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PMID: 8529891 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

A putative pathway for perosamine biosynthesis is the first function encoded within the rfb region of Vibrio cholerae O1.

Gene ·Vol. 166 ·No. 1 ·1995-12-01 ·Pages 33-42

Stroeher UH, Karageorgos LE, Brown MH, Morona R, Manning PA

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.

MeSH Terms
Amino Acid Sequence Bacterial Proteins Base Sequence Binding Sites Carbohydrate Epimerases/genetics,metabolism DNA, Bacterial/genetics Genes, Bacterial Hydro-Lyases/genetics,metabolism Mannose/analogs & derivatives,biosynthesis Mannose-6-Phosphate Isomerase/genetics,metabolism Molecular Sequence Data Multienzyme Complexes/metabolism Nucleotidyltransferases/genetics,metabolism O Antigens/biosynthesis Operon Oxidoreductases/genetics,metabolism Phosphotransferases (Phosphomutases)/genetics Recombinant Proteins/chemistry Regulatory Sequences, Nucleic Acid Restriction Mapping Sequence Alignment Sequence Homology, Amino Acid Transaminases/genetics,metabolism Vibrio cholerae/enzymology,genetics,immunology
Chemicals
Bacterial Proteins DNA, Bacterial Multienzyme Complexes O Antigens Recombinant Proteins phosphomannose isomerase-guanosine diphospho-D-mannose pyrophosphorylase 4-amino-4,6-dideoxy-D-mannose Oxidoreductases Transaminases Nucleotidyltransferases dTDP-D-glucose synthase Hydro-Lyases dTDPglucose 4,6-dehydratase Carbohydrate Epimerases perosamine synthetase dTDP-4-ketorhamnose 3,5-epimerase Mannose-6-Phosphate Isomerase Phosphotransferases (Phosphomutases) phosphomannomutase Mannose
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Stroeher U H
Department of Microbiology and Immunology, University of Adelaide, Australia.
Karageorgos L E
Brown M H
Morona R
Manning P A
Article Info
Journal
Gene
Abbr.
Gene
ISSN
0378-1119
Published
1995-12-01
Pages
33-42
Language
English
Region
Netherlands
NLM ID
7706761
Subset
IM
Databases
GENBANK
A38598, C40630, L04596, L17071, L23941, P14167, P15263, P23054, P24174, P24175, P25048, P25177, P26276, P26340, P26341, P26391, P26397, P26404, P26405, P27833, P29955, P29956, Q01410, Q01411, S22621, S30187, U02489, U02490, X59554, X73124
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