Inhibition of mycoplasma pneumoniae hemadsorption and adherence to respiratory epithelium by antibodies to a membrane protein.
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.
D018829:Adhesins, Bacterial; D000268:Adhesiveness; D000818:Animals; D000907:Antibodies, Bacterial / Q000502:physiology; D001426:Bacterial Proteins / Q000276:immunology / Q000502:physiology*; D002645:Chickens / Q000097:blood; D006224:Cricetinae; D006382:Hemadsorption; D008565:Membrane Proteins / Q000276:immunology / Q000502:physiology*; D009177:Mycoplasma pneumoniae / Q000378:metabolism / Q000502:physiology*; D009924:Organ Culture Techniques; D013936:Thymidine / Q000378:metabolism; D014132:Trachea / Q000382:microbiology*
D018829:Adhesins, Bacterial; D000907:Antibodies, Bacterial; D001426:Bacterial Proteins; D008565:Membrane Proteins; C035471:adhesin, Mycoplasma pneumoniae; D013936:Thymidine