actin ligand in vivo uncertain
  18. 2018 High

    Receptor swaps and a hexon HVR1 deletion mutant formally defined hexon as the adenoviral ligand for SR-A6 across multiple adenovirus types, with species differences in receptor activity.

    Evidence SR-A6 KO and cross-species overexpression, soluble receptor domain, hexon HVR1 deletion, binding/transduction assays

    PMID:29522575

    Open questions at the time
    • Structural basis of hexon-SRCR recognition not solved
    • In vivo consequence for adenoviral pathogenesis not established
  19. 2019 High

    Alphavirus clearance studies showed MARCO on Kupffer cells removes circulating CHIKV/RRV/ONNV in an antibody- and complement-independent manner dictated by specific E2 lysines, defining a sequence-specific antiviral clearance mechanism.

    Evidence MARCO-/- and C3-/- mice, alphavirus E2 K→R mutants, viremia, Kupffer-cell depletion

    PMID:31596239

    Open questions at the time
    • Atomic contacts between E2 lysines and SRCR domain not resolved
    • Fate of captured virions in Kupffer cells unclear
  20. 2020 High

    Multiple studies expanded MARCO's roles: exosome internalization via dynamin/macropinocytosis, PI3K-driven beneficial lipid-buffering adipose macrophages, IL-10/STAT3-dependent induction enhancing bacterial killing, and cigarette-smoke suppression via p300 degradation blocking Nrf2 acetylation.

    Evidence CHO-MARCO exosome uptake; macrophage PTEN-KO and dual MARCO/PTEN-KO mice; IL-10-/- mice with STAT3 inhibition; CSE with siRNA and proteasome inhibition

    PMID:32153580 PMID:32512637 PMID:33199895 PMID:33311558

    Open questions at the time
    • Direct exosome ligand on MARCO not identified
    • Whether smoke-induced MARCO loss explains COPD susceptibility not tested in patients
  21. 2021 Medium

    MARCO was shown to bind β5 integrin to drive SYK/PI3K/Rac1-dependent tumor-cell phagocytosis, to interact physically with TLR2 via its SRCR domain in neuroinflammation, and to capture alphaviruses on lymph-node lymphatic endothelial cells upstream of Kupffer-cell clearance.

    Evidence Co-IP for β5 integrin and TLR2 with SRCR deletion; MARCO KD/OE phagocytosis; MARCO-/- mice with intravital imaging of LEC alphavirus capture

    PMID:34398403 PMID:34618370 PMID:34626585

    Open questions at the time
    • β5-integrin and TLR2 interactions rest on single-lab co-IPs without reciprocal validation
    • Whether LEC capture uses same E2-lysine determinants as Kupffer cells not tested
  22. 2023 High

    Domain-swap studies tied alphavirus internalization to the SRCR domain with species-specific efficiency matching amplification-host status, and tumor studies defined MARCO+ TAMs as immunosuppressive by clearing dying cells and damping STING/IFN-β signaling.

    Evidence SRCR domain mutants/swaps with in vitro virus internalization and rhesus viremia; clinical specimens, tumor models, cGAMP/ATP and STING assays, anti-MARCO+anti-PD-L1 treatment

    PMID:37083332 PMID:37212598 PMID:38065400

    Open questions at the time
    • Mechanistic link between SRCR sequence and host range incomplete
    • Tumor STING-suppression pathway elements from single labs

Open questions

Synthesis pass · forward-looking unresolved questions
  • How MARCO physically couples ligand engagement to intracellular signaling (the adaptor or transducing partner driving Rac1, MAPK, and co-receptor amplification) and the full-length trimeric receptor structure remain undefined.
  • No cytoplasmic signaling adaptor identified
  • No full-length trimer structure
  • Mechanism of ligand handoff to TLR/Nod/cGAS sensors not molecularly defined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0038024 cargo receptor activity 7 GO:0001618 virus receptor activity 6 GO:0060089 molecular transducer activity 4 GO:0008289 lipid binding 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005886 plasma membrane 5 GO:0005764 lysosome 2 GO:0031410 cytoplasmic vesicle 2
Pathway
R-HSA-9609507 Protein localization 5 R-HSA-162582 Signal Transduction 4 R-HSA-168256 Immune System 4 R-HSA-1430728 Metabolism 2 R-HSA-1643685 Disease 2
Partners
CD14FPRL1ITGB5NOD2TLR2TLR9

