Extracellular adherence protein (Eap) from Staphylococcus aureus does not function as a superantigen.
Extracellular adherence protein (Eap) from Staphylococcus aureus has been reported to have strong anti-inflammatory properties, which make Eap a potential anti-inflammatory agent. However, Eap has also been demonstrated to trigger T-cell activation and to share structural homology with superantigens. In this study, we focused on whether Eap fulfilled the definition criteria for a superantigen. We demonstrate that T-cell activation by Eap is dependent on both major histocompatibility complex class II and intercellular adhesion molecule type 1, that cellular processing is required for Eap to elicit T-cell proliferation, and that the kinetics of proliferation resemble the profile of a conventional antigen and not that of a superantigen.
Haggar
A
A
Centre for Infectious Medicine, Karolinska Institutet, Karolinska University Hospital Huddinge, Stockholm, Sweden. axana.haggar@ki.se
Flock
J-I
JI
Norrby-Teglund
A
A
D001426:Bacterial Proteins / Q000276:immunology*; D049109:Cell Proliferation; D000949:Histocompatibility Antigens Class II / Q000276:immunology; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000276:immunology; D008213:Lymphocyte Activation / Q000187:drug effects; D016601:RNA-Binding Proteins / Q000276:immunology*; D013211:Staphylococcus aureus / Q000276:immunology* / Q000472:pathogenicity*; D018089:Superantigens / Q000276:immunology*; D013601:T-Lymphocytes / Q000187:drug effects / Q000276:immunology; D037521:Virulence Factors / Q000276:immunology*
D001426:Bacterial Proteins; C444739:Eap-N protein, Staphylococcus aureus; D000949:Histocompatibility Antigens Class II; D016601:RNA-Binding Proteins; D018089:Superantigens; D037521:Virulence Factors; D018799:Intercellular Adhesion Molecule-1