Abstract
The O antigen unit of Pseudomonas aeruginosa serotype O5 is a complex trisaccharide containing 2-acetamido-3-acetiminido-2,3-dideoxy-β- D-mannuronic acid, 2-acetimido-3-acetimido-2,3-dideoxy-β- D-mannuronic acid, and 2-acetimido-2,6-deoxy-β- D-galactosamine. Specific knockout mutations in the putative UDP- D- N-acetylglucosamine (UDP- D-GlcNAc) epimerase gene, wbpI, or the putative UDP- D- N-acetylmannosamine dehydrogenase gene, wbpA, resulted in strains that no longer produced B-band lipopolysaccharide, confirming the essential roles of these genes in B-band O antigen synthesis. Despite approximately 50% similarity of wbpI and wbpA to the Escherichia coli genes wecB ( rffE) and wecC ( rffD) involved in enterobacterial common antigen synthesis, cross-complementation experiments were not successful. These results imply that the P. aeruginosa UDP- D-GlcNAc precursor may be di- N-acetylated prior to further modification, preventing the E. coli enzymes from recognizing it as a substrate.
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