Pasteurella multocida expresses two lipopolysaccharide glycoforms simultaneously, but only a single form is required for virulence: identification of two acceptor-specific heptosyl I transferases: Infect.Immun.

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TypeArticle
Journal titleInfect.Immun.
Volume75
Issue8
Pages38853893; # of pages: 9
SubjectACID; Animals; ANTIGEN; bacterial; chemistry; Chickens; core oligosaccharide; enzymology; EXPRESSION; Form; Gene Deletion; genetics; Glycosyltransferases; Heptoses; IDENTIFICATION; KDO; lipooligosaccharide; LIPOPOLYSACCHARIDE; Lipopolysaccharides; LPS; metabolism; Microbial Viability; Microbiology; MOLECULE; MUTANT; MUTANTS; oligosaccharide; Pasteurella Infections; Pasteurella multocida; pathogenicity; PHASE; PHASE VARIATION; Phosphorylation; REGION; RESIDUES; Spectrometry,Mass,Electrospray Ionization; STRUCTURAL; structure; sugar; Sugar Acids; Survival Analysis; transferase; Transferases; Virulence
AbstractLipopolysaccharide (LPS) is a critical virulence determinant in Pasteurella multocida and a major antigen responsible for host protective immunity. In other mucosal pathogens, variation in LPS or lipooligosaccharide structure typically occurs in the outer core oligosaccharide regions due to phase variation. P. multocida elaborates a conserved oligosaccharide extension attached to two different, simultaneously expressed inner core structures, one containing a single phosphorylated 3-deoxy-D-manno-octulosonic acid (Kdo) residue and the other containing two Kdo residues. We demonstrate that two heptosyltransferases, HptA and HptB, add the first heptose molecule to the Kdo(1) residue and that each exclusively recognizes different acceptor molecules. HptA is specific for the glycoform containing a single, phosphorylated Kdo residue (glycoform A), while HptB is specific for the glycoform containing two Kdo residues (glycoform B). In addition, KdkA was identified as a Kdo kinase, required for phosphorylation of the first Kdo molecule. Importantly, virulence data obtained from infected chickens showed that while wild-type P. multocida expresses both LPS glycoforms in vivo, bacterial mutants that produced only glycoform B were fully virulent, demonstrating for the first time that expression of a single LPS form is sufficient for P. multocida survival in vivo. We conclude that the ability of P. multocida to elaborate alternative inner core LPS structures is due to the simultaneous expression of two different heptosyltransferases that add the first heptose residue to the nascent LPS molecule and to the expression of both a bifunctional Kdo transferase and a Kdo kinase, which results in the initial assembly of two inner core structures
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberHARPER2007
NPARC number9363967
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Record identifier070ebe15-6f5c-4f4b-98d5-110a396fce64
Record created2009-07-10
Record modified2016-05-09
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