Functional genomics of Helicobacter pylori: identification of a β-1,4 galactosyltransferase and generation of mutants with altered lipopolysaccharide

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DOIResolve DOI: http://doi.org/10.1046/j.1365-2958.2000.01784.x
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TypeArticle
Journal titleMolecular Microbiology
ISSN0950-382X
1365-2958
Volume35
Issue5
Pages11561167
AbstractA previously annotated open reading frame (ORF) (HP0826) from Helicobacter pylori was cloned and expressed in Escherichia coli cells and determined to be a β-1,4-galactosyltransferase that used GlcNAc as an acceptor. Mutational analysis in H. pylori strains demonstrated that this enzyme plays a key role in the biosynthesis of the type 2 N-acetyl-lactosamine (LacNAc) polysaccharide O-chain backbone, by catalysing the addition of Gal to GlcNAc. To examine the potential role of this O-chain structure in bacterial colonization of the host stomach, the mutation was introduced into H. pylori strain SS1 which is known to be capable of colonizing the gastric mucosa of mice. Compared with the parental strain, mutated SS1 was less efficient at colonizing the murine stomach.
Publication date
PublisherWiley
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Biological Sciences
Peer reviewedYes
NPARC number23002078
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Record identifier225e6ce7-d0d3-49df-b378-d6dbc84d5d21
Record created2017-08-08
Record modified2017-08-08
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