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• W2921308944 abstract "Abstract Methicillin resistant Staphylococcus aureus (MRSA) is a major human pathogen, which causes superficial to lethal clinical infections. Neutrophils are the most abundant leukocytes in the blood and are the first defense mechanism against S . aureus infections. Here we show S taphylococcal S uperantigen- L ike protein 11 (SSL11) from MRSA USA300_FPR3757 mediated differentiated human neutrophil-like cells (dHL60) motility arrest by inducing cell adhesion and “locking” cells in adhesion stage, without inducing oxidative burst. Pre-incubation of SSL11 with the glycan Sialyl Lewis X blocked SSL11 function and de-glycosylation of dHL60 cells by PNGase F abolished SSL11 binding, suggesting that SSL11 functions via interacting with glycans. This is the first description of a bacterial toxin inhibiting neutrophil motility by inducing adhesion and “locking” cells in an adhesion stage. Therefore, this study might provide a new target against S . aureus infections." @default.
• W2921308944 created "2019-03-22" @default.
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• W2921308944 date "2019-03-12" @default.
• W2921308944 modified "2023-10-16" @default.
• W2921308944 title "Staphylococcal Superantigen-like protein 11 mediates neutrophil adhesion and motility arrest, a unique bacterial toxin action" @default.
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• W2921308944 doi "https://doi.org/10.1038/s41598-019-40817-x" @default.
• W2921308944 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6414612" @default.
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