Molecular cloning of a Coxiella burnetii gene encoding a macrophage infectivity potentiator (Mip) analogue
Article Abstract:
The open reading frame of the Coxiella burnetii gene encodes a protein which is homologous to the macrophage infectivity potentiator (Mip) encoded by Legionella pneumophila (LpMip) and Chlamydia trachomatis Mip. The C. burnetii CbMip protein reacts with antibodies against LpMip. CbMip is probably a virulence factor of the pathogenic bacteria. The C-terminal of the protein is similar to the FK506-binding proteins present in prokaryotes and eukaryotes. CbMip overexpressed in Escherichia coil demonstrates peptidyl-prolyl cis-trans isomerase activity.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Secretion of proteins by Coxiella burnetii
Article Abstract:
Incubation of viable Coxiella burnetii organisms in host-cell-free medium at low pH leads to translocation of proteins secreted by the bacteria to the exterior of the cell. Three polypeptides with molecular masses of 34, 24 and 12 kDa are the major constituents of the exported protein. A membrane fraction has the de novo-synthesized proteins. The physiological process of protein transport is inhibited by dicylohexylcarbodiimide and carbonyl cyanide m-chlorophenylhydrazone.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Involvement of outer-membrane proteins in the aggregation of Azospirillum brasilense
Article Abstract:
A study was conducted to analyze the biological factors involved in the aggregation of Azospirillum brasilense strain CD. The cells were grown under aggregation-inducing and non-aggregation-inducing environments. They were then washed by centrifugation and resuspended in a potassium phosphate buffer solution. Results indicated that outer-membrane proteins are involved in the aggregation process of cells of A brasilense.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1999
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