Origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in Campylobacter coli

Abstract Campylobacter jejuni and Campylobacter coli are the most common cause of bacterial gastroenteritis worldwide. Additionally, C. jejuni is the most common bacterial etiological agent in the autoimmune Guillain-Barré syndrome (GBS). Ganglioside mimicry by C. jejuni lipooligosaccharide (LOS) is...

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Autores principales:	Alejandra Culebro, Miguel P. Machado, João André Carriço, Mirko Rossi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ea148f3495cb45a89e3aadf8f7a7f550
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spelling	oai:doaj.org-article:ea148f3495cb45a89e3aadf8f7a7f5502021-12-02T15:07:56ZOrigin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in Campylobacter coli10.1038/s41598-018-21438-22045-2322https://doaj.org/article/ea148f3495cb45a89e3aadf8f7a7f5502018-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-21438-2https://doaj.org/toc/2045-2322Abstract Campylobacter jejuni and Campylobacter coli are the most common cause of bacterial gastroenteritis worldwide. Additionally, C. jejuni is the most common bacterial etiological agent in the autoimmune Guillain-Barré syndrome (GBS). Ganglioside mimicry by C. jejuni lipooligosaccharide (LOS) is the triggering factor of the disease. LOS-associated genes involved in the synthesis and transfer of sialic acid (glycosyltranferases belonging to family GT-42) are essential in C. jejuni to synthesize ganglioside-like LOS. Despite being isolated from GBS patients, scarce genetic evidence supports C. coli role in the disease. In this study, through data mining and bioinformatics analysis, C. coli is shown to possess a larger GT-42 glycosyltransferase repertoire than C. jejuni. Although GT-42 glycosyltransferases are widely distributed in C. coli population, only a fraction of C. coli strains (1%) are very likely able to express ganglioside mimics. Even though the activity of C. coli specific GT-42 enzymes and their role in shaping the bacterial population are yet to be explored, evidence presented herein suggest that loss of function of some LOS-associated genes occurred during agriculture niche adaptation.Alejandra CulebroMiguel P. MachadoJoão André CarriçoMirko RossiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-9 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alejandra Culebro Miguel P. Machado João André Carriço Mirko Rossi Origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in Campylobacter coli
description	Abstract Campylobacter jejuni and Campylobacter coli are the most common cause of bacterial gastroenteritis worldwide. Additionally, C. jejuni is the most common bacterial etiological agent in the autoimmune Guillain-Barré syndrome (GBS). Ganglioside mimicry by C. jejuni lipooligosaccharide (LOS) is the triggering factor of the disease. LOS-associated genes involved in the synthesis and transfer of sialic acid (glycosyltranferases belonging to family GT-42) are essential in C. jejuni to synthesize ganglioside-like LOS. Despite being isolated from GBS patients, scarce genetic evidence supports C. coli role in the disease. In this study, through data mining and bioinformatics analysis, C. coli is shown to possess a larger GT-42 glycosyltransferase repertoire than C. jejuni. Although GT-42 glycosyltransferases are widely distributed in C. coli population, only a fraction of C. coli strains (1%) are very likely able to express ganglioside mimics. Even though the activity of C. coli specific GT-42 enzymes and their role in shaping the bacterial population are yet to be explored, evidence presented herein suggest that loss of function of some LOS-associated genes occurred during agriculture niche adaptation.
format	article
author	Alejandra Culebro Miguel P. Machado João André Carriço Mirko Rossi
author_facet	Alejandra Culebro Miguel P. Machado João André Carriço Mirko Rossi
author_sort	Alejandra Culebro
title	Origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in Campylobacter coli
title_short	Origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in Campylobacter coli
title_full	Origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in Campylobacter coli
title_fullStr	Origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in Campylobacter coli
title_full_unstemmed	Origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in Campylobacter coli
title_sort	origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in campylobacter coli
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/ea148f3495cb45a89e3aadf8f7a7f550
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Origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in Campylobacter coli

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