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https://hdl.handle.net/2440/11567
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Type: | Journal article |
Title: | A putative pathway for perosamine biosynthesis is the first function encoded within the rfb region of Vibrio cholerae O1 |
Author: | Stroeher, U. Karageorgos, L. Brown, M. Morona, R. Manning, P. |
Citation: | Gene, 1995; 166(1):33-42 |
Publisher: | Elsevier |
Issue Date: | 1995 |
ISSN: | 0378-1119 1879-0038 |
Statement of Responsibility: | Stroeher, Uwe H. ; Karageorgos, Litsa E. ; Brown, Melissa H. ; Morona, Renato ; Manning, Paul A. |
Abstract: | The first four genes (rfbA,B,D,E) of the rfb region of Vibrio cholerae O1 are predicted to encode the enzymes required for the biosynthesis of perosamine, which constitutes the backbone structure of the O-antigen of the lipopolysaccharide. Based on homology to known proteins/protein families, the following functions are predicted: RfbA, phosphomannose isomerase-guanosine diphosphomannose pyrophosphorylase; RfbB, phosphomanno-mutase; RfbD, oxido reductase and RfbE, perosamine synthetase (amino-transferase). Thus, perosamine is synthesized from fructose 6-phosphate via the intermediates mannose 6-phosphate by RfbA, to mannose 1-phosphate by RfbB, to GDP-mannose by RfbA, to GDP-4-keto-6-dideoxymannose by RfbD and to GDP-perosamine by RfbE. This final product would then serve as the substrate for the addition of the tetronate, which could then be polymerized into the O-antigen for transfer to the lipid A plus core oligosaccharide and export to the cell surface. The organization of these genes are such that one would expect them to be translationally coupled as part of the rfb operon. However, the absence of readily detectable promoter sequences suggests low levels of transcription, in line with other studies. The nucleotide sequence of these genes is absolutely conserved in the two isolates 569B (classical, Inaba) and O17 (El Tor, Ogawa) which were expected to show maximal sequence variation. This suggests very tight constraints on the micro-evolution within these sequences. |
Keywords: | Vibrio cholerae Multienzyme Complexes Mannose-6-Phosphate Isomerase Phosphotransferases (Phosphomutases) Carbohydrate Epimerases Hydro-Lyases Oxidoreductases Transaminases Nucleotidyltransferases Mannose O Antigens Bacterial Proteins Recombinant Proteins DNA, Bacterial Restriction Mapping Sequence Alignment Binding Sites Amino Acid Sequence Base Sequence Regulatory Sequences, Nucleic Acid Sequence Homology, Amino Acid Genes, Bacterial Operon Molecular Sequence Data |
DOI: | 10.1016/0378-1119(95)00589-0 |
Published version: | http://dx.doi.org/10.1016/0378-1119(95)00589-0 |
Appears in Collections: | Aurora harvest 7 Microbiology and Immunology publications |
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