Role of the viaB locus in synthesis, transport and expression of Salmonella typhi Vi antigen
Article Abstract:
The viaB locus encodes proteins that participate in the synthesis of Vi polymer, translocation of the polymer to the bacterial cell surface and the control of expression of the Vi antigen in Salmonella (S.) typhi. The Vi antigen is a polysaccharide expressed in S. typhi that causes typhoid fever in humans. The viaB locus has 11 genes, tviA to tviE, vexA to vexE and ORF11. The TviB and TviC polypeptides catalyze the synthesis of Vi antigen. The proteins encoded by the vexA, vexB and vexC genes take part in the transport of the antigen to the bacterial surface.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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An antigenic protein gene of a phytoplasma associated with sweet potato witches' broom
Article Abstract:
The genome of the phytoplasma associated with sweet potato witches' broom was screened identify the gene encoding its major antigenic protein. The predicted gene product is a protein consisting of 172 amino acid residues with an estimated molecular mass of 19.15 kiloDalton. Sequences proximal to the promoter and terminator regions were similar to those found among prokaryotic organisms. This major antigenic protein bears significant homology with that of peanut witches' broom-associated phytoplasma.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
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Homologous regions of the Salmonella enteritidis virulence plasmid and the chromosome of Salmonella typhi encode thiol: disulphide oxidoreductases belonging to the DsbA thioredoxin family
Article Abstract:
Southern blot hybridization was used to characterize the hybridizing region of the Salmonella typhi chromosome. Small plasmid-derived DNA probes were used to analyze the nucleotide sequence similarity between the virulence plasmid of Salmonella enteriditis strain 82139 and the chromosomal DNA of Salmonella typhi. Motif of an identified ORF revealed that it was present in the active site of the DsbA family of thiol:disulphide oxidoreductase proteins.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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