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
Cited by
64 articles.
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