Evidence

Reading pass · 47 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 The bacteria-binding region of human MARCO was localized to a region proximal to the cysteine-rich part of the COOH-terminal domain V (SRCR domain). The intrachain disulfide bond pattern of domain V was established: cysteine pairs C1-C5, C2-C6, and C3-C4. The human MARCO polypeptide lacks the intracellular cysteine present in mouse MARCO and two extracellular cysteines that form interchain disulfide bonds in murine protein. Binding studies with full-length and truncated MARCO variants expressed in cells; structural analysis The Journal of biological chemistry High 9468508
1999 MARCO mediates binding of unopsonized environmental particles (TiO2, Fe2O3, latex beads) and unopsonized bacteria (E. coli, S. aureus) by alveolar macrophages. Transfection of COS cells with MARCO cDNA conferred particle-binding activity inhibitable by anti-MARCO mAb PAL-1, demonstrating MARCO is sufficient for this function. Monoclonal antibody inhibition assay, COS cell transfection with MARCO cDNA, flow cytometry, immunoprecipitation The Journal of experimental medicine High 10224290
1999 MARCO expression on marginal zone macrophages of spleen and lymph node macrophages is required for capturing heat-killed bacteria in the splenic marginal zone in vivo. Inhibitory anti-MARCO mAbs blocked this capturing. LPS stimulation up-regulates MARCO surface expression on macrophages in a dose- and time-dependent fashion. In vivo bacterial clearance with inhibitory mAbs; LPS stimulation of J774.2 cells; immunohistochemistry Journal of immunology Medium 9916718
1999 Ectopic expression of MARCO in non-macrophage cell lines (CHO, HeLa, NIH3T3, 293) induces dramatic cell shape changes including formation of large lamellipodia-like structures and long dendritic processes, accompanied by disassembly of actin stress fibers and loss of focal adhesions. These morphogenic effects are dependent on cell adhesion, partially inhibited by dominant-negative Rac1 but not Cdc42, and require the proximal segment of the cysteine-rich domain V. Ectopic expression in cell lines, dominant-negative Rac1/Cdc42 mutants, truncated MARCO variants, fluorescence microscopy The Journal of biological chemistry High 10196178
2002 The primary bacteria-binding region of MARCO is localized to domain V (SRCR domain). An arginine-rich segment containing the RXR motif within domain V is essential for high-affinity bacterial binding, as shown by deletion and single amino acid substitution variants. This differs from SR-A and SRCL, whose ligand-binding is localized to the collagenous domain. Deletion and single amino acid substitution mutagenesis of human and mouse MARCO; bacterial binding assays in transfected cells Biochemical and biophysical research communications High 11820786
2002 Soluble recombinant MARCO (sMARCO) has a triple-helical collagenous structure confirmed by circular dichroism and rotary shadowing electron microscopy. sMARCO binds heat-killed and living bacteria and LPS. The O-side chain of LPS is not needed for bacterial recognition. The isolated monomeric SRCR domain showed low bacteria-binding activity, suggesting cooperation between the SRCR domain and the collagenous domain, or that the SRCR domain must be trimeric for high-affinity bacterial binding. Circular dichroism, protease-sensitive assay, rotary shadowing electron microscopy, cell-free bacterial binding assays, recombinant SRCR domain binding studies The Journal of biological chemistry High 12097327
2003 MARCO expression in dendritic cells (DCs) and microglia is associated with profound actin cytoskeleton rearrangements. Simple expression of MARCO was sufficient to induce cytoskeleton modifications (round, non-adherent morphology with punctate actin) in DCs. Knockdown of MARCO prevented DCs from reaching mature phenotype. MARCO expression is also associated with decreased antigen internalization capacity. MARCO transfection in immature DCs, MARCO knockdown (siRNA/antisense), actin cytoskeleton imaging, antigen uptake assays Blood High 12842997
2004 MARCO-deficient mice show impaired clearance of S. pneumoniae from lungs, increased pulmonary inflammation and cytokine release, and diminished survival. In vitro binding of S. pneumoniae and in vivo uptake of unopsonized TiO2 particles by MARCO-/- alveolar macrophages were dramatically impaired. MARCO-mediated clearance of inert particles by alveolar macrophages prevents inflammatory responses otherwise initiated by other lung cells. MARCO-/- mouse model, pneumococcal pneumonia challenge, in vitro bacterial binding assay, in vivo particle uptake, cytokine measurement The Journal of experimental medicine High 15263032
2005 MARCO is the major binding receptor for unopsonized particles and bacteria on human alveolar macrophages. Anti-human MARCO mAb PLK-1 inhibited AM binding of TiO2 (63%), latex beads (67%), E. coli (~84%), and S. aureus (~41%). PLK-1 epitope was mapped to MARCO domain V between amino acid residues 420-431. Other SR antibodies failed to inhibit TiO2 or S. aureus binding. Functional screening of anti-AM hybridomas, mAb inhibition assay, COS cell transfection with truncated MARCO forms, flow cytometry, immunoprecipitation Journal of immunology High 16237101
2005 Ligation of MARCO on peritoneal macrophages costimulates IL-12 production (in contrast to SR-AI/II which inhibits it). MARCO-deficient macrophages show 2.7x lower IL-12 production in response to LPS+IFN-γ. Th1 adjuvants (LPS, CpG-ODN, IL-12, GM-CSF) increase MARCO expression, while Th2 factors (IL-4, M-CSF) decrease it—opposite to SR-A regulation. MARCO-/- and SR-AI/II-/- peritoneal macrophages, IL-12 ELISA, immobilized mAb ligation, pharmacological manipulation of macrophage polarization Journal of immunology High 16339540
2005 Genetic ablation of MARCO leads to changes in splenic marginal zone organization and significant reduction of resident peritoneal macrophage population, suggesting roles in adhesion and migration. In MARCO/SR-A double-KO mice these effects are more apparent. MARCO-/- mice show impaired response to thymus-independent type 2 antigen (pneumococcal polysaccharide vaccine), dependent on intact marginal zone. MARCO-/- and MARCO/SR-A double-KO mice, histological analysis, macrophage population counts, pneumococcal polysaccharide vaccination, macrophage depletion/reconstitution Journal of immunology High 16339556
