Open AccessThe wavB gene of Vibrio cholerae and the waaE of Klebsiella pneumoniae codify for a β‐1,4‐glucosyltransferase involved in the transfer of a glucose residue to the l ‐glycero‐ d ‐manno‐heptose I in the lipopolysaccharide inner core
Author(s) -
Izquierdo Luis,
Merino Susana,
Coderch Nuria,
Regué Miguel,
Tomás Juan M
Publication year - 2002
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/j.1574-6968.2002.tb11437.x
Subject(s) - vibrio cholerae , klebsiella pneumoniae , complementation , microbiology and biotechnology , mutant , biology , heptose , lipid a , serratia marcescens , escherichia coli , campylobacter jejuni , glucosyltransferase , lipopolysaccharide , gene , bacteria , biochemistry , genetics , endocrinology
Vibrio cholerae WavB protein showed some similarity to WaaE of Klebsiella pneumoniae and Serratia marcescens . From previous data obtained by us and by chemical analyses of a K. pneumoniae non‐polar waaE mutant from strain 889 (08:K69), its lipopolysaccharide (LPS) core structure has recently been elucidated. We demonstrated that WaaE is a β‐1,4‐glucosyltransferase involved in the transfer of a glucose residue to the l ‐glycero‐ d ‐manno‐heptose I in the LPS inner core. Complementation of this K. pneumoniae non‐polar waaE mutant with gene wavB obtained, either from V. cholerae or V. mimicus , showed a full complementation either by chemical studies or by a biological test (susceptibility to non‐immune serum). The V. cholerae wavB gene is located in a putative core oligosaccharide (OS) gene cluster and the V. cholerae OS core structure showed the same β‐1,4‐glucose residue attached to Hep I as is observed for the K. pneumoniae 889 OS core structure. No other glucose residue is found in the ligosaccharide core structure of K. pneumoniae 889. We concluded that WavB protein is able to perform the same function as WaaE.