Lipopolysaccharide diversity evolving in Helicobacter pylori communities through genetic modifications in fucosyltransferases.

Helicobacter pylori persistently colonizes the gastric mucosa of half the human population. It is one of the most genetically diverse bacterial organisms and subvariants are continuously emerging within an H. pylori population. In this study we characterized a number of single-colony isolates from H...

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Main Authors: Christina Nilsson, Anna Skoglund, Anthony P Moran, Heidi Annuk, Lars Engstrand, Staffan Normark
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2008-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC2583950?pdf=render
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author Christina Nilsson
Anna Skoglund
Anthony P Moran
Heidi Annuk
Lars Engstrand
Staffan Normark
author_facet Christina Nilsson
Anna Skoglund
Anthony P Moran
Heidi Annuk
Lars Engstrand
Staffan Normark
author_sort Christina Nilsson
collection DOAJ
description Helicobacter pylori persistently colonizes the gastric mucosa of half the human population. It is one of the most genetically diverse bacterial organisms and subvariants are continuously emerging within an H. pylori population. In this study we characterized a number of single-colony isolates from H. pylori communities in various environmental settings, namely persistent human gastric infection, in vitro bacterial subcultures on agar medium, and experimental in vivo infection in mice. The lipopolysaccharide (LPS) O-antigen chain revealed considerable phenotypic diversity between individual cells in the studied bacterial communities, as demonstrated by size variable O-antigen chains and different levels of Lewis glycosylation. Absence of high-molecular-weight O-antigen chains was notable in a number of experimentally passaged isolates in vitro and in vivo. This phenotype was not evident in bacteria obtained from a human gastric biopsy, where all cells expressed high-molecular-weight O-antigen chains, which thus may be the preferred phenotype for H. pylori colonizing human gastric mucosa. Genotypic variability was monitored in the two genes encoding alpha1,3-fucosyltransferases, futA and futB, that are involved in Lewis antigen expression. Genetic modifications that could be attributable to recombination events within and between the two genes were commonly detected and created a diversity, which together with phase variation, contributed to divergent LPS expression. Our data suggest that the surrounding environment imposes a selective pressure on H. pylori to express certain LPS phenotypes. Thus, the milieu in a host will select for bacterial variants with particular characteristics that facilitate adaptation and survival in the gastric mucosa of that individual, and will shape the bacterial community structure.
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spelling doaj.art-c6fbddbd748a42e6a880e0a114fe1ade2022-12-21T22:30:14ZengPublic Library of Science (PLoS)PLoS ONE1932-62032008-01-01311e381110.1371/journal.pone.0003811Lipopolysaccharide diversity evolving in Helicobacter pylori communities through genetic modifications in fucosyltransferases.Christina NilssonAnna SkoglundAnthony P MoranHeidi AnnukLars EngstrandStaffan NormarkHelicobacter pylori persistently colonizes the gastric mucosa of half the human population. It is one of the most genetically diverse bacterial organisms and subvariants are continuously emerging within an H. pylori population. In this study we characterized a number of single-colony isolates from H. pylori communities in various environmental settings, namely persistent human gastric infection, in vitro bacterial subcultures on agar medium, and experimental in vivo infection in mice. The lipopolysaccharide (LPS) O-antigen chain revealed considerable phenotypic diversity between individual cells in the studied bacterial communities, as demonstrated by size variable O-antigen chains and different levels of Lewis glycosylation. Absence of high-molecular-weight O-antigen chains was notable in a number of experimentally passaged isolates in vitro and in vivo. This phenotype was not evident in bacteria obtained from a human gastric biopsy, where all cells expressed high-molecular-weight O-antigen chains, which thus may be the preferred phenotype for H. pylori colonizing human gastric mucosa. Genotypic variability was monitored in the two genes encoding alpha1,3-fucosyltransferases, futA and futB, that are involved in Lewis antigen expression. Genetic modifications that could be attributable to recombination events within and between the two genes were commonly detected and created a diversity, which together with phase variation, contributed to divergent LPS expression. Our data suggest that the surrounding environment imposes a selective pressure on H. pylori to express certain LPS phenotypes. Thus, the milieu in a host will select for bacterial variants with particular characteristics that facilitate adaptation and survival in the gastric mucosa of that individual, and will shape the bacterial community structure.http://europepmc.org/articles/PMC2583950?pdf=render
spellingShingle Christina Nilsson
Anna Skoglund
Anthony P Moran
Heidi Annuk
Lars Engstrand
Staffan Normark
Lipopolysaccharide diversity evolving in Helicobacter pylori communities through genetic modifications in fucosyltransferases.
PLoS ONE
title Lipopolysaccharide diversity evolving in Helicobacter pylori communities through genetic modifications in fucosyltransferases.
title_full Lipopolysaccharide diversity evolving in Helicobacter pylori communities through genetic modifications in fucosyltransferases.
title_fullStr Lipopolysaccharide diversity evolving in Helicobacter pylori communities through genetic modifications in fucosyltransferases.
title_full_unstemmed Lipopolysaccharide diversity evolving in Helicobacter pylori communities through genetic modifications in fucosyltransferases.
title_short Lipopolysaccharide diversity evolving in Helicobacter pylori communities through genetic modifications in fucosyltransferases.
title_sort lipopolysaccharide diversity evolving in helicobacter pylori communities through genetic modifications in fucosyltransferases
url http://europepmc.org/articles/PMC2583950?pdf=render
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