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Query: UMLS:C0348321 (Haemophilus)
 15,372 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

The nonencapsulated, IgA protease-positive Haemophilus influenzae strain Rd and serogroup b clinical isolates were found to proliferate in human milk. Growth did not require supplemental X and V factors. In milk, strain Rd synthesized IgA protease, but it was completely inhibited by antibody, so secretory IgA in milk cultures remained intact. Inhibition was largely attributable to IgA1 antibodies. Rd cells also aggregated during growth in milk and showed colony size variation, whereas a protease-negative mutant of Rd (Rd225DK) aggregated less and had uniform colony size. Like differences in protease inhibition, these differences in growth pattern were mediated by secretory IgA1. Thus, milk antibody not only inhibited the extracellular protease but also interacted directly with the enzyme precursor or related antigens on growing bacterial cells. This self-protective property of milk secretory IgA may be an important immunologic attribute for the upper respiratory mucosa of the infant.
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PMID:Growth of Haemophilus influenzae in human milk: synthesis, distribution, and activity of IgA protease as determined by study of iga+ and mutant iga- cells. 160 7

The amino acid sequence T-P-P-T-P-S-P-S is tandemly duplicated in the heavy chain of human immunoglobulin A1 (IgA1), the major antibody in secretions. The bacterial pathogen Streptococcus sanguis, a precursor to dental caries and a cause of bacterial endocarditis, yields IgA protease that cleaves only the Pro-Thr peptide bond in the left duplication, while the type 2 IgA proteases of the genital pathogen Neisseria gonorrhoeae and the respiratory pathogen Haemophilus influenzae cleave only the P-T bond in the right half. We have sequenced the entire S. sanguis iga gene cloned into Escherichia coli. A segment consisting of 20 amino acids tandemly repeated 10 times, of unknown function, occurs near the amino-terminal end of the enzyme encoded in E. coli. Identification of a predicted zinc-binding region in the S. sanguis enzyme and the demonstration that mutations in this region result in production of a catalytically inactive protein support the idea that the enzyme is a metalloprotease. The N. gonorrhoeae and H. influenzae enzymes were earlier shown to be serine-type proteases, while the Bacteroides melaninogenicus IgA protease was shown to be a cysteine-type enzyme. The streptococcal IgA protease amino acid sequence has no significant homology with either of the two previously determined IgA protease sequences, that of type 2 N. gonorrhoeae and type 1 H. influenzae. The differences in both structure and mechanism among these functionally analogous enzymes underscore their role in the infectious process and offer some prospect of therapeutic intervention.
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PMID:Analysis of the immunoglobulin A protease gene of Streptococcus sanguis. 198 65

The alpha-aminoboronic acid analog of proline has been synthesized and incorporated into a number of peptides as the COOH-terminal residue. These peptide prolyl boronic acids are potent inhibitors of both the type 1 and type 2 IgA proteinases from Neisseria gonorrhoeae and Hemophilus influenzae, but not of the functionally similar IgA proteinase from Streptococcus sanguis. The best inhibitors synthesized thus far have Ki values in the nanomolar range (4.0 to 60 nM). These results indicate that the N. gonorrhoeae and the H. influenzae enzymes belong to the serine protease family of proteolytic enzymes while that from S. sanguis does not. As a group, the IgA proteinases have been noted for their remarkable specificity; thus, the peptide prolyl boronic acids reported here are the first small synthetic molecules to exhibit a relatively high affinity for the active site of an IgA proteinase and are therefore the first to yield some insight into the active site structure and specificity requirements of these enzymes.
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PMID:Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus influenzae by peptide prolyl boronic acids. 210 53

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

Secretion of immunoglobulin A1 (IgA1) proteases is a characteristic of Haemophilus influenzae and several other bacterial pathogens causing infectious diseases, including meningitis. Indirect evidence suggests that the proteases are important virulence factors. In this study, we cloned the iga gene encoding immunoglobulin A1 (IgA1) protease from H. influenzae serotype b into Escherichia coli, in which the recombinant H. influenzae iga gene was expressed and the resulting protease was secreted. Sequencing a part of a 7.5-kilobase DNA fragment containing the iga gene revealed a large open reading frame with a strongly biased codon usage and having the potential of encoding a protein of 1,541 amino acids and a molecular mass of 169 kilodaltons. Putative promoter and terminator elements flanking the open reading frame were identified. Comparison of the deduced amino acid sequence of this H. influenzae IgA1 protease with that of a similar protease from Neisseria gonorrhoeae revealed several domains with a high degree of homology. Analogous to mechanisms known from the N. gonorrhoeae IgA protease secretion, we propose a scheme of posttranslational modifications of the H. influenzae IgA1 protease precursor, leading to a secreted protease with a molecular mass of 108 kilodaltons, which is close to the 100 kilodaltons reported for the mature IgA1 protease.
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PMID:Cloning and sequencing of the immunoglobulin A1 protease gene (iga) of Haemophilus influenzae serotype b. 250 30

