Natural selection in the chicken host identifies 3-deoxy-D-manno-octulosonic acid kinase residues essential for phosphorylation of Pasteurella multocida lipopolysaccharide.

ABSTRACT: Pasteurella multocida is the causative agent of a number of diseases in animals, including fowl cholera. P. multocida strains simultaneously express two lipopolysaccharide (LPS) glycoforms (glycoforms A and B) that differ only in their inner core structure. Glycoform A contains a single 3-deoxy-d-manno-octulosonic acid (Kdo) residue that is phosphorylated by the Kdo kinase, KdkA, whereas glycoform B contains two unphosphorylated Kdo residues. We have previously shown that P. multocida mutants lacking the heptosyltransferase, HptA, produce full-length glycoform B LPS and a large amount of truncated glycoform A LPS, as they cannot add heptose to the glycoform A inner core. These hptA mutants were attenuated in chickens because the truncated LPS made them vulnerable to host defense mechanisms

SUBMITTER: Harper M 

PROVIDER: S-EPMC2937434 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature