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Staphylococcal Superantigen-like protein 11 mediates neutrophil adhesion and motility arrest, a unique bacterial toxin action. Sci Rep 2019 Mar 12;9(1):4211

Date

03/14/2019

Pubmed ID

30862940

Pubmed Central ID

PMC6414612

DOI

10.1038/s41598-019-40817-x

Scopus ID

2-s2.0-85062821069 (requires institutional sign-in at Scopus site)   10 Citations

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 Staphylococcal Superantigen-Like 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.

Author List

Chen C, Yang C, Barbieri JT

Author

Joseph T. Barbieri PhD Professor in the Microbiology and Immunology department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Bacterial Proteins
Cell Adhesion
Cell Movement
HL-60 Cells
Humans
Methicillin-Resistant Staphylococcus aureus
Neutrophils
Superantigens