| 2000 |
SLAMF1 (SLAM/CD150) functions as a cellular receptor for measles virus, including wild-type clinical isolates and the Edmonston strain; transfection of human SLAM cDNA into non-susceptible cell lines confers measles virus binding, replication, and cytopathic effects. |
Transfection of human SLAM cDNA into non-susceptible cell lines followed by virus binding assay and replication assay |
Nature |
High |
10972291
|
| 2001 |
CD150 associates with SH2-containing inositol phosphatase (SHIP) or SH2-containing protein tyrosine phosphatase (SHP-2) via phosphorylated tyrosines Y281 and Y327 in its cytoplasmic tail; the adaptor SH2D1A (SAP) regulates this association by facilitating SHIP binding and blocking SHP-2 binding, acting through a TxYxxV/I immunoreceptor tyrosine-based switch motif (ITSM). |
Co-immunoprecipitation, GST-fusion protein pulldown with tyrosine-to-phenylalanine mutants (Y269F, Y281F, Y307F, Y327F) |
Journal of immunology |
High |
11313386
|
| 2001 |
CDw150/SLAM is an expression-cloned receptor for lymphotropic measles virus strains; both lymphotropic and laboratory measles virus strains bind human and marmoset CDw150 but show weak interaction with mouse CDw150; infection via CDw150 is independent of CD46. |
Expression cloning from B95-8 cDNA library, binding assay with soluble MV H protein, infection of CDw150-transfected CHO and HEK293T cells |
Virology |
High |
11145884
|
| 2001 |
Measles virus hemagglutinin (H) protein, but not the fusion protein, is sufficient to downregulate SLAM (CD150) from the cell surface; downregulation can occur through intracellular interactions between H and SLAM in the ER, and also through receptor-mediated binding at the cell surface. |
Transfection of H protein expression plasmid, confocal microscopy, flow cytometry for surface SLAM levels |
Archives of virology |
Medium |
11855632
|
| 2002 |
CD150 co-localizes with the TCR following CD3 triggering and is rapidly and reversibly tyrosine-phosphorylated upon TCR cross-linking; Src-like kinases Lck and Fyn phosphorylate tyrosine residues in the cytoplasmic tail of CD150. SAP binds CD150 via two distinct modes: phosphotyrosine-independent binding to Thr-Ile-Y281-Ala-Gln-Val and phosphotyrosine-dependent binding to Thr-Val-Y327-Ala-Ser-Val; a leucine residue L278 further stabilizes non-phospho binding at Y281. SAP blocks SHP-2 binding primarily at Y281. |
Confocal microscopy (co-localization), in vitro kinase assay, co-immunoprecipitation, site-directed mutagenesis |
Blood |
High |
11806999
|
| 2002 |
SLAM (CD150) is a cellular receptor common to all 28 measles virus strains tested; a single amino acid exchange in the hemagglutinin at position 481 (Asn/Tyr, H481NY) determines whether virus can additionally utilize CD46, demonstrating that the binding sites for SLAM and CD46 on hemagglutinin are distinct. |
Infection of CHO cells expressing recombinant CD46 or SLAM with a panel of MV strains; recombinant virus with site-directed mutations |
The Journal of general virology |
High |
12029158
|
| 2002 |
Measles virus can infect SLAM-negative cells at 2–3 log lower efficiency through an unidentified receptor distinct from both SLAM and CD46; this entry is blocked by anti-MV hemagglutinin antibody or fusion block peptide but not by anti-CD46 antibody, and occurs under conditions that inhibit endocytosis. |
Recombinant EGFP-expressing MV infection of SLAM-negative cell lines, antibody blocking assays, endocytosis inhibition |
Journal of virology |
Medium |
12050387
|
| 2004 |
SLAMF1 (SLAM) knockout macrophages show defective production of IL-12, TNF, and nitric oxide in response to LPS but normal phagocytosis and normal responses to peptidoglycan or CpG; SLAM acts as a co-receptor regulating signals downstream of TLR4. SLAM-deficient CD4+ T cells show reduced TCR-induced IL-4 secretion with only slight upregulation of IFN-γ. SLAM-/- C57Bl/6 mice fail to clear Leishmania major due to defective macrophage function. |
Targeted gene knockout, in vitro cytokine assays, in vivo infection model (Leishmania major) |
The Journal of experimental medicine |
High |
15123745
|
| 2004 |
