Cloning, expression, and occurrence of the Brucella Cu-Zn superoxide dismutase

Author:

Bricker B J1,Tabatabai L B1,Judge B A1,Deyoe B L1,Mayfield J E1

Affiliation:

1. National Animal Disease Center, U.S. Department of Agriculture, Ames, Iowa 50010.

Abstract

Recently, the complete amino acid sequence of a protein expressed in Escherichia coli from cloned Brucella abortus DNA was reported. On the basis of amino acid homology, this protein was identified as a copper-zinc superoxide dismutase (Cu-Zn SOD) (B. L. Beck, L. B. Tabatabai, and J. E. Mayfield, Biochemistry 29:372-376, 1990). We demonstrate in this paper that the sequenced protein is the same as the previously studied salt-extractable protein BCSP20. The plasmid-encoded protein expressed from recombinant E. coli is identical to the Brucella-derived BCSP20 in molecular mass, N-terminal amino acid sequence, and cross-reactivity with homologous and heterologous rabbit sera against either the recombinant gene product or the Brucella-derived protein. A survey of the expression of the Cu-Zn SOD protein in Brucella biovars representing all species was done by Western blotting (immunoblotting) using antisera raised against the recombinant E. coli-derived protein. With the exception of B. neotomae and B. suis biovar 2, the Cu-Zn SOD protein was detectable in all Brucella species and biovars tested, including eight biovars of B. abortus.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference16 articles.

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3. Conservation of antigenicity in a 31-kDa Brucella protein;Bricker B. J.;Vet. Microbiol.,1988

4. The interaction of Brucella cell surface components with plant agglutinins;Corbel M. J.;Dev. Biol. Stand.,1984

5. Isolation of microgram quantities of proteins from polyacrylamide gels for amino acid sequence analysis;Hunkapillar M. W.;Methods Enzymol.,1983

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