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

Uzuncayir, Sibel (author): Lund University,Lunds universitet,Medicinsk strukturbiologi,Forskargrupper vid Lunds universitet,Medical Structural Biology,Lund University Research Groups

Regenthal, Paulina (author): Lund University,Lunds universitet,Institutionen för experimentell medicinsk vetenskap,Medicinska fakulteten,Department of Experimental Medical Science,Faculty of Medicine

Åbacka, Hannah (author): Lund University,Lunds universitet,Medicinsk strukturbiologi,Forskargrupper vid Lunds universitet,Medical Structural Biology,Lund University Research Groups

Emanuelsson, Cecilia (author): Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH

Lindkvist-Petersson, Karin (author): Lund University,Lunds universitet,Medicinsk strukturbiologi,Forskargrupper vid Lunds universitet,Medical Structural Biology,Lund University Research Groups,LINXS - Lund institute of advanced neutron and x-ray science

(creator_code:org_t)

2022-01-30
2022
English.
In: FEBS Letters. - : Wiley. - 1873-3468 .- 0014-5793. ; 596:7, s. 910-923

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Abstract Subject headings

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.

By the author/editor: Uzuncayir, Sibel; Vera-Rodriguez, ...; Regenthal, Pauli ...; Åbacka, Hannah; Emanuelsson, Cec ...; Bahl, Christophe ...; show more...; Lindkvist-Peters ...; show less...

About the subject

MEDICAL AND HEALTH SCIENCES: MEDICAL AND HEAL ...; and Basic Medicine; and Immunology in th ...

MEDICAL AND HEALTH SCIENCES: MEDICAL AND HEAL ...; and Basic Medicine; and Microbiology in ...

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