Characterization of the sortase repertoire in Bacillus anthracis.

LPXTG proteins, present in most if not all Gram-positive bacteria, are known to be anchored by sortases to the bacterial peptidoglycan. More than one sortase gene is often encoded in a bacterial species, and each sortase is supposed to specifically anchor given LPXTG proteins, depending of the seque...

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Autores principales:	Willy Aucher, Sophie Davison, Agnès Fouet
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0da9a9ea0c874fd09940231508e0096e
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spelling	oai:doaj.org-article:0da9a9ea0c874fd09940231508e0096e2021-11-18T07:34:53ZCharacterization of the sortase repertoire in Bacillus anthracis.1932-620310.1371/journal.pone.0027411https://doaj.org/article/0da9a9ea0c874fd09940231508e0096e2011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22076158/?tool=EBIhttps://doaj.org/toc/1932-6203LPXTG proteins, present in most if not all Gram-positive bacteria, are known to be anchored by sortases to the bacterial peptidoglycan. More than one sortase gene is often encoded in a bacterial species, and each sortase is supposed to specifically anchor given LPXTG proteins, depending of the sequence of the C-terminal cell wall sorting signal (cwss), bearing an LPXTG motif or another recognition sequence. B. anthracis possesses three sortase genes. B. anthracis sortase deleted mutant strains are not affected in their virulence. To determine the sortase repertoires, we developed a genetic screen using the property of the gamma phage to lyse bacteria only when its receptor, GamR, an LPXTG protein, is exposed at the surface. We identified 10 proteins that contain a cell wall sorting signal and are covalently anchored to the peptidoglycan. Some chimeric proteins yielded phage lysis in all sortase mutant strains, suggesting that cwss proteins remained surface accessible in absence of their anchoring sortase, probably as a consequence of membrane localization of yet uncleaved precursor proteins. For definite assignment of the sortase repertoires, we consequently relied on a complementary test, using a biochemical approach, namely immunoblot experiments. The sortase anchoring nine of these proteins has thus been determined. The absence of virulence defect of the sortase mutants could be a consequence of the membrane localization of the cwss proteins.Willy AucherSophie DavisonAgnès FouetPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 11, p e27411 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Willy Aucher Sophie Davison Agnès Fouet Characterization of the sortase repertoire in Bacillus anthracis.
description	LPXTG proteins, present in most if not all Gram-positive bacteria, are known to be anchored by sortases to the bacterial peptidoglycan. More than one sortase gene is often encoded in a bacterial species, and each sortase is supposed to specifically anchor given LPXTG proteins, depending of the sequence of the C-terminal cell wall sorting signal (cwss), bearing an LPXTG motif or another recognition sequence. B. anthracis possesses three sortase genes. B. anthracis sortase deleted mutant strains are not affected in their virulence. To determine the sortase repertoires, we developed a genetic screen using the property of the gamma phage to lyse bacteria only when its receptor, GamR, an LPXTG protein, is exposed at the surface. We identified 10 proteins that contain a cell wall sorting signal and are covalently anchored to the peptidoglycan. Some chimeric proteins yielded phage lysis in all sortase mutant strains, suggesting that cwss proteins remained surface accessible in absence of their anchoring sortase, probably as a consequence of membrane localization of yet uncleaved precursor proteins. For definite assignment of the sortase repertoires, we consequently relied on a complementary test, using a biochemical approach, namely immunoblot experiments. The sortase anchoring nine of these proteins has thus been determined. The absence of virulence defect of the sortase mutants could be a consequence of the membrane localization of the cwss proteins.
format	article
author	Willy Aucher Sophie Davison Agnès Fouet
author_facet	Willy Aucher Sophie Davison Agnès Fouet
author_sort	Willy Aucher
title	Characterization of the sortase repertoire in Bacillus anthracis.
title_short	Characterization of the sortase repertoire in Bacillus anthracis.
title_full	Characterization of the sortase repertoire in Bacillus anthracis.
title_fullStr	Characterization of the sortase repertoire in Bacillus anthracis.
title_full_unstemmed	Characterization of the sortase repertoire in Bacillus anthracis.
title_sort	characterization of the sortase repertoire in bacillus anthracis.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/0da9a9ea0c874fd09940231508e0096e
work_keys_str_mv	AT willyaucher characterizationofthesortaserepertoireinbacillusanthracis AT sophiedavison characterizationofthesortaserepertoireinbacillusanthracis AT agnesfouet characterizationofthesortaserepertoireinbacillusanthracis
_version_	1718423204087726080

Characterization of the sortase repertoire in Bacillus anthracis.

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