Identification of Novel Glycosyltransferases Required for Assembly of the Pasteurella multocida A:1 Lipopolysaccharide and Their Involvement in Virulence

Boyce, John D., Harper, Marina, Michael, Frank St., John, Marietta, Aubry, Annie, Parnas, Henrietta, Logan, Susan M., Wilkie, Ian W., Ford, Mark, Cox, Andrew D. and Adler, Ben (2009) Identification of Novel Glycosyltransferases Required for Assembly of the Pasteurella multocida A:1 Lipopolysaccharide and Their Involvement in Virulence. Infection and Immunity, 77 4: 1532-1542. doi:10.1128/IAI.01144-08

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Author Boyce, John D.
Harper, Marina
Michael, Frank St.
John, Marietta
Aubry, Annie
Parnas, Henrietta
Logan, Susan M.
Wilkie, Ian W.
Ford, Mark
Cox, Andrew D.
Adler, Ben
Title Identification of Novel Glycosyltransferases Required for Assembly of the Pasteurella multocida A:1 Lipopolysaccharide and Their Involvement in Virulence
Formatted title
Identification of Novel Glycosyltransferases Required for Assembly of the Pasteurella multocida A:1 Lipopolysaccharide and Their Involvement in Virulence
Journal name Infection and Immunity   Check publisher's open access policy
ISSN 1098-5522
1070-6313
Publication date 2009-04-01
Sub-type Article (original research)
DOI 10.1128/IAI.01144-08
Open Access Status File (Publisher version)
Volume 77
Issue 4
Start page 1532
End page 1542
Total pages 11
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
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 β-1,4 glucosyltransferase, a putative bifunctional 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 being the most sensitive.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Veterinary Science Publications
 
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Created: Thu, 03 Sep 2009, 18:31:37 EST by Mr Andrew Martlew on behalf of Faculty Of Nat Resources, Agric & Veterinary Sc