IgA protease produced by various strains of Haemophilus influenzae can digest serum IgA and yield its fragments which can react with anti-IgA serum. We assayed IgA protease activity by detecting the digests of IgA by SDS-PAGE and immunoblotting. The digests were separated with SDS-PAGE, transferred to nitrocellulose membranes and detected with anti- (alpha chain of human IgA, its Fab and its Fc) immunoglobulin conjugated peroxidases. Using this method, we can determine which type of IgA protease is produced by various of H. influenzae strains. All the 20 strains isolated from respiratory tracts produced IgA protease.
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PMID:Detection of IgA protease from Haemophilus influenzae by immunoblotting. 267 Jun 4

Monoclonal IgA paraproteins of subclasses 1 and 2, isolated from the sera of myeloma patients, were incubated for 4, 24, 48 and 72 hours with B. pertussis, B. parapertussis, B. bronchiseptica cultures, as well as Haemophilus influenzae strain. The fragmentation of IgA was studied by immunielectrophoresis with antisera to alpha-chain, to Fab alpha + Fc alpha, to Fab alpha and with antisera to light chains corresponding to the type of paraprotein. B. pertussis and B. parapertussis were found to have subclass-unspecific IgA protease which splitted off a cathode fragment, similar to Fab-fragment and, probably, corresponding to the variable domain of alpha-chain (Fv), after 48-hour incubation. Similar IgA protease was detected in H. influenzae, found to have classical IgA1 protease as well. All Bordetella species under study splitted off anode components from IgA paraproteins of both subclasses. These components, containing the determinants of heavy and light IgA chains, were either IgA - alpha I-antitrypsin complexes or some IgA fragments with high electrophoretic motility. None of the strains under study splitted monoclonal IgG.
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PMID:[IgA protease activity of microbes in the genus Bordetella]. 286 69

Haemophilus influenzae are small, gram-negative, rod-shaped bacteria. Because of their special growth requirements, they do not grow on usual blood agar media, but flourish on the mucosal membranes of the human respiratory tract where they adhere to the epithelial cells by fimbriae (a potential vaccine component). Nasopharyngeal carriage of Haemophilus influenzae is very common, and in healthy carriers the bacteria are usually unencapsulated. The outer membrane of Haemophilus influenzae contains lipopolysaccharide (of so called R form, without O antigen) and major outer membrane proteins. The lipopolysaccharide is a virulence determinant. An extracellular enzyme, IgA protease, is another potential virulence determinant. The outer membrane of Haemophilus influenzae is a rather ineffective barrier towards antibiotics, and thus the major determinants of antibacterial resistance in Haemophilus influenzae are plasmid-coded enzymes that inactivate the antibiotic, and changes in the target molecules.
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PMID:Unencapsulated Haemophilus influenzae--what kind of pathogen? 290 69

It has previously been shown that secretory immunoglobulin A (S-IgA) influences the sorption of oral streptococci to hydroxyapatite as well as to cell surfaces. The present experiments demonstrate that bacterial IgA proteases, which cleave S-IgA in the hinge region, are capable of interfering with this mechanism. This result was obtained with an IgA1 specific protease from Haemophilus influenzae and with a protease from Clostridium ramosum that cleaves IgA1 as well as IgA2 of A2m(1) allotype. The modulation of S-IgA-mediated effects by IgA proteases were studied by means of an in vitro method which permits quantitative determination of the sorption of radiolabeled oral bacteria to hydroxyapatite beads. Other authors have suggested that IgA protease-mediated effects may be explained by a strongly reduced antigen-binding capacity of released Fab alpha fragments. Here we present evidence that streptococci, after exposure to specific S-IgA and IgA protease, are coated with Fab alpha fragments.
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PMID:Interference of IgA protease with the effect of secretory IgA on adherence of oral streptococci to saliva-coated hydroxyapatite. 304 Aug 26


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