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)

Post-proline hydrolytic-activity exists in various tissues and body fluids of human organism. Using electrophoretic techniques, column chromatographic methods and kinetic investigations two peaks of proteolytic activity towards glycyl-prolyl-p-nitroanilide were detected in human cerebrospinal fluid. The identity of one enzyme with dipeptidylpeptidase IV (EC 3.4.14.5) must now constitute proof of this. Among 650 patients with cerebral diseases, characterised by post-proline hydrolytic activity in cerebrospinal fluid, high enzyme activity coincide with bacterial meningitis. Furthermore, all bacteria which could be isolated from cerebrospinal fluid exhibit high activities of post-proline cleaving hydrolases. Until now, the origin of the cerebrospinal post proline hydrolytic activity is not clear, although our investigations suggested, that lymphocytes, cerebral parenchyma and bacteria may be involved in the enzyme secretion.
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PMID:[Post-proline hydrolysis activities in cerebrospinal fluid]. 278 47

This paper describes a gradient system for separating D- and L-isomers of Dns-amino acids by mixed chelate complexation through the addition of histidine methyl ester and copper sulfate to the mobile phase. Most of the biologically important amino acids were separated in a single analysis. With a simple solvent gradient consisting of increasing concentrations of acetonitrile in L-histidine methyl ester buffer all the common amino acids were resolved except cysteine and all optical isomers were resolved except those of threonine, alanine and proline. Analysis time was 90 min. Use of this system for determining non-protein amino acids in human cerebrospinal fluid showed the amino acids to be L-isomers, as expected. The pattern in fluid from a patient with bacterial meningitis was different from that of most of the others.
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PMID:Stereoselective D- and L-amino acid analysis by high-performance liquid chromatography. 673 58

IgA1 protease activity, which allows bacteria to cleave human IgA1 in the hinge region, represents a striking example of convergent evolution of a specific property in bacteria. Although it has been known since 1979 that IgA1 protease is produced by the three leading causes of bacterial meningitis in addition to important urogenital pathogens and some members of the oropharyngeal flora, the exact role of this enzyme in bacterial pathogenesis is still incompletely understood owing to lack of a satisfactory animal model. Cleavage of IgA1 by these post-proline endopeptidases efficiently separates the monomeric antigen-binding fragments from the secondary effector functions of the IgA1 antibody molecule. Several in vivo and in vitro observations indicate that the enzymes are important for the ability of bacteria to colonize mucosal membranes in the presence of S-IgA antibodies. Furthermore, the extensive cleavage of IgA sometimes observed in vivo, suggests that IgA1 protease activity results in a local functional IgA deficiency that may facilitate colonization of other microorganisms and the penetration of potential allergens. It has been hypothesized that IgA1 protease activity of Haemophilus influenzae, Neisseria meningitidis, and Streptococcus pneumoniae, under special immunological circumstances, allows these bacteria to take advantage of specific IgA1 antibodies in a strategy to evade other immune factors of the human body. The decisive factor is the balance between IgA antibodies against surface antigens of the respective bacteria and their IgA1 protease. Recent studies have shown that serine-type IgA1 proteases of H. influenzae, meningococci, and gonococci belong to a family of proteins used by a diverse group of Gram-negative bacteria for colonization and invasion.
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PMID:Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: critical evaluation of experimental evidence. 870 38