| Structural highlights
Function
SSL10_STAA8 Plays a role in the inhibition of host complement activation via the classical pathway by interacting with the Fc region of human IgG and thereby interfering with the IgG/C1q interaction (PubMed:19913916). Inhibits also the penultimate step of plasma clotting by interacting with prothrombin/F2 and coagulation factor X/F12. Does not affect the protease activity of thrombin but interferes with the conversion of prothrombin to thrombin (PubMed:23754290, PubMed:28193526). Interacts with human receptor CXCR4 and specifically inhibits CXCL12-induced calcium mobilization and cell migration (PubMed:19308288).[1] [2] [3] [4]
References
- ↑ Walenkamp AM, Boer IG, Bestebroer J, Rozeveld D, Timmer-Bosscha H, Hemrika W, van Strijp JA, de Haas CJ. Staphylococcal superantigen-like 10 inhibits CXCL12-induced human tumor cell migration. Neoplasia. 2009 Apr;11(4):333-44. PMID:19308288 doi:10.1593/neo.81508
- ↑ Itoh S, Hamada E, Kamoshida G, Yokoyama R, Takii T, Onozaki K, Tsuji T. Staphylococcal superantigen-like protein 10 (SSL10) binds to human immunoglobulin G (IgG) and inhibits complement activation via the classical pathway. Mol Immunol. 2010 Jan;47(4):932-8. PMID:19913916 doi:10.1016/j.molimm.2009.09.027
- ↑ Itoh S, Yokoyama R, Kamoshida G, Fujiwara T, Okada H, Takii T, Tsuji T, Fujii S, Hashizume H, Onozaki K. Staphylococcal superantigen-like protein 10 (SSL10) inhibits blood coagulation by binding to prothrombin and factor Xa via their γ-carboxyglutamic acid (Gla) domain. J Biol Chem. 2013 Jul 26;288(30):21569-80. PMID:23754290 doi:10.1074/jbc.M113.451419
- ↑ Itoh S, Takii T, Onozaki K, Tsuji T, Hida S. Identification of the blood coagulation factor interacting sequences in staphylococcal superantigen-like protein 10. Biochem Biophys Res Commun. 2017 Mar 25;485(1):201-208. PMID:28193526 doi:10.1016/j.bbrc.2017.02.053
|