SAP is required for phosphorylation of SLAM in thymocytes and peripheral T cells; SAP binds directly to both the SH3 domain and kinase domain of FynT, and addition of SAP to autoinhibited FynT causes a large increase in FynT catalytic activity; a SAP mutant (R78E) that cannot bind FynT SH3 domain neither activates FynT nor functions as an adaptor in T cells. |
In vitro kinase assay, yeast two-hybrid, GST pulldown, transfection with mutant constructs |
International immunology |
High |
15096483
|
| 2004 |
Measles virus hemagglutinin (H) protein interacts with SLAM in the endoplasmic reticulum, promoting SLAM downregulation from the host cell surface; surface interactions between H and SLAM also contribute. H expression alone is sufficient for this downregulation. |
Plasmid transfection, co-culture experiments, flow cytometry, ER co-localization studies |
Journal of virology |
Medium |
15331699
|
| 2005 |
SLAM (CD150) V domain is necessary and sufficient for measles virus receptor function; murine SLAM differs from human SLAM in receptor function due to residues at positions 60, 61, and 63, with histidine 61 being most critical; exchange of the region at amino acids 58–67 allows mouse SLAM to function as an MV receptor. |
Human/mouse chimeric SLAM constructs assessed by VSV pseudotype assay with site-directed mutagenesis |
The Journal of general virology |
High |
12917459
|
| 2007 |
Homotypic interactions mediated by SLAMF1 and SLAMF6 (Ly108) on cortical thymocytes generate co-stimulatory signals during NKT cell selection; these signals involve downstream recruitment of SAP and Fyn kinase and are required for NKT lineage expansion and differentiation. These interactions only occur when selecting ligands (CD1d) are presented by thymocytes, not by epithelial cells, which do not express Slamf1/Slamf6. |
Genetic knockout models, epistasis analysis, in vivo NKT development assays |
Immunity |
High |
18031695
|
| 2008 |
Measles virus hemagglutinin residue isoleucine 194 is essential for primary SLAM binding (as measured by surface plasmon resonance); a quartet of residues on propeller blade 5 is required for SLAM-dependent membrane fusion after binding but not for initial binding, indicating receptor-specific conformational changes post-binding trigger fusion protein unfolding. |
Surface plasmon resonance, receptor-specific fusion assays, crystal structure localization, site-directed mutagenesis |
The Journal of biological chemistry |
High |
18292085
|
| 2010 |
SLAMF1 (CD150) signaling via SAP is specifically required for IL-4 production by germinal center T follicular helper (GC TFH) cells; SAP-deficient TFH cells lack GC TFH cells and are defective in IL-4 and IL-21 production; SLAM receptor ligation is required for this IL-4 production but not for TFH or GC TFH cell differentiation. |
SAP-deficient and SLAM-deficient mouse models, in vivo immunization, FACS-based identification of GC TFH cells, intracellular cytokine staining |
Journal of immunology |
High |
20525889
|
| 2012 |
In E. coli-containing phagosomes of macrophages, SLAMF1 recruits a Beclin-1/Vps34/UVRAG protein complex; this complex regulates NOX2 (NADPH oxidase 2) activity and phagolysosomal maturation. The interaction requires the cytoplasmic tail of Slamf1 but not its ITAM motifs. Beclin-1 BD and CCD domains are required for binding to Slamf1. Slamf1 does not interact with Atg14L or Rubicon. |
Co-immunoprecipitation, in vitro pulldown, NOX2 activity assay in Beclin-1+/- macrophages, domain deletion mutagenesis, transfected HEK293 cells |
The Journal of biological chemistry |
High |
22493499
|
| 2012 |
In the absence of SAP, SLAM family receptors Ly108 and 2B4 recruit increased levels of SHP-1 phosphatase, causing altered SHP-1 localization and decreased Src kinase activation at the immunological synapse. SAP-deficient CD8+ T cells show specific defects in synapse organization with B cell and low-avidity T cell targets (inefficient actin clearance), resulting in impaired cytotoxicity against these targets but not fibrosarcoma targets. |
SAP-deficient mouse T cells, immunological synapse imaging, phosphatase recruitment assay, cytotoxicity assays |
Immunity |
High |
22683123
|
| 2015 |
