Proteolytic action of Legionella pneumophila on human serum proteins.
Proteolysis by four strains of Legionella pneumophila, the etiological agent of Legionnaires disease, was studied by the method of immunoelectrophoresis. Twenty-three human serum proteins were tested as substrates. Five proteins were degraded: alpha 1-acid glycoprotein, alpha 1-antichymotrypsin, beta-lipoprotein, beta 1E-globulin, and beta 2-glycoprotein-I. Moreover, the degradation of alpha 1-antichymotrypsin was demonstrated by investigation of an enzyme-blocking test. It is suggested that the proteolytic activity of L. pneumophila may bear some relationship to its pathogenic activity.
D001419:Bacteria / Q000378:metabolism* / Q000472:pathogenicity; D001798:Blood Proteins / Q000378:metabolism*; D006801:Humans; D007877:Legionnaires' Disease / Q000382:microbiology*; D010447:Peptide Hydrolases / Q000378:metabolism*
D001798:Blood Proteins; D010447:Peptide Hydrolases