2006 MARCO is the critical scavenger receptor for silica uptake and cytotoxicity in primary alveolar macrophages from C57BL/6 mice. No silica particle uptake or cell death occurred in MARCO-/- alveolar macrophages. Silica uptake was proportional to cell surface MARCO expression. Transfection of CHO cells with human MARCO conferred silica binding and silica-induced apoptosis. MARCO-/-, CD204-/-, CD36-/- single and double null mice, anti-MARCO antibody blockade, CHO cell transfection with human MARCO, particle uptake and cytotoxicity assays The Journal of biological chemistry High 16984918
2006 MARCO and SR-AI/II differentially recognize polyanionic ligands and surface proteins from Neisseria meningitidis; acetylated LDL (AcLDL) is a ligand for SR-A but not MARCO. Both mouse and human MARCO bind NM independently of NM LPS. MARCO and SR-A contribute independently to NM binding but neither is required for TNF-α and nitric oxide release. MARCO-/-, SR-A-/-, SR-A-MARCO-/- peritoneal macrophages; binding assays; TNF-α and NO measurement European journal of immunology Medium 16525990
2006 MARCO binds and costimulates macrophage responses to CpG oligodeoxynucleotides (PS-linked). MARCO-deficient thioglycollate-elicited peritoneal macrophages fail to produce IL-12 and NO in response to PS-CpG-ODN. MARCO is a signaling receptor that costimulates TLR9-mediated NO and IL-12 production. MARCO-/- peritoneal macrophages, IL-12 and NO assays, immobilized mAb MARCO ligation Journal of leukocyte biology Medium 16882874
2007 Crystal structure of mouse MARCO SRCR domain was determined at 1.77-1.78 Å resolution. The monomer has a compact globular fold with a twisted five-stranded antiparallel β-sheet and a long loop covering a single α-helix. The dimer forms via β-strand swapping generating an eight-stranded β-sheet. A basic cluster (arginines on β-sheet) and an acidic cluster (in the long loop) both contribute to ligand binding. All arginines of the basic cluster are involved in ligand binding via cooperative mechanism. The acidic cluster binds Ca2+ ions, and Ca2+ depletion affects ligand binding. X-ray crystallography, SRCR domain mutants expressed in cells, ligand-binding assays, Ca2+ depletion experiments The Journal of biological chemistry High 17405873
2007 MARCO and SR-AI/II on alveolar macrophages protect against inhaled oxidants by scavenging oxidized lipids from lung lining fluid. MARCO-/- mice show greater lung injury after ozone exposure. Normal AMs show greater in vitro uptake of 5β,6β-epoxycholesterol compared to MARCO-/- AMs. Instillation of oxidized lipids (beta-epoxide, PON-GPC) causes neutrophil influx in MARCO-/- but not MARCO+/+ mice. MARCO-/- and SR-AI/II-/- mice, ozone and oxidized lipid exposure, BAL neutrophil counts, in vitro oxidized lipid uptake assay The Journal of clinical investigation High 17332894
2007 MARCO and SR-AI/II expressed on lung dendritic cells limit DC migration from lung to draining lymph nodes. SR-A-deficient mice show significantly higher traffic of labeled DCs to thoracic lymph nodes after allergen challenge and enhanced T cell proliferation. This identifies a role for scavenger receptors on DCs in downregulating adaptive immune responses to aeroallergens. SR-AI/II-/- and MARCO-/- mice, OVA sensitization/challenge model, fluorescent antigen trafficking, adoptive transfer of OVA-specific T cells, lymph node DC counts Journal of immunology Medium 17442975
2007 Murine scavenger receptor MARCO recognizes polystyrene nanoparticles (20 nm, 200 nm, 1 μm). MARCO-transfected COS-7 cells associated with all three sizes of particles in a time-dependent manner; uptake was partially inhibited by polyG. COS-7 cell transfection with MARCO cDNA, fluorescence microscopy, atomic force microscopy, polyG inhibition Toxicological sciences Medium 17361018
2008 The SRCR domain of MARCO is required for particle binding of all tested particles (amorphous silica, crystalline silica, TiO2). TiO2 uniquely required divalent cations (Ca2+/Mg2+) for MARCO binding. TiO2 and silica particles bound to different motifs within the SRCR domain of MARCO, as shown by competitive binding studies. CHO cells transfected with human MARCO and MARCO mutants, competitive binding studies, divalent cation chelation, anti-MARCO antibody blockade Toxicological sciences High 18836211
2009 MARCO is required for macrophage cytokine responses to mycobacterial trehalose dimycolate (TDM/cord factor). MARCO tethers TDM to the macrophage and activates the TLR2/CD14 signaling pathway. TDM-induced NF-κB signaling requires MARCO in addition to TLR2 and CD14. MARCO-/- and MARCO-/-SRA-/- macrophages are defective in ERK1/2 activation and pro-inflammatory cytokine production in response to TDM. MARCO-expressing macrophages also produce markedly higher pro-inflammatory cytokines in response to virulent M. tuberculosis infection. NF-κB-luciferase reporter assay, MARCO-/-, TLR2-/-, CD14-/- macrophages, ERK1/2 phosphorylation, cytokine ELISA, M. tuberculosis infection PLoS pathogens High 19521507
2009 MARCO deficiency in BXSB mice results in impaired clearance of apoptotic cells and a generalized defect in both endocytosis and phagocytosis. Reduced MARCO expression contributes to the development of SLE-like disease by failure to clear apoptotic cells, leading to anti-dsDNA antibody production. BXSB congenic mice, apoptotic cell clearance assays, endocytosis and phagocytosis assays, anti-dsDNA antibody measurement Journal of immunology Medium 19201851
2010 SR-A and MARCO attenuate TLR4-mediated responses while enhancing responses by intracellular sensors TLR3, NOD2, and NALP3. This occurs because SR-A/MARCO-mediated rapid ligand internalization prevents sensing by surface TLRs while increasing ligand availability in intracellular compartments. SR-A-/-, MARCO-/-, SR-A-/-MARCO-/- mice; NF-κB reporter; TLR3, NOD2, NALP3 agonists; cytokine assays Blood High 21098741
2010 MARCO physically interacts with formyl peptide receptors FPR and FPRL1, as demonstrated by co-immunoprecipitation and fluorescence microscopy. MARCO functionally interacts with FPRL1 in fucoidan-mediated ERK1/2 phosphorylation and cAMP signaling in glial cells. FPRL1 (not MARCO alone) is the primary mediator of Aβ1-42-induced ERK1/2 signaling. Co-immunoprecipitation, fluorescence microscopy, siRNA knockdown, ERK1/2 phosphorylation assay, cAMP measurement in astrocytes/microglia and HEK293 transfectants Journal of neurochemistry Medium 20141570
