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

John Dallas Boyce, Marina Harper, Frank St Michael, Marietta John, Annie Aubry, Henrietta Parnas, Susan M Logan, Ian W Wilkie, Mark E Ford, Andrew D Cox, Ben Adler

Research output: Contribution to journalArticleResearchpeer-review

26 Citations (Scopus)

Abstract

We previously determined the structure of the Pasteurella multocida Heddleston type 1 lipopolysaccharide (LPS) molecule and characterized some of the transferases essential for LPS biosynthesis. We also showed that P. multocida strains expressing truncated LPS display reduced virulence. Here we have identified all of the remaining glycosyltransferases required for synthesis of the oligosaccharide extension of the P. multocida Heddleston type 1 LPS, including a novel alpha-1,6 glucosyltransferase, a beta-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 increased sensitivity to the chicken antimicrobial peptide fowlicidin-1, with mutants expressing highly truncated LPS the most sensitive.
Original languageEnglish
Pages (from-to)1532 - 1542
Number of pages11
JournalInfection and Immunity
Volume77
Issue number4
DOIs
Publication statusPublished - 2009

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