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

DOI	Resolve DOI: https://doi.org/10.1046/j.1365-2958.2000.01784.x
Author	Search for: Logan, S. M.¹; Search for: Conlan, J. W.; Search for: Monteiro, M. A.¹; Search for: Wakarchuk, W. W.¹; Search for: Altman, E.¹
Name affiliation	National Research Council of Canada. NRC Institute for Biological Sciences
Format	Text, Article
Journal title	Molecular Microbiology
ISSN	0950-382X 1365-2958
Volume	35
Issue	5
Pages	1156–1167
Abstract	A 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	2000-03
Publisher	Wiley
Language	English
Peer reviewed	Yes
NPARC number	23002078
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Record identifier	225e6ce7-d0d3-49df-b378-d6dbc84d5d21
Record created	2017-08-08
Record modified	2020-03-26