ArticleInfection and immunity1999
Phase variation in Helicobacter pylori lipopolysaccharide due to changes in the lengths of poly(C) tracts in alpha3-fucosyltransferase genes.
Article in Infection and immunity, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 48 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
48 citing papers in PubMed, 142 citations in OpenAlex.
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- A Tripartite Efflux System Affects Flagellum Stability inInternational journal of molecular sciences · 2022Article
- Natural Transmission of Helicobacter saguini Causes Multigenerational Inflammatory Bowel Disease in C57/129 IL-10mSphere · 2020Article
- East-Asian Helicobacter pylori strains synthesize heptan-deficient lipopolysaccharide.PLoS genetics · 2019Article
- Review
- Stromal C-type lectin receptor COLEC12 integrates H. pylori, PGE2-EP2/4 axis and innate immunity in gastric diseases.Scientific reports · 2018Article
- Molecular mimicry inWorld journal of gastroenterology · 2017Review
- Review
- Quantum changes in Helicobacter pylori gene expression accompany host-adaptation.DNA research : an international journal for rapid publication of reports on genes and genomes · 2017Article
- Structural modifications of Helicobacter pylori lipopolysaccharide: an idea for how to live in peace.World journal of gastroenterology · 2014Review
- A variable homopolymeric G-repeat defines small RNA-mediated posttranscriptional regulation of a chemotaxis receptor in Helicobacter pylori.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Role of energy sensor TlpD of Helicobacter pylori in gerbil colonization and genome analyses after adaptation in the gerbil.Infection and immunity · 2013Article
- Novel functions for glycosyltransferases Jhp0562 and GalT in Lewis antigen synthesis and variation in Helicobacter pylori.Infection and immunity · 2012Article
- Comparative transcriptomics of H. pylori strains AM5, SS1 and their hpyAVIBM deletion mutants: possible roles of cytosine methylation.PloS one · 2012Article
- Genotypic and phenotypic variation of Lewis antigen expression in geographically diverse Helicobacter pylori isolates.Helicobacter · 2011Article
- New implications on genomic adaptation derived from the Helicobacter pylori genome comparison.PloS one · 2011Article
- Removal of the outer Kdo from Helicobacter pylori lipopolysaccharide and its impact on the bacterial surface.Molecular microbiology · 2010Article
- Helicobacter pylori: gastric cancer and beyond.Nature reviews. Cancer · 2010Review
- Helicobacter pylori lipopolysaccharide is synthesized via a novel pathway with an evolutionary connection to protein N-glycosylation.PLoS pathogens · 2010Article
- Surreptitious manipulation of the human host by Helicobacter pylori.Gut microbes · 2010Article
Corrections and comments
- Erratum issued
Authors and funding
13 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lipopolysaccharide (LPS) of Helicobacter pylori expresses the Lewis x (Lex) and/or Ley antigen. We have shown previously that H. pylori LPS displays phase variation whereby an Lex-positive strain yields variants with different LPS serotypes, for example, Lex plus Ley or nonfucosylated polylactosamine. H. pylori has two alpha3-fucosyltransferase genes that both contain poly(C) tracts. We now demonstrate that these tracts can shorten or lengthen randomly, which results in reversible frameshifting and inactivation of the gene products. We provide genetic and serological evidence that this mechanism causes H. pylori LPS phase variation and demonstrate that the on or off status of alpha3-fucosyltransferase genes determines the LPS serotypes of phase variants and clinical isolates. The role of the alpha3-fucosyltransferase gene products in determining the LPS serotype was confirmed by structural-chemical analysis of alpha3-fucosyltransferase knockout mutants. The data also show that the two alpha3-fucosyltransferase genes code for enzymes with different fine specificities, and we propose the names futA and futB to designate the orthologs of the H. pylori 26695 alpha3-fucosyltransferase genes HP0379 and HP0651, respectively. The data also show that the alpha3-fucosylation precedes alpha2-fucosylation [corrected], an order of events opposite to that which prevails in mammals. Finally, the data provide an understanding at the molecular level of the mechanisms underlying LPS diversity in H. pylori, which may play an important role in adaptation to the host.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.