The Klebsiella pneumoniae wabG Gene: Role inBiosynthesis of the Core Lipopolysaccharide andVirulence

ABSTRACT To determine the function of the wabG gene in the biosynthesis of the core lipopolysaccharide (LPS) of Klebsiella pneumoniae , we constructed wabG nonpolar mutants. Data obtained from the comparative chemical and structural analysis of LPS samples obtained from the wild type, the mutant str...

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Published inJournal of bacteriology Vol. 185; no. 24; pp. 7213 - 7221
Main Authors Izquierdo, Luis, Coderch, Núria, Piqué, Nuria, Bedini, Emiliano, Corsaro, Maria Michela, Merino, Susana, Fresno, Sandra, Tomás, Juan M., Regué, Miguel
Format Journal Article
LanguageEnglish
Published 15.12.2003
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Summary:ABSTRACT To determine the function of the wabG gene in the biosynthesis of the core lipopolysaccharide (LPS) of Klebsiella pneumoniae , we constructed wabG nonpolar mutants. Data obtained from the comparative chemical and structural analysis of LPS samples obtained from the wild type, the mutant strain, and the complemented mutant demonstrated that the wabG gene is involved in attachment toα - l -glycero- d -manno-heptopyranose II ( l , d -Hep p II) at the O-3 position of anα - d -galactopyranosyluronic acid (α- d -GalA p ) residue. K. pneumoniae nonpolar wabG mutants were devoid of the cell-attached capsular polysaccharide but were still able to produce capsular polysaccharide. Similar results were obtained with K. pneumoniae nonpolar waaC and waaF mutants, which produce shorter LPS core molecules than do wabG mutants. Other outer core K. pneumoniae nonpolar mutants in the waa gene cluster were encapsulated. K. pneumoniae waaC , waaF , and wabG mutants were avirulent when tested in different animal models. Furthermore, these mutants were more sensitive to some hydrophobic compounds than the wild-type strains. All these characteristics were rescued by reintroduction of the waaC , waaF , and wabG genes from K. pneumoniae .
ISSN:0021-9193
1098-5530
DOI:10.1128/JB.185.24.7213-7221.2003