2011 MARCO mediates cellular uptake of carbon nanotubes (MWCNTs) in MARCO-transfected CHO-K1 cells. MWCNTs are first tethered to MARCO-induced dendritic structures and then taken up via membrane ruffling (macropinocytosis-like). MARCO transfection also caused formation of dynamic dendritic structures. MARCO transfection in CHO-K1 cells, live cell microscopy, transmission electron microscopy, cytotoxicity assays Toxicology and applied pharmacology Medium 22209804
2011 MARCO is required for maximal TLR2- and Nod2-dependent NF-κB activation and signaling during S. pneumoniae nasopharyngeal colonization. MARCO-/- mice show impaired clearance, abrogated cytokine/chemokine production including type I IFNs, and reduced cellular recruitment to the nasopharynx. MARCO-/-, SRA-/-, MR-/- KO mice; nasopharyngeal colonization model; NF-κB reporter assays; cytokine/chemokine ELISA Journal of immunology High 23197261
2013 HSV-1 glycoprotein C binds directly to purified MARCO with high affinity. MARCO functions together with heparan sulfate proteoglycans to mediate HSV-1 adsorption to epithelial cells. MARCO-/- mice have reduced susceptibility to HSV-1 infection. Ligands of MARCO inhibit HSV-1 adsorption and infection. Increasing MARCO expression enhances HSV-1 infection. Direct binding assay with purified MARCO and HSV-1 glycoprotein C, MARCO-/- mice infection model, MARCO overexpression, MARCO ligand competition assays, co-localization studies Nature communications High 23739639
2014 Vaccinia virus binds directly to MARCO on keratinocytes. Overexpression of MARCO increased susceptibility to VV infection. Ligands with affinity for MARCO or excess soluble MARCO competitively inhibited VV infection. Direct binding assay, MARCO overexpression, competitive inhibition with MARCO ligands, infection assays The Journal of investigative dermatology Medium 25089661
2014 The SRCR domain of MARCO is critical for ligand binding, phagocytosis, TLR2-mediated pro-inflammatory signaling, and cellular adhesion. A naturally occurring transcript variant MARCOII lacking the SRCR domain abolished ligand binding. Co-expression of MARCO and MARCOII impaired phagocytic function (dominant-negative effect). MARCOII did not enhance TLR2-mediated signaling. MARCO-expressing cells were more adherent with dendritic-like phenotype, MARCOII-expressing cells were less adherent. MARCOII natural variant expression, co-expression dominant-negative assays, ligand binding, TLR2 NF-κB reporter, adhesion assays Immunology and cell biology High 26888252
2014 In the absence of MARCO, NLRP3 inflammasome activation and IL-1β release are increased in response to silica particles in alveolar macrophages. MARCO-/- AMs show greater cathepsin B release, caspase-1 activation, and acid sphingomyelinase activity, consistent with lysosomal membrane permeabilization (LMP). MARCO contributes to normal cholesterol recycling in macrophages; absence of MARCO leads to increased susceptibility to LMP. MARCO-/- vs. WT alveolar macrophages, NLRP3 inflammasome assays, cathepsin B and caspase-1 activation, cholesterol sequestration assay, U18666A treatment Journal of immunology research Medium 25054161
2015 MARCO is internalized by two pathways: (1) macropinocytosis via plasma membrane ruffling generating large vesicles, and (2) endocytosis followed by fusion with autophagosomes (amphisomes) generating small puncta that co-localize with LC3B and lysosomes. Trafficking of small puncta is regulated by tubulin but not actin. GFP-MARCO stable transfection in CHO-K1 cells, live fluorescence microscopy, co-localization with LC3B/lysosome markers, pharmacological inhibitors, tubulin/actin disruption PloS one Medium 26545255
2016 HIF-2α suppresses MARCO-dependent phagocytosis under non-hypoxic conditions. Loss of HIF-2α induces MARCO expression via the antioxidant transcription factor NRF2 (shown by chromatin immunoprecipitation). Inhibition of mitochondrial ROS suppresses MARCO expression and phagocytic uptake. IL-4-induced HIF-2α also suppresses MARCO-dependent phagocytosis in vivo. Hif-2α-/- macrophages, chromatin immunoprecipitation for NRF2, mitochondrial ROS inhibition, phagocytosis assays, IL-4 treatment, in vivo bacterial clearance Journal of immunology Medium 27671111
2017 MARCO mediates rapid adenovirus (HAdV-C5) transduction of macrophages. MARCO-blocking antibodies, MARCO gene-deficient cells, and soluble extracellular SR-A6 domain reduced adenovirus binding and transduction. MARCO-mediated adenovirus infection contributes to efficient innate virus recognition through the cytoplasmic DNA sensor cGAS, leading to IL-6, type I IFN, and IL-1α production. MARCO gene-deficient cells, MARCO-transfected cells, anti-MARCO blocking antibodies, soluble MARCO domain, cGAS pathway assays, cytokine measurement mBio High 28765216
2017 Akt and Nrf2 regulate MARCO expression in alveolar macrophages. Activation of Nrf2 (sulforaphane) or Akt (SC79) increases MARCO expression and improves MARCO-dependent phagocytosis. Akt increases MARCO expression through TFEB (transcription factor E-box); Akt-mediated MARCO increase was abrogated in TFEB-knockdown cells. RNAseq, pharmacological Nrf2/Akt activators, TFEB overexpression and knockdown, phagocytosis assays in IFN-γ-treated macrophages, in vivo mouse model American journal of physiology. Lung cellular and molecular physiology Medium 28408365
2017 Free extracellular actin inhibits MARCO-dependent bacterial binding and uptake by macrophages. Actin binding was reduced in MARCO/SR-AI/II-deficient cell line and in MARCO-/- alveolar macrophages. Scavenger receptor inhibitors reduced binding of fluorescent actin, indicating actin binds to MARCO/SR-A. MARCO/SR-AI/II-deficient cell line, MARCO-/- mouse AMs, SR inhibitor competition assays, bacterial phagocytosis with free actin, Western blot for actin in BAL American journal of physiology. Lung cellular and molecular physiology Medium 28385809
2018 SR-A6 (MARCO) is an entry receptor for human adenovirus type C5 (HAdV-C5) in murine alveolar macrophage-like MPI cells. Knockout of SR-A6 reduced HAdV-C5 binding and transduction; expression of murine SR-A6 boosted virion binding and transduction in human cells. Deletion of the negatively charged hypervariable region 1 (HVR1) of hexon reduced HAdV-C5 binding, identifying hexon as the viral ligand for SR-A6. SR-A6 also facilitates macrophage entry of HAdV-B35 and HAdV-D26. SR-A6 KO cells, SR-A6 overexpression, soluble extracellular SR-A6 domain, proximity localization, hexon HVR1 deletion mutant, binding and transduction assays PLoS pathogens High 29522575
