Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0085437 (bacterial meningitis)
 4,038 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Thirty-seven strains of the genus Haemophilus and five strains of Streptococcus pneumoniae were examined for their ability to produce extracellular enzyme that cleaves immunoglobulin molecules. All strains of H. influenzae, H. aegyptius, and S. pneumoniae elaborated enzyme that selectively cleaved human immunoglobulin A1 (IgA1) myeloma proteins but was inactive against a variety of other proteins including human IgA2, IgG, and IgM, porcine and bovine secretory IgA, human and bovine serum albumins, and ovalbumin. Although susceptible, human secretory IgA remained largely undigested. Two strains of H. pleuropneumoniae isolated from fatally infected pigs cleaved porcine secretory IgA, but had no effect on human IgA proteins. None of 16 strains that belonged to nonpathogenic Haemophilus species produced IgA protease. Analyses of the cleavage products of human IgA1 and secretory IgA proteins by immunochemical methods, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and analytical ultracentrifugation revealed that Fab and Fc fragments were produced. Since the production of IgA1 protease by Neisseria meningitidis has been reported previously, our finding that H. influenzae and S. pneumoniae produce an IgA1 protease indicates that this is a property of all three major etiological agents of bacterial meningitis. This suggests that IgA1 protease production may be an important factor in the pathogenesis of this disease.
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PMID:Pathogenic species of the genus Haemophilus and Streptococcus pneumoniae produce immunoglobulin A1 protease. 4 Aug 78

Haemophilus influenzae type b is a major cause of bacterial meningitis and other invasive diseases in children under four years of age. One surface antigen, the type b capsular polysaccharide, polyribosylribitol phosphate (PRP), is a primary virulence factor of the organism. Antibody directed against PRP is protective; however, the purified polysaccharide is poorly immunogenic in young children. Polysaccharide-protein conjugate vaccines have been prepared which are significantly more immunogenic and efficacious in young children compared to the plain polysaccharide vaccine. Noncapsular surface antigens may also play a role in the virulence of H. influenzae. Some mutants (or phase variants) which differ in lipooligosaccharide (LOS) structure exhibit decreased virulence in the infant rat model of bacteremia. Proteins including the IgA protease, pili, a 98K outer membrane protein (OMP) as well as OMPs P1, P2 and P6 have also been examined in considerable detail, but whether they have a role in the virulence of the organism remains to be determined. However, antibody directed against the 98K OMP as well as P1, P2 and P6 is protective in the infant rat model of bacteremia. The role of antibody directed against LOS epitopes in protection is less clear, due at least in part, to phase variation in LOS antigens. Characterization of one surface antigen of H. influenzae type b, the capsular polysaccharide, already has led to the prevention of many cases of Haemophilus disease. Characterization of the noncapsular antigens together with a more detailed understanding of the mechanisms of virulence, most likely will permit development of even better vaccines, and possibly better treatment modalities, in the future.
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PMID:Haemophilus influenzae: surface antigens and aspects of virulence. 219 7