Abstract
Staphylococcal enterotoxin A (SEA) functions both as superantigens that stimulate non-specific T cell proliferation as well as potent gastrointestinal toxins. We previously reported that (−)-epigallocatechin gallate (EGCG) binds to SEA. Therefore, the ability of EGCG to inhibit SEA toxin activity was examined. As a result, EGCG significantly decreased SEA-induced expression and production of interferon gamma (IFN-γ). In addition, EGCG inhibited SEA-induced spleen cell proliferation. To investigate the role of the galloyl group in EGCG on SEA cytotoxicity in more detail, the effect of the binding of a hydroxyl group at position 3 of the galloyl group in EGCG to SEA on SEA cytotoxicity was examined using two methylated EGCG. SEA cytotoxicity was significantly controlled in both (−)-3′′-Me-EGCG and (−)-4′′-Me-EGCG. These results suggest that EGCG inhibits toxic activity via direct interaction with SEA or without any interaction with SEA. The binding affinity between SEA and EGCG under in vivo conditions was examined using a model solution. Although after treatment under acidic and alkaline conditions, the presence of protein and the digestive tract model solution, EGCG still interacted with SEA. Our studies are the first to demonstrate the effect of the binding of EGCG to SEA on toxin activity.
Highlights
Staphylococcus aureus, an indigenous bacterium, is sometimes pathogenic to humans and animals [1].S. aureus produces various toxins, among which staphylococcal enterotoxin A (SEA) has superantigenic activity, and is involved in multiple sclerosis, rheumatoid arthritis, psoriasis, atopic dermatitis, and chronic rhinosinusitis [2,3]
It has been reported that Staphylococcal enterotoxin A (SEA) activates enormous number of T cells activity and induces the production many cytokines, such as interferon gammaan (IFN-γ), by its superantigen of Catechins many cytokines, such as interferon gamma (IFN- ), by its superantigen activity are major functional components of green tea (Camellia sinensis), and some of these
We understanding of the molecular properties of catechins may lead to their application in medicine and previously reported that epigallocatechin gallate (EGCG) binds to SEA [18], indicating that EGCG may have the ability to inhibit food chemistry
Summary
Staphylococcus aureus, an indigenous bacterium, is sometimes pathogenic to humans and animals [1]. It has been reported that SEA activates enormous number of T cells activity and induces the production many cytokines, such as interferon gammaan (IFN-γ), by its superantigen [10,11,12]. Of Catechins many cytokines, such as interferon gamma (IFN- ), by its superantigen activity are major functional components of green tea (Camellia sinensis), and some of these. We understanding of the molecular properties of catechins may lead to their application in medicine and previously reported that EGCG binds to SEA [18], indicating that EGCG may have the ability to inhibit food chemistry. SEA toxin activitytoby binding to the site, toxinthe active site, the binding affinity between catechins under in vivo conditions was examined. SEA and the catechins under in vivo conditions was examined
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
