Identification of novel glycosyltransferases required for assembly of the Pasteurella multocida A:1 lipopolysaccharide and their involvement in virulence

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DOIResolve DOI: http://doi.org/10.1128/IAI.01144-08
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TypeArticle
Journal titleInfection and Immunity
Volume77
Issue4
Pages15321542; # of pages: 11
SubjectLipopolysaccharide; Pasteurella multocida; virulence; Mass spectrometry; Animals; Antimicrobial Cationic Peptides; Bacterial Proteins; biosynthesis; CHAIN; chemical synthesis; chemistry; Chickens; DISEASE; enzymology; Galactosyltransferases; genetics; Glucosyltransferases; Glycosyltransferases; IDENTIFICATION; Lipopolysaccharides; LPS; metabolism; Microbial Sensitivity Tests; Microbiology; MOLECULE; MUTANT; MUTANTS; Mutation; oligosaccharide; Pasteurella Infections; pathogenicity; peptide; Peptides; pharmacology; physiopathology; Poultry Diseases; protein; Proteins; STRAIN; STRAINS; STRUCTURAL; structure; Synthesis; transferase; Transferases; veterinary
AbstractWe previously determined the structure of the Pasteurella multocida Heeleston type 1 lipopolysaccharide (LPS) molecule and characterized some of the transferases essential for LPS biosythesis. We also showed that P. multocida strains expressing truncated LPS display reduced virulence. Here we have identified all the remaining glycosyltransferases required for synthesis of the oligosaccharide extension of the P. multocida Heddleston type 1 LPS, including a novel α-1,6 glucosyltransferase, a β-1,4 glucosyltransferase, a putative bi-functional galactosyltransferase and two heptosyltransferases. In addition, we identified a novel oligosaccharide extension expressed only in a heptosyltransferase (hptE) mutant background. All of the analyzed mutants expressing LPS with a truncated main oligosaccharide extension displayed reduced virulence but those expressing LPS with an intact heptose side chain were able to persist for long periods in muscle tissue. The hptC mutant, which expressed LPS with the shortest oligosaccharide extension and no heptose side chain, was unable to persist on the muscle or cause any disease. Furthermore, all of the mutants displayed inclreased sensitivity to the chicken antimicrobial peptide fowlicidin-1, with mutants expressing highly truncated LPS the most sensitive.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences
Peer reviewedYes
NRC numberBOYCE2009
NPARC number15459208
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Record identifierb85a438a-9576-414a-baa3-c0708f0729fe
Record created2010-08-16
Record modified2016-05-09
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