Virulent human strains of group G streptococci express a C5a peptidase enzyme similar to that produced by group A streptococci

Author:

Cleary P P1,Peterson J1,Chen C1,Nelson C1

Affiliation:

1. Department of Microbiology, University of Minnesota, Minneapolis 55455.

Abstract

Specific proteolytic destruction of the human chemotaxin, C5a, is a property of group A and B streptococcal pathogens. Here we show that virulent group G streptococci from human sources also express C5a peptidase activity. The enzyme responsible for this activity is approximately the same size as and is antigenically similar to that produced by group A streptococci. On the basis of Southern hybridization analysis with an internal fragment of the group A C5a peptidase gene (scpA) as a probe, a copy of this gene was found in the genome of all group G human isolates tested. Comparison of partial restriction maps of scpA and scpG revealed significant similarity between the two genes. Group G strains isolated from dogs and cows were found to lack C5a peptidase activity and did not hybridize to the scpA-specific probe. The association of this activity with three streptococcal species suggests that elimination of phagocyte chemotactic attractants is a more universal virulence mechanism than originally anticipated.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference26 articles.

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2. M proteins of group G streptococci isolated from bacteremic human infections;Bisno A. L.;Infect. Immun.,1986

3. Streptococcal protein G expressed by streptococci or by Escherichia coli, has separate binding sites for human albumin and IgG;Bjorck L.;Mol. Immunol.,1987

4. Complete nucleotide sequence of the streptococcal C5a peptidase gene of Streptococcus pyogenes;Chen C.;J. Biol. Chem.,1990

5. Cloning and expression of the streptococcal C5a peptidase gene in Escherichia coli: linkage to the type 12 M protein gene;Chen C. C.;Infect. Immun.,1989

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