Analyses of the complex formation of staphylococcal enterotoxin A and the human gp130 cytokine receptor

FEBS Letters

article

Sibel Uzunçayır¹  Arturo Vera-Rodriguez²  Paulina Regenthal¹  Hannah Åbacka¹  Cecilia Emanuelsson⁴  Christopher D. Bahl²  Karin Lindkvist-Petersson¹ 

[1] Department of Experimental Medical Science, Lund University;Institute for Protein Innovation;Division of Hematology-Oncology, Boston Children’s Hospital, Harvard Medical School;Department of Chemistry, Division for Biochemistry and Structural Biology, Lund University;LINXS – Lund Institute of Advanced Neutron and X-ray Science

关键词: food poisoning;    gp130;    SEA;    SPR;    superantigen;   

DOI  :  10.1002/1873-3468.14292

来源: John Wiley & Sons Ltd.

【 摘 要 】

Superantigens (SAgs) are bacterial enterotoxins produced by Staphylococcus aureus . Staphylococcal enterotoxin type A (SEA), a staphylococcal superantigen, has been shown to bind to the cytokine signalling receptor glycoprotein 130 (gp130). The structural details, as well as the exact physiological role of this interaction, remain unclear. Here, we describe the structural details of the SEA–gp130 complex by combining crosslinking mass spectrometry and computational modelling. Interestingly, SEA is not able to bind gp130-homologues from rat and mouse. Our data suggest that SEA may interact with human gp130 in a different manner than other known gp130-ligands. Moreover, the fact that SEA does not bind mouse or rat gp130 suggests that SAgs have additional mechanisms of action in humans.

【 授权许可】

Unknown