SLAMF1 ligation with an agonistic antibody induces ROS accumulation, phosphorylation of p38, JNK1/2, and BCL2, and promotes autophagic flux in CLL cells. Beclin-1 dissociates from BCL2 upon SLAMF1 ligation, forming an autophagy macrocomplex containing SLAMF1, beclin-1, and VPS34. SLAMF1 silencing in CLL cells increases CXCR4, CD38, and CD44 expression and enhances chemotactic responses to CXCL12; SLAMF1-low cells are resistant to autophagy-activating agents. |
SLAMF1 siRNA knockdown, agonistic antibody ligation, co-immunoprecipitation (SLAMF1/beclin-1/VPS34 complex), ROS assay, autophagic flux assay, transwell chemotaxis assay |
The Journal of clinical investigation |
High |
26619119
|
| 2015 |
SLAMF1 and SLAMF8 oppositely regulate in vivo migration of myeloid cells during inflammation: Slamf1-/- dendritic cells and macrophages show reduced migration in vivo and in vitro, whereas Slamf8-/- cells show accelerated migration. These effects are cell-intrinsic. Inhibition of ROS production in Slamf8-/- macrophages blocks their enhanced migration, linking SLAMF1/SLAMF8-mediated ROS regulation to myeloid cell migration. |
Slamf1-/- and Slamf8-/- mouse models, in vivo migration assays (skin sensitization, peritonitis, intestinal repopulation), transwell migration assay, ROS inhibitor (DPI) |
PloS one |
Medium |
25799045
|
| 2017 |
SLAMF1 engagement by measles virus (MeV) induces macropinocytosis-like endocytic uptake of viral particles dependent on actin cytoskeletal rearrangement, membrane blebbing, and the RhoA-ROCK-myosin II signaling axis; this endocytic entry pathway is specific to SLAMF1-positive cells and occurs within 60 minutes of viral attachment. |
Live-cell imaging of viral particle colocalization with blebs, chemical inhibition of macropinocytosis/actin dynamics/ROCK-myosin II, infection assay in SLAMF1+ vs SLAMF1- cells |
Journal of virology |
Medium |
28100610
|
| 2018 |
SLAMF1 is required for TLR4-mediated TRAM-TRIF-dependent signaling (IFNβ induction) and killing of Gram-negative bacteria by human macrophages. In resting macrophages, SLAMF1 localizes to the endocytic recycling compartment (ERC) and is trafficked together with TRAM to E. coli phagosomes in a Rab11-dependent manner upon bacterial stimulation. Endogenous SLAMF1 interacts with TRAM via amino acids 68–95 of TRAM and the 15 C-terminal amino acids of SLAMF1; this interaction is observed for human but not mouse proteins. |
SLAMF1 knockdown/knockout in human macrophages, co-immunoprecipitation (SLAMF1-TRAM), confocal microscopy of ERC-to-phagosome trafficking, domain deletion constructs, IFNβ induction assay, bacterial killing assay |
The Journal of cell biology |
High |
29440514
|
| 2019 |
SLAM family receptors (SFRs), including SLAMF1, promote iNKT cell development by reducing TCR signal strength after positive selection; SFR deficiency upregulates inhibitory receptors (PD-1) to partially compensate; SLAMF6 alone can mimic SFR function and this involves the SAP-Fyn complex and phosphatase SHP-1. |
SFR-deficient mouse models, SLAMF6 single-receptor rescue experiments, epistasis with SAP/Fyn/SHP-1, iNKT cell development quantification, TCR signal strength assays |
Nature immunology |
High |
30833791
|
| 2020 |
Brucella abortus outer membrane protein Omp25 specifically binds SLAMF1 in vitro; Omp25-dependent SLAMF1 engagement limits NF-κB translocation in dendritic cells, decreases pro-inflammatory cytokine secretion, impairs DC activation, and promotes bacterial persistence at the chronic stage of infection in vivo. |
In vitro binding assay (Omp25-SLAMF1), NF-κB translocation assay, cytokine measurement, mouse infection model |
Cellular microbiology |
Medium |
31953913
|
| 2020 |
Human neutrophils upregulate SLAMF1 expression upon Mycobacterium tuberculosis (Mtb) stimulation; SLAMF1 co-localizes with LC3B+ vesicles, and SLAMF1 activation increases neutrophil autophagy induced by Mtb; tuberculosis patients' neutrophils show reduced SLAMF1 levels and lower autophagy. |
Flow cytometry for SLAMF1 expression, confocal microscopy (SLAMF1/LC3B co-localization), SLAMF1 agonistic antibody activation, autophagy flux assay |
Autophagy |
Medium |
32954947
|
| 1993 |
