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

Par Conseil national de recherches du Canada

DOI	Trouver le DOI : https://doi.org/10.1128/IAI.01144-08
Auteur	Rechercher : Boyce, John D.; Rechercher : Harper, Marina; Rechercher : St. Michael, Frank¹; Rechercher : John, Marietta; Rechercher : Aubry, Annie¹; Rechercher : Parnas, Henrietta¹; Rechercher : Logan, Susan M.¹; Rechercher : Wilkie, Ian W.; Rechercher : Ford, Mark; Rechercher : Cox, Andrew D.¹; Rechercher : Adler, Ben
Affiliation	Conseil national de recherches du Canada. Institut des sciences biologiques du CNRC
Format	Texte, Article
Sujet	lipopolysaccharide; pasteurella multocida; virulence; mass spectrometry; antimicrobial cationic peptides; bacterial proteins; biosynthesis; chain; chemical synthesis; chemistry; chickens; enzymology; genetics; galactosyltransferases; glucosyltransferases; identification; lipopolysaccharides; LPS; metabolism; microbial sensitivity tests; microbiology; molecule; mutant; mutation; oligosaccharide; Pasteurella infections; pathogenicity; peptide; pharmacology; physiopathology; poultry diseases; protein; strain; structural; structure; synthesis; transferase; veterinary
Résumé	We 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.
Date de publication	2009-01-21
Dans	Infection and Immunity 77, nº 4 (21 janvier 2009) : 1532–1542.
Langue	anglais
Publications évaluées par des pairs	Oui
Numéro du CNRC	BOYCE2009
Numéro NPARC	15459208
Exporter la notice	Exporter en format RIS
Signaler une correction	Signaler une correction (s'ouvre dans un nouvel onglet)
Identificateur de l’enregistrement	b85a438a-9576-414a-baa3-c0708f0729fe
Enregistrement créé	2010-08-16
Enregistrement modifié	2020-04-16

Date de modification :: 2024-06-26