Analyses of the complex formation of staphylococcal enterotoxin A and the human gp130 cytokine receptor. Issue 7 (30th January 2022)

• Record Type: Journal Article
• Authors: Uzunçayır, Sibel; Vera‐Rodriguez, Arturo; Regenthal, Paulina; Åbacka, Hannah; Emanuelsson, Cecilia; Bahl, Christopher D.; Lindkvist‐Petersson, Karin
• Is Part Of: FEBS letters. Volume 596:Issue 7(2022)
• Page Start: 910
• Page End: 923
• Publication Date: 2022-01-30
• Subjects: food poisoning -- gp130 -- SEA -- SPR -- superantigen; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.14292
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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. Abstract : Here, the structural details of the complex between a bacterial superantigen (SEA) and human cytokine signalling receptor gp130 were analysed. The data suggest that SEA may interact with human gp130 in a different manner than other gp130‐ligands. Moreover, as SEA was shown to not bind rodent gp130, the interaction with human gp130 is speculated to be coupled to food poisoning.