Open AccessThe Wzy O‐antigen polymerase of Y ersinia pseudotuberculosis O:2a has a dependence on the Wzz chain‐length determinant for efficient polymerization
Author(s) -
Kenyon Johanna J.,
Reeves Peter R.
Publication year - 2013
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12311
Subject(s) - yersinia pseudotuberculosis , polymerase , lipopolysaccharide , mutant , biology , microbiology and biotechnology , escherichia coli , serotype , yersinia , chemistry , bacteria , genetics , gene , virulence , endocrinology
Lipopolysaccharide is a major immunogenic structure for the pathogen Y ersinia pseudotuberculosis, which contains the O‐specific polysaccharide ( OPS ) that is presented on the cell surface. The OPS contains many repeats of the oligosaccharide O‐unit and exhibits a preferred modal chain length that has been shown to be crucial for cell protection in Y ersinia . It is well established that the Wzz protein determines the preferred chain length of the OPS , and in its absence, the polymerization of O units by the Wzy polymerase is uncontrolled. However, for Y . pseudotuberculosis , a wzz mutation has never been described. In this study, we examine the effect of Wzz loss in Y . pseudotuberculosis serotype O:2a and compare the lipopolysaccharide chain‐length profile to that of E scherichia coli serotype O111. In the absence of Wzz, the lipopolysaccharides of the two species showed significant differences in Wzy polymerization. Y ersinia pseudotuberculosis O:2a exhibited only OPS with very short chain lengths, which is atypical of wzz ‐mutant phenotypes that have been observed for other species. We hypothesise that the Wzy polymerase of Y . pseudotuberculosis O:2a has a unique default activity in the absence of the Wzz, revealing the requirement of Wzz to drive O‐unit polymerization to greater lengths.