2019 Multiple alphaviruses (CHIKV, RRV, ONNV) are cleared from murine circulation by MARCO (SR-A6) expressed on liver Kupffer cells. Clearance is independent of natural antibodies or complement factor C3, and strictly dependent on lysine residues at specific positions of the E2 glycoprotein (CHIKV/ONNV E2 K200, RRV E2 K251). Lysine-to-arginine substitutions at these sites allow escape from MARCO-mediated clearance. MARCO-/- mice, complement C3-/- mice, alphavirus E2 mutants (K→R), viremia measurements, Kupffer cell depletion eLife High 31596239
2020 MARCO mediates cellular internalization of exosomes via dynamin-dependent endocytosis and macropinocytosis. Exosome and nanoparticle association was greater in CHO-MARCO cells than controls. Exosomes and nanoparticles co-localized with GFP-MARCO. Inhibitory studies showed actin reorganization and dynamin are required for MARCO-mediated exosome internalization. CHO-K1 MARCO transfection, fluorescence microscopy, GFP-MARCO co-localization, dynamin inhibition (dynasore), actin disruption, quantitative uptake analysis Scientific reports Medium 33311558
2020 PI3K signaling (via PTEN deletion in macrophages) drives a beneficial adipose tissue macrophage (ATM) population characterized by MARCO-dependent lipid uptake and catabolism. Dual MARCO and myeloid PTEN deficiencies prevent lipid-buffering ATM generation, reversing the metabolic benefits. MARCO thus mediates PI3K-driven lipid uptake in adipose tissue macrophages. Macrophage-specific PTEN deletion mice, bone marrow chimeras with additional PTEN copies, dual MARCO/PTEN-KO mice, metabolic phenotyping, ATM characterization Nature metabolism High 33199895
2020 IL-10 enhances phagocytosis and bacterial killing of Acinetobacter baumannii by macrophages by upregulating MARCO expression via STAT3 activation. A. baumannii-induced STAT3 activation was impaired in IL-10-deficient macrophages, and STAT3 is essential for MARCO expression. IL-10-/- mice, recombinant IL-10 treatment, MARCO expression assays, STAT3 inhibition, phagocytosis assays, adoptive macrophage transfer Frontiers in immunology Medium 32153580
2020 Cigarette smoke extract (CSE) decreases MARCO expression by causing proteasomal degradation of the histone acetyltransferase p300. LPS-induced MARCO upregulation is Nrf2-dependent; CSE blocks Nrf2 acetylation by degrading p300, thereby suppressing MARCO expression. Proteasome inhibitors blocked CSE-induced p300 degradation and rescued MARCO expression. siRNA knockdown of Nrf2 and p300, CSE treatment, immunofluorescence, immunoprecipitation, proteasome inhibitors, qRT-PCR, flow cytometry Respirology Medium 32512637
2021 MARCO-expressing lymphatic endothelial cells (LECs) in the draining lymph node rapidly capture arthritogenic alphavirus particles following subcutaneous inoculation, limiting viral spread to the bloodstream. Upon reaching the bloodstream, alphavirus particles are cleared by MARCO-expressing Kupffer cells in the liver. MARCO-/- mice show elevated viremia, higher viral tissue burdens, and more severe disease. MARCO-/- mice, subcutaneous alphavirus inoculation, intravital imaging, LEC identification, Kupffer cell studies, viremia and tissue burden measurements The EMBO journal High 34618370
2021 MARCO directly binds to β5 integrin of tumor (SL4) cells, as shown by Co-IP. MARCO overexpression in macrophages elevated SYK, PI3K, and Rac1 activity, promoted formation of stress fibers and pseudopodia, and enhanced phagocytosis of tumor cells. MARCO knockdown decreased engulfment pseudopodia and inhibited tumor cell phagocytosis. Lentiviral MARCO knockdown/overexpression, Co-IP for β5 integrin interaction, SYK/PI3K/Rac1 activity assays, macrophage morphology analysis, tumor cell phagocytosis assay Experimental cell research Medium 34626585
2021 TLR2 potentiates MARCO-mediated neuroinflammation by directly interacting with the SRCR domain of MARCO. Deletion of the SRCR domain disrupted both the inflammatory response and the TLR2-MARCO interaction. TLR2 knockdown in microglia and mouse substantia nigra decreased MARCO expression. MARCO overexpression/silencing, SRCR domain deletion mutants, TLR2 knockdown, neuroinflammation assays in microglia, in vivo substantia nigra injections, co-immunoprecipitation Molecular neurobiology Medium 34398403
2023 MARCO SRCR domain mediates binding and internalization of CHIKV, ONNV, and RRV in vitro. MARCO SRCR domain shows species-specific effects on CHIKV internalization: SRCR domains from known amplification hosts (e.g., rhesus macaque) fail to promote CHIKV internalization, consistent with inefficient clearance of CHIKV from rhesus macaque circulation in vivo. MARCO expression constructs with SRCR domain mutations/swaps, in vitro virus binding and internalization assays, in vivo rhesus macaque viremia studies Cell reports High 37083332
2023 MARCO suppresses IFN-β secretion from tumor-associated macrophages, reducing antigen presentation, CD8+ T cell infiltration, and function. Mechanistically, MARCO promotes clearance of dying tumor cells by macrophages, reducing tumor-derived cGAMP and ATP accumulation in the tumor microenvironment and inhibiting STING-IFN-β pathway activation mediated by P2X7R in MARCO+ TAMs. Clinical specimens, in vitro macrophage assays, in vivo mouse tumor models, cGAMP/ATP measurement, STING pathway assays, anti-MARCO + anti-PD-L1 combination treatment Cancer letters Medium 38065400
2023 Cancer cells upregulate MARCO on human macrophages via IL-6-induced STAT3 activation and also via sphingosine-1-phosphate receptor (S1PR)-mediated IL-6 and IL-10 expression followed by STAT3 activation. MARCO ligation activates the MEK/ERK/p90RSK/CREB signaling cascade, leading to IL-10 expression and STAT3-dependent PD-L1 upregulation. Human macrophage MARCO expression assays, STAT3 inhibition, S1PR inhibition, MARCO ligation with mAb, MEK/ERK/CREB pathway assays, PD-L1 expression measurement Journal of immunology Medium 37212598
2006 Phage display screening of soluble MARCO revealed that the SRCR domain contains the major ligand-binding site. Surface plasmon resonance showed sMARCO binds LPS and lipoteichoic acid, but with much lower affinity than polyinosinic acid. Hydrophobic peptides (VRWGSFAAWL, RLNWAWWLSY) bound to the SRCR domain. Minor sequence changes in the MARCO SRCR domain can profoundly affect binding of acetylated LDL, identifying the SRCR domain as crucial for AcLDL binding in MARCO. Phage display, surface plasmon resonance, chimeric scavenger receptor binding studies, acetylated LDL binding assays The Journal of biological chemistry High 16524885

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 The scavenger receptor MARCO is required for lung defense against pneumococcal pneumonia and inhaled particles. The Journal of experimental medicine 268 15263032
2009 MARCO, TLR2, and CD14 are required for macrophage cytokine responses to mycobacterial trehalose dimycolate and Mycobacterium tuberculosis. PLoS pathogens 253 19521507
1999 Regulation and functional involvement of macrophage scavenger receptor MARCO in clearance of bacteria in vivo. Journal of immunology (Baltimore, Md. : 1950) 204 9916718
2020 Targeting MARCO and IL37R on Immunosuppressive Macrophages in Lung Cancer Blocks Regulatory T Cells and Supports Cytotoxic Lymphocyte Function. Cancer research 189 33293426
2005 MARCO is the major binding receptor for unopsonized particles and bacteria on human alveolar macrophages. Journal of immunology (Baltimore, Md. : 1950) 170 16237101
1999 Role of the scavenger receptor MARCO in alveolar macrophage binding of unopsonized environmental particles. The Journal of experimental medicine 170 10224290
2000 The macrophage receptor MARCO. Microbes and infection 149 10758408
2006 MARCO mediates silica uptake and toxicity in alveolar macrophages from C57BL/6 mice. The Journal of biological chemistry 140 16984918
1998 Structure of the human macrophage MARCO receptor and characterization of its bacteria-binding region. The Journal of biological chemistry 117 9468508
2007 Protection against inhaled oxidants through scavenging of oxidized lipids by macrophage receptors MARCO and SR-AI/II. The Journal of clinical investigation 105 17332894
2007 A murine scavenger receptor MARCO recognizes polystyrene nanoparticles. Toxicological sciences : an official journal of the Society of Toxicology 97 17361018
2010 SR-A/MARCO-mediated ligand delivery enhances intracellular TLR and NLR function, but ligand scavenging from cell surface limits TLR4 response to pathogens. Blood 96 21098741
2003 The scavenger receptor MARCO mediates cytoskeleton rearrangements in dendritic cells and microglia. Blood 93 12842997
2007 Crystal structure of the cysteine-rich domain of scavenger receptor MARCO reveals the presence of a basic and an acidic cluster that both contribute to ligand recognition. The Journal of biological chemistry 88 17405873
2005 Disparate regulation and function of the class A scavenger receptors SR-AI/II and MARCO. Journal of immunology (Baltimore, Md. : 1950) 85 16339540
2018 Expression of scavenger receptor MARCO defines a targetable tumor-associated macrophage subset in non-small cell lung cancer. International journal of cancer 81 29667169
2009 Critical role of MARCO in crystalline silica-induced pulmonary inflammation. Toxicological sciences : an official journal of the Society of Toxicology 79 19151164
2006 MARCO, an innate activation marker of macrophages, is a class A scavenger receptor for Neisseria meningitidis. European journal of immunology 72 16525990
2023 Long-Chain Acyl Carnitines Aggravate Polystyrene Nanoplastics-Induced Atherosclerosis by Upregulating MARCO. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 71 37144527
2012 MARCO is required for TLR2- and Nod2-mediated responses to Streptococcus pneumoniae and clearance of pneumococcal colonization in the murine nasopharynx. Journal of immunology (Baltimore, Md. : 1950) 70 23197261
2017 Key Role of the Scavenger Receptor MARCO in Mediating Adenovirus Infection and Subsequent Innate Responses of Macrophages. mBio 69 28765216
2018 Lung macrophage scavenger receptor SR-A6 (MARCO) is an adenovirus type-specific virus entry receptor. PLoS pathogens 64 29522575
2010 Functional and physical interactions between formyl-peptide-receptors and scavenger receptor MARCO and their involvement in amyloid beta 1-42-induced signal transduction in glial cells. Journal of neurochemistry 64 20141570
2005 Defective microarchitecture of the spleen marginal zone and impaired response to a thymus-independent type 2 antigen in mice lacking scavenger receptors MARCO and SR-A. Journal of immunology (Baltimore, Md. : 1950) 62 16339556
2002 Characterization of recombinant soluble macrophage scavenger receptor MARCO. The Journal of biological chemistry 62 12097327
2008 Differential binding of inorganic particles to MARCO. Toxicological sciences : an official journal of the Society of Toxicology 61 18836211
2002 Arginine residues in domain V have a central role for bacteria-binding activity of macrophage scavenger receptor MARCO. Biochemical and biophysical research communications 60 11820786
2011 MARCO regulates early inflammatory responses against influenza: a useful macrophage function with adverse outcome. American journal of respiratory cell and molecular biology 58 21562316
2007 Scavenger Receptors SR-AI/II and MARCO limit pulmonary dendritic cell migration and allergic airway inflammation. Journal of immunology (Baltimore, Md. : 1950) 56 17442975
2020 Scavenger receptor MARCO contributes to cellular internalization of exosomes by dynamin-dependent endocytosis and macropinocytosis. Scientific reports 54 33311558
2006 Role of scavenger receptor MARCO in macrophage responses to CpG oligodeoxynucleotides. Journal of leukocyte biology 53 16882874
1999 Roles of a macrophage receptor with collagenous structure (MARCO) in host defense and heterogeneity of splenic marginal zone macrophages. Archives of histology and cytology 50 10223745
