Nonimmune antibody interactions of Group A Streptococcus M and M-like proteins.

M and M-like proteins are major virulence factors of the widespread and potentially deadly bacterial pathogen Streptococcus pyogenes. These proteins confer resistance against innate and adaptive immune responses by recruiting specific human proteins to the streptococcal surface. Nonimmune recruitmen...

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Autores principales:	Jori O Mills, Partho Ghosh
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/ca231fa063bf464f9bb7ce6c57c7e84d
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spelling	oai:doaj.org-article:ca231fa063bf464f9bb7ce6c57c7e84d2021-11-25T05:48:02ZNonimmune antibody interactions of Group A Streptococcus M and M-like proteins.1553-73661553-737410.1371/journal.ppat.1009248https://doaj.org/article/ca231fa063bf464f9bb7ce6c57c7e84d2021-02-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.1009248https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374M and M-like proteins are major virulence factors of the widespread and potentially deadly bacterial pathogen Streptococcus pyogenes. These proteins confer resistance against innate and adaptive immune responses by recruiting specific human proteins to the streptococcal surface. Nonimmune recruitment of immunoglobulins G (IgG) and A (IgA) through their fragment crystallizable (Fc) domains by M and M-like proteins was described almost 40 years ago, but its impact on virulence remains unresolved. These interactions have been suggested to be consequential under immune conditions at mucosal surfaces and in secretions but not in plasma, while other evidence suggests importance in evading phagocytic killing in nonimmune blood. Recently, an indirect effect of Fc-binding through ligand-induced stabilization of an M-like protein was shown to increase virulence. Nonimmune recruitment has also been seen to contribute to tissue damage in animal models of autoimmune diseases triggered by S. pyogenes infection. The damage was treatable by targeting Fc-binding. This and other potential therapeutic applications warrant renewed attention to Fc-binding by M and M-like proteins.Jori O MillsPartho GhoshPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 17, Iss 2, p e1009248 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Jori O Mills Partho Ghosh Nonimmune antibody interactions of Group A Streptococcus M and M-like proteins.
description	M and M-like proteins are major virulence factors of the widespread and potentially deadly bacterial pathogen Streptococcus pyogenes. These proteins confer resistance against innate and adaptive immune responses by recruiting specific human proteins to the streptococcal surface. Nonimmune recruitment of immunoglobulins G (IgG) and A (IgA) through their fragment crystallizable (Fc) domains by M and M-like proteins was described almost 40 years ago, but its impact on virulence remains unresolved. These interactions have been suggested to be consequential under immune conditions at mucosal surfaces and in secretions but not in plasma, while other evidence suggests importance in evading phagocytic killing in nonimmune blood. Recently, an indirect effect of Fc-binding through ligand-induced stabilization of an M-like protein was shown to increase virulence. Nonimmune recruitment has also been seen to contribute to tissue damage in animal models of autoimmune diseases triggered by S. pyogenes infection. The damage was treatable by targeting Fc-binding. This and other potential therapeutic applications warrant renewed attention to Fc-binding by M and M-like proteins.
format	article
author	Jori O Mills Partho Ghosh
author_facet	Jori O Mills Partho Ghosh
author_sort	Jori O Mills
title	Nonimmune antibody interactions of Group A Streptococcus M and M-like proteins.
title_short	Nonimmune antibody interactions of Group A Streptococcus M and M-like proteins.
title_full	Nonimmune antibody interactions of Group A Streptococcus M and M-like proteins.
title_fullStr	Nonimmune antibody interactions of Group A Streptococcus M and M-like proteins.
title_full_unstemmed	Nonimmune antibody interactions of Group A Streptococcus M and M-like proteins.
title_sort	nonimmune antibody interactions of group a streptococcus m and m-like proteins.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/ca231fa063bf464f9bb7ce6c57c7e84d
work_keys_str_mv	AT joriomills nonimmuneantibodyinteractionsofgroupastreptococcusmandmlikeproteins AT parthoghosh nonimmuneantibodyinteractionsofgroupastreptococcusmandmlikeproteins
_version_	1718414484938162176

Nonimmune antibody interactions of Group A Streptococcus M and M-like proteins.

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