Abstract
The phoA gene technology was used to investigate secreted proteins of the intracellular pathogen Mycobacteriumn avium subspecies paratuberculosis. This led to the identification of sodC, a gene which codes for a copper and zinc cofactored superoxide dismutase (Cu,ZnSOD) which has been implicated as a virulence factor for some pathogens. The predicted protein possessed a 76% identity with Cu,ZnSOD of Mycobacterium tuberculosis. To characterize Cu,ZnSOD from M. avium subspecies paratuberculosis, the gene was cloned and overexpressed in Escherichia coli. The renatured, affinity-purified recombinant protein possessed enzymatic activity that was inhibited by the presence of cyanide, which is characteristic of a Cu,ZnSOD.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Alkaline Phosphatase / genetics
-
Alkaline Phosphatase / metabolism
-
Amino Acid Sequence
-
Animals
-
Base Sequence
-
Cloning, Molecular*
-
Escherichia coli / genetics
-
Escherichia coli / metabolism
-
Escherichia coli Proteins*
-
Gene Library*
-
Molecular Sequence Data
-
Mycobacterium avium subsp. paratuberculosis / enzymology*
-
Mycobacterium avium subsp. paratuberculosis / genetics
-
Paratuberculosis / microbiology
-
Recombinant Fusion Proteins / genetics
-
Recombinant Fusion Proteins / metabolism
-
Sequence Analysis, DNA
-
Superoxide Dismutase / chemistry
-
Superoxide Dismutase / genetics*
-
Superoxide Dismutase / metabolism*
Substances
-
Escherichia coli Proteins
-
Recombinant Fusion Proteins
-
Superoxide Dismutase
-
sodC protein, E coli
-
Alkaline Phosphatase