2009 A defect in Marco expression contributes to systemic lupus erythematosus development via failure to clear apoptotic cells. Journal of immunology (Baltimore, Md. : 1950) 49 19201851
2023 Blocking MARCO+ tumor-associated macrophages improves anti-PD-L1 therapy of hepatocellular carcinoma by promoting the activation of STING-IFN type I pathway. Cancer letters 45 38065400
2013 HSV-1 exploits the innate immune scavenger receptor MARCO to enhance epithelial adsorption and infection. Nature communications 44 23739639
2009 Pivotal Advance: Expansion of small sputum macrophages in CF: failure to express MARCO and mannose receptors. Journal of leukocyte biology 44 19403625
2021 Scavenger receptor MARCO contributes to macrophage phagocytosis and clearance of tumor cells. Experimental cell research 43 34626585
1999 Expression of macrophage MARCO receptor induces formation of dendritic plasma membrane processes. The Journal of biological chemistry 42 10196178
2016 MARCO variants are associated with phagocytosis, pulmonary tuberculosis susceptibility and Beijing lineage. Genes and immunity 40 27853145
2020 IL-10 Protects Mice From the Lung Infection of Acinetobacter baumannii and Contributes to Bacterial Clearance by Regulating STAT3-Mediated MARCO Expression in Macrophages. Frontiers in immunology 39 32153580
2014 Vaccinia virus binds to the scavenger receptor MARCO on the surface of keratinocytes. The Journal of investigative dermatology 39 25089661
2003 Inducible expression of macrophage receptor Marco by dendritic cells following phagocytic uptake of dead cells uncovered by oligonucleotide arrays. Journal of immunology (Baltimore, Md. : 1950) 39 12960310
2014 Role of lysosomes in silica-induced inflammasome activation and inflammation in absence of MARCO. Journal of immunology research 38 25054161
2011 The formyl peptide receptor like-1 and scavenger receptor MARCO are involved in glial cell activation in bacterial meningitis. Journal of neuroinflammation 38 21299846
2014 Phagocytosis of mycobacteria by zebrafish macrophages is dependent on the scavenger receptor Marco, a key control factor of pro-inflammatory signalling. Developmental and comparative immunology 37 25086293
2014 The scavenger receptor MARCO modulates TLR-induced responses in dendritic cells. PloS one 37 25089703
2000 Molecular characterization of a human scavenger receptor, human MARCO. European journal of biochemistry 37 10651831
2017 Scavenger Receptor MARCO Orchestrates Early Defenses and Contributes to Fungal Containment during Cryptococcal Infection. Journal of immunology (Baltimore, Md. : 1950) 36 28298522
2004 Induction of macrophage scavenger receptor MARCO in nonalcoholic steatohepatitis indicates possible involvement of endotoxin in its pathogenic process. International journal of experimental pathology 36 15566430
2008 SR-A, MARCO and TLRs differentially recognise selected surface proteins from Neisseria meningitidis: an example of fine specificity in microbial ligand recognition by innate immune receptors. Journal of innate immunity 35 20375573
2018 Inhibition of MARCO ameliorates silica-induced pulmonary fibrosis by regulating epithelial-mesenchymal transition. Toxicology letters 34 30391304
2019 Discrete viral E2 lysine residues and scavenger receptor MARCO are required for clearance of circulating alphaviruses. eLife 33 31596239
2017 Immunomodulators targeting MARCO expression improve resistance to postinfluenza bacterial pneumonia. American journal of physiology. Lung cellular and molecular physiology 33 28408365
2020 The PI3K pathway preserves metabolic health through MARCO-dependent lipid uptake by adipose tissue macrophages. Nature metabolism 32 33199895
2021 MARCO+ lymphatic endothelial cells sequester arthritogenic alphaviruses to limit viremia and viral dissemination. The EMBO journal 31 34618370
2010 Targeting MARCO can lead to enhanced dendritic cell motility and anti-melanoma activity. Cancer immunology, immunotherapy : CII 31 20054688
2008 Cigarette smoke decreases MARCO expression in macrophages: implication in Mycoplasma pneumoniae infection. Respiratory medicine 31 18590957
2002 Protein structure and the spandrels of San Marco: insulin's receptor-binding surface is buttressed by an invariant leucine essential for its stability. Biochemistry 31 11790102
2013 Genetic variants of MARCO are associated with susceptibility to pulmonary tuberculosis in a Gambian population. BMC medical genetics 30 23617307
2016 HIF-2α in Resting Macrophages Tempers Mitochondrial Reactive Oxygen Species To Selectively Repress MARCO-Dependent Phagocytosis. Journal of immunology (Baltimore, Md. : 1950) 29 27671111
2011 Macrophage receptor with collagenous structure (MARCO) is a dynamic adhesive molecule that enhances uptake of carbon nanotubes by CHO-K1 cells. Toxicology and applied pharmacology 29 22209804
2016 A naturally occurring transcript variant of MARCO reveals the SRCR domain is critical for function. Immunology and cell biology 26 26888252
2006 A phage display screen and binding studies with acetylated low density lipoprotein provide evidence for the importance of the scavenger receptor cysteine-rich (SRCR) domain in the ligand-binding function of MARCO. The Journal of biological chemistry 25 16524885
1997 Mitochondrial antisense RNA for cytochrome C oxidase (MARCO) can induce morphologic changes and cell death in human hematopoietic cell lines. Blood 25 9373268
2022 Superenhancer drives a tumor-specific splicing variant of MARCO to promote triple-negative breast cancer progression. Proceedings of the National Academy of Sciences of the United States of America 24 36343244
