Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023241 (Legionella)
 6,990 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ability of proteolysis by four stains of L. pneumophila the etiologic agent of the Legionnaires' Disease was studied by the method of immunoelectrophoresis. 18 human serum proteins were tested as substrates (Table 1). Four proteins were degraded: alpha 1-acid glycoprotein (Fig. 1), alpha 1-antichymotrypsin (Fig. 2), beta-lipoprotein (Fig. 3), and beta 2-glycoprotein-I (Fig. 4). It can be suggested that the pathogenic action of L. pneumophila is due to that enzymatic activity, especially since alpha 1-acid glycoprotein, alpha 1-antichymotrypsin and beta 2-glycoprotein-I belong to the acute phase proteins and also beta-lipoprotein is involved in the unspecific resistance of the organism against infections.
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PMID:[The action of proteolytic enzymes of Legionella pneumophila on human serum proteins (author's transl)]. 615 12

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.
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PMID:Proteolytic action of Legionella pneumophila on human serum proteins. 698 77