Affiliation:
1. Department of Microbiology, The University of Texas Health Science Center at San Antonio, San Antonio, Texas 78284
Abstract
Antiserum and purified immunoglobulin directed against
Mycoplasma pneumoniae
membrane protein P1 were examined for their influence on mycoplasma viability, metabolism, and cytadsorption. Anti-P1 immunoglobulin inhibited adherence of
M. pneumoniae
to hamster tracheal rings in vitro by up to 80% and inhibited hemadsorption by greater than 90%. Cytadsorption was also inhibited by anti-P1 Fab fragments. Anti-P1 antibodies had no effect on
M. pneumoniae
viability or metabolism. The data indicate that anti-P1 antibody obstructs the interaction of
M. pneumoniae
adhesin P1 with its host receptors.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
86 articles.
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