A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes

Abstract The capsular polysaccharide (CPS) is the major virulence factor of the emerging zoonotic pathogen Streptococcus suis. CPS differences are also the basis for serological differentiation of the species into 29 serotypes. Serotypes 2 and 1/2, which possess identical gene content in their cps l...

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Autores principales:	David Roy, Taryn B. T. Athey, Jean-Philippe Auger, Guillaume Goyette-Desjardins, Marie-Rose Van Calsteren, Daisuke Takamatsu, Masatoshi Okura, Sarah Teatero, Martín Alcorlo, Juan A. Hermoso, Mariela Segura, Marcelo Gottschalk, Nahuel Fittipaldi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3d9c511fd06949b3a5702c341d1b3338
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spelling	oai:doaj.org-article:3d9c511fd06949b3a5702c341d1b33382021-12-02T15:06:07ZA single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes10.1038/s41598-017-04403-32045-2322https://doaj.org/article/3d9c511fd06949b3a5702c341d1b33382017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04403-3https://doaj.org/toc/2045-2322Abstract The capsular polysaccharide (CPS) is the major virulence factor of the emerging zoonotic pathogen Streptococcus suis. CPS differences are also the basis for serological differentiation of the species into 29 serotypes. Serotypes 2 and 1/2, which possess identical gene content in their cps loci, express CPSs that differ only by substitution of galactose (Gal) by N-acetylgalactosamine (GalNAc) in the CPS side chain. The same sugar substitution differentiates the CPS of serotypes 14 and 1, whose cps loci are also identical in gene content. Here, using mutagenesis, CPS structural analysis, and protein structure modeling, we report that a single amino acid polymorphism in the glycosyltransferase CpsK defines the enzyme substrate predilection for Gal or GalNAc and therefore determines CPS composition, structure, and strain serotype. We also show that the different CPS structures have similar antiphagocytic properties and that serotype switching has limited impact on the virulence of S. suis.David RoyTaryn B. T. AtheyJean-Philippe AugerGuillaume Goyette-DesjardinsMarie-Rose Van CalsterenDaisuke TakamatsuMasatoshi OkuraSarah TeateroMartín AlcorloJuan A. HermosoMariela SeguraMarcelo GottschalkNahuel FittipaldiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q David Roy Taryn B. T. Athey Jean-Philippe Auger Guillaume Goyette-Desjardins Marie-Rose Van Calsteren Daisuke Takamatsu Masatoshi Okura Sarah Teatero Martín Alcorlo Juan A. Hermoso Mariela Segura Marcelo Gottschalk Nahuel Fittipaldi A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes
description	Abstract The capsular polysaccharide (CPS) is the major virulence factor of the emerging zoonotic pathogen Streptococcus suis. CPS differences are also the basis for serological differentiation of the species into 29 serotypes. Serotypes 2 and 1/2, which possess identical gene content in their cps loci, express CPSs that differ only by substitution of galactose (Gal) by N-acetylgalactosamine (GalNAc) in the CPS side chain. The same sugar substitution differentiates the CPS of serotypes 14 and 1, whose cps loci are also identical in gene content. Here, using mutagenesis, CPS structural analysis, and protein structure modeling, we report that a single amino acid polymorphism in the glycosyltransferase CpsK defines the enzyme substrate predilection for Gal or GalNAc and therefore determines CPS composition, structure, and strain serotype. We also show that the different CPS structures have similar antiphagocytic properties and that serotype switching has limited impact on the virulence of S. suis.
format	article
author	David Roy Taryn B. T. Athey Jean-Philippe Auger Guillaume Goyette-Desjardins Marie-Rose Van Calsteren Daisuke Takamatsu Masatoshi Okura Sarah Teatero Martín Alcorlo Juan A. Hermoso Mariela Segura Marcelo Gottschalk Nahuel Fittipaldi
author_facet	David Roy Taryn B. T. Athey Jean-Philippe Auger Guillaume Goyette-Desjardins Marie-Rose Van Calsteren Daisuke Takamatsu Masatoshi Okura Sarah Teatero Martín Alcorlo Juan A. Hermoso Mariela Segura Marcelo Gottschalk Nahuel Fittipaldi
author_sort	David Roy
title	A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes
title_short	A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes
title_full	A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes
title_fullStr	A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes
title_full_unstemmed	A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes
title_sort	single amino acid polymorphism in the glycosyltransferase cpsk defines four streptococcus suis serotypes
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/3d9c511fd06949b3a5702c341d1b3338
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A single amino acid polymorphism in the glycosyltransferase CpsK defines four Streptococcus suis serotypes

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