IPO-3 (later identified as CD150/SLAMF1) is a novel heavily N-glycosylated phosphoglycoprotein (~75-95 kDa, 42 kDa protein core) expressed on activated B cells and some T cells; it has an associated protein kinase activity maintained in detergent lysates; cross-linking IPO-3 on B cells triggers increases in intracellular Ca2+ and augments IL-4/anti-CD40-driven proliferation. |
Monoclonal antibody characterization, in vitro kinase assay, calcium flux assay, proliferation assay |
Journal of immunology |
Medium |
8409422
|
| 2002 |
CD150 (SLAMF1)-mediated T cell DNA synthesis (proliferation) induced by anti-CD150 antibody does not depend on SAP/SH2D1A, as similar levels are observed in SAP-/- T cells; however, SAP-/- T cells show higher IFN-γ production than WT upon anti-CD150 stimulation. Anti-CD150 cross-linking on CD4 T cells induces rapid serine phosphorylation of Akt/PKB. |
SAP-/- mouse T cells, anti-CD150 antibody stimulation, DNA synthesis assay, IFN-γ ELISA, Akt phosphorylation assay |
Blood |
Medium |
12351401
|
| 2004 |
CD150 (SLAMF1)-induced ERK pathway activation in B cells requires SHIP but not SH2D1A (SAP); CD150-mediated Akt phosphorylation requires Syk and SH2D1A and is negatively regulated by Lyn and Btk; Lyn directly phosphorylates Y327 in CD150; the Akt pathway does not depend on CD150 tyrosine phosphorylation or CD150-SHP-2 association. |
DT40 B-cell sublines deficient in SHIP, SAP, Syk, Lyn, or Btk; CD150 ligation, Western blotting for ERK/Akt phosphorylation |
Blood |
High |
15315965
|
| 2001 |
SLAM (CD150) is downregulated from the surface of activated peripheral blood lymphocytes and cell lines after measles virus infection or surface contact with MV envelope proteins; blocking SLAM or CD46 prevents virus binding but does not interfere with contact-mediated proliferation inhibition, indicating these are separable functions. |
Flow cytometry for SLAM surface expression, antibody blocking assays, proliferation assays |
Journal of virology |
Medium |
11312320
|
| 2001 |
SLAM (CD150) is inducible on monocytes (which are SLAM-negative at rest) after stimulation with PHA, LPS, or MV; anti-SLAM monoclonal antibodies efficiently block MV infection of activated monocytes with a wild-type strain. |
Flow cytometry for SLAM induction on monocytes, blocking antibody assay for MV infection |
The Journal of general virology |
Medium |
11714966
|
| 2006 |
CDV unable to recognize SLAM (CD150) does not spread in ferrets, formally proving that SLAM recognition is necessary for morbillivirus virulence and for lymphocyte-based dissemination into mucosal tissue and lymphatic organs. |
Recombinant CDV with receptor-ablating mutations in ferret infection model, GFP-reporter virus tracking |
Journal of virology |
High |
16731947
|
| 2010 |
A recombinant measles virus with a single R533A substitution in hemagglutinin that is selectively unable to recognize SLAM (SLAM-blind) infects primary lymphocytes at low levels regardless of SLAM expression and causes no viremia or clinical symptoms in rhesus monkeys, formally proving that efficient SLAM recognition is necessary for MV virulence and pathogenesis. |
Site-directed mutagenesis of MV hemagglutinin, ex vivo lymphocyte infection assay, rhesus monkey intranasally inoculation model |
Journal of virology |
High |
20071568
|
| 2001 |
SLAM (CD150) augments TCR-mediated cytotoxicity in both CD4+ and CD8+ T cells; SLAM engagement alone triggers cytotoxicity in herpesvirus saimiri-transformed T cells via lytic granule release, requiring extracellular Ca2+, cytoskeletal rearrangements, and MEK1/2 signaling, independent of CD95. |
Antibody crosslinking of SLAM on primary and transformed T cells, cytotoxicity assay, pharmacological inhibitors (MEK1/2, cytoskeletal), Ca2+ chelation |
European journal of immunology |
Medium |
11536173
|
| 2012 |
Slamf1-/- mice are completely protected from acute lethal Trypanosoma cruzi challenge; Slamf1-deficient myeloid cells are impaired in intracellular T. cruzi replication and show altered cytokine production; IFN-γ production is reduced in the heart of Slamf1-/- mice despite comparable immune cell infiltration. |
Slamf1-/- mouse infection model, in vitro parasite replication assay in myeloid cells, cytokine measurement, anti-Slamf1 monoclonal antibody treatment |
PLoS pathogens |
Medium |
22807679
|