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Group A Streptococcal M1 Protein Sequesters Cathelicidin to Evade Innate Immune Killing.

Abstract：

:The antimicrobial peptide LL-37 is generated upon proteolytic cleavage of cathelicidin and limits invading pathogens by directly targeting microbial membranes as well as stimulating innate immune cell function. However, some microbes evade LL-37-mediated defense. Notably, group A Streptococcus (GAS) strains belonging to the hypervirulent M1T1 serogroup are more resistant to human LL-37 than other GAS serogroups. We show that the GAS surface-associated M1 protein sequesters and neutralizes LL-37 antimicrobial activity through its N-terminal domain. M1 protein also binds the cathelicidin precursor hCAP-18, preventing its proteolytic maturation into antimicrobial forms. Exogenous M1 protein rescues M1-deficient GAS from killing by neutrophils and within neutrophil extracellular traps and neutralizes LL-37 chemotactic properties. M1 also binds murine cathelicidin, and its virulence contribution in a murine model of necrotizing skin infection is largely driven by its ability to neutralize this host defense peptide. Thus, cathelicidin resistance is essential for the pathogenesis of hyperinvasive M1T1 GAS.

journal_name

Cell Host Microbe

journal_title

Cell host & microbe

authors

LaRock CN,Döhrmann S,Todd J,Corriden R,Olson J,Johannssen T,Lepenies B,Gallo RL,Ghosh P,Nizet V

doi

10.1016/j.chom.2015.09.004

subject

Has Abstract

pub_date

2015-10-14 00:00:00

pages

471-7

issue

4

eissn

1931-3128

issn

1934-6069

pii

S1931-3128(15)00373-X

journal_volume

18

pub_type

杂志文章

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