2014 Identification of SCARA3, SCARA5 and MARCO of class A scavenger receptor-like family in Pseudosciaena crocea. Fish & shellfish immunology 24 25218683
2011 Genetic variants in MARCO are associated with the susceptibility to pulmonary tuberculosis in Chinese Han population. PloS one 24 21886847
2008 Characterization of immortalized MARCO and SR-AI/II-deficient murine alveolar macrophage cell lines. Particle and fibre toxicology 24 18452625
2022 PLG nanoparticles target fibroblasts and MARCO+ monocytes to reverse multiorgan fibrosis. JCI insight 23 35104243
2016 Determinants of host susceptibility to murine respiratory syncytial virus (RSV) disease identify a role for the innate immunity scavenger receptor MARCO gene in human infants. EBioMedicine 23 27554839
2011 Surface lipoprotein PpiA of Streptococcus mutans suppresses scavenger receptor MARCO-dependent phagocytosis by macrophages. Infection and immunity 23 21986627
2014 Is the scavenger receptor MARCO a new immune checkpoint? Oncoimmunology 22 25941575
2018 Role of a macrophage receptor with collagenous structure (MARCO) in regulating monocyte/macrophage functions in ayu, Plecoglossus altivelis. Fish & shellfish immunology 21 29305330
2017 Draft genome of the Marco Polo Sheep (Ovis ammon polii). GigaScience 21 29112761
2012 The Silk Road, Marco Polo, a Bible and its proteome: a detective story. Journal of proteomics 21 22504796
1999 Structure and chromosomal localization of the human and murine genes for the macrophage MARCO receptor. Genomics 20 10331948
2024 The application of MARCO for immune regulation and treatment. Molecular biology reports 18 38300385
2023 UGRP1-modulated MARCO+ alveolar macrophages contribute to age-related lung fibrosis. Immunity & ageing : I & A 18 36934284
2019 Therapeutic effects of scavenger receptor MARCO ligand on silica-induced pulmonary fibrosis in rats. Toxicology letters 17 31028789
2009 The scavenger receptor MARCO is involved in Leishmania major infection by CBA/J macrophages. Parasite immunology 17 19292770
2023 Species-specific MARCO-alphavirus interactions dictate chikungunya virus viremia. Cell reports 16 37083332
2023 Cancer Cells Promote Immune Regulatory Function of Macrophages by Upregulating Scavenger Receptor MARCO Expression. Journal of immunology (Baltimore, Md. : 1950) 16 37212598
2021 MARCO+ Macrophage Dynamics in Regenerating Liver after 70% Liver Resection in Mice. Biomedicines 16 34572315
2017 Free actin impairs macrophage bacterial defenses via scavenger receptor MARCO interaction with reversal by plasma gelsolin. American journal of physiology. Lung cellular and molecular physiology 16 28385809
2017 Evaluation of the relationship between MARCO and CD36 single-nucleotide polymorphisms and susceptibility to pulmonary tuberculosis in a Chinese Han population. BMC infectious diseases 16 28693442
2024 Modulating tumor-associated macrophage polarization by anti-maRCO mAb exerts anti-osteosarcoma effects through regulating osteosarcoma cell proliferation, migration and apoptosis. Journal of orthopaedic surgery and research 15 39085912
2021 TLR2 Potentiates SR-Marco-Mediated Neuroinflammation by Interacting with the SRCR Domain. Molecular neurobiology 15 34398403
2020 Binding of Macrophage Receptor MARCO, LDL, and LDLR to Disease-Associated Crystalline Structures. Frontiers in immunology 15 33363539
2004 The structure and function of marco, a macrophage class a scavenger receptor. Cellular and molecular biology (Noisy-le-Grand, France) 15 15588554
2019 Age-dependent effect between MARCO and TLR4 on PMMA particle phagocytosis by macrophages. Journal of cellular and molecular medicine 14 31225947
2015 Macrophage Receptor with Collagenous Structure (MARCO) Is Processed by either Macropinocytosis or Endocytosis-Autophagy Pathway. PloS one 14 26545255
2013 Examination of MARCO activity on dendritic cell phenotype and function using a gene knockout mouse. PloS one 14 23840879
2005 Increased expression of macrophage receptor with collagenous structure (MARCO) in mouse cortex following middle cerebral artery occlusion. Neuroscience letters 14 15936512
2023 Colorectal cancer-derived extracellular vesicles containing HSP70 enhance macrophage phagocytosis by up-regulating MARCO expression. Experimental cell research 13 36958650
2023 MARCO Inhibits Porcine Reproductive and Respiratory Syndrome Virus Infection through Intensifying Viral GP5-Induced Apoptosis. Microbiology spectrum 13 37078873
2010 MARCO, a macrophage scavenger receptor highly expressed in rodents, mediates dalcetrapib-induced uptake of lipids by rat and mouse macrophages. Toxicology in vitro : an international journal published in association with BIBRA 13 20074633
2006 Species-specific restriction of cell surface expression of mouse MARCO glycoprotein in murine cell lines. Biochemical and biophysical research communications 12 16460688
2020 Cigarette smoke extract decreased basal and lipopolysaccharide-induced expression of MARCO via degradation of p300. Respirology (Carlton, Vic.) 11 32512637
2018 Human-Specific Mutations and Positively Selected Sites in MARCO Confer Functional Changes. Molecular biology and evolution 11 29165618
2017 Scavengers for bacteria: Rainbow trout have two functional variants of MARCO that bind to gram-negative and -positive bacteria. Developmental and comparative immunology 11 28743433

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