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FAF and SufA: Proteins of Finegoldia magna That Modulate the Antibacterial Activity of Histones.

In English

Författare

Summary, in English

Many bacterial pathogens have developed methods to overcome the defences of the host innate immune system. One such defence is the release of antimicrobial peptides (AMPs). Histones have been found to function as AMPs, in addition to their main biological function of packaging and organising DNA into nucleosomes. In this study, the Gram-positive anaerobic coccus Finegoldia magna was found to bind histones by Western blot and immunoprecipitation analysis. F. magna, which is normally a commensal of the skin and mucous membranes, is also known to act as an opportunistic pathogen and has been isolated from various clinical infection sites. It was found to bind to histones extracted from human skin epidermis through its surface and extracellular adhesion protein FAF. Through FAF binding, F. magna was protected from histone bactericidal activity. Furthermore, the histones were found to be degraded by SufA, a subtilisin-like extracellular serine protease of F. magna. Hence, the results of the present study will give more insight into how F. magna persists both as a commensal organism at the basement membrane of the skin and as an opportunistic pathogen during infection. © 2013 S. Karger AG, Basel.

Avdelning/ar

Publiceringsår

2013-12-11

Språk

Engelska

Publikation/Tidskrift/Serie

Journal of Innate Immunity

Dokumenttyp

Artikel i tidskrift

Förlag

Karger

Ämne

  • Immunology in the medical area

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1662-811X