Journal
FEMS MICROBIOLOGY LETTERS
Volume 189, Issue 2, Pages 135-141Publisher
ELSEVIER SCIENCE BV
DOI: 10.1111/j.1574-6968.2000.tb09219.x
Keywords
WbpA; dehydrogenase; WbpI; epimerase; O antigen; lipopolysaccharide; enterobacterial common antigen; Pseudomonas aeruginosa
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The O antigen unit of Pseudomonas aeruginosa serotype O5 is a complex trisaccharide containing 2-acetamido-3-acetiminido-2,3-dideoxy-beta-D-mannuronic acid, 2-acetimido-3-acetimido-2,3-dideoxy-beta-D-mannuronic acid, and 2-acetimido-2,6-deoxy-beta-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 (vffD) 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. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
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