Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two primer sets were chosen for the detection of Haemophilus influenzae in cerebrospinal fluid by polymerase chain reaction (PCR) DNA amplification. One primer set was selected from sequences encoding a capsulation-associated protein and reacted with target DNA from all 15 capsulate H. influenzae strains (all serotypes) examined. The other primer set was selected from the DNA sequence of a gene encoding for outer-membrane protein P6 and reacted with the 15 capsulate and 10 non-capsulate strains of H. influenzae tested. This primer set also reacted with the closely related species H. haemolyticus and H. aegyptius, and with two of nine H. parainfluenzae strains. In reconstruction experiments, PCR DNA amplification was able to detect as few as five H. influenzae cells when 40 cycles of amplification were used. Two hundred cerebrospinal fluid (CSF) samples collected consecutively from patients suffering from meningitis were investigated by PCR; 40 were culture-positive for H. influenzae and 39 of these were also clearly positive in the PCR test with both primer sets. Contamination occurred to some extent with 40 cycles of amplification but was completely eliminated when the number of cycles was reduced to 35. We conclude that the two primer sets are appropriate for the detection of H. influenzae by PCR, each having its own specificity. When these two primer sets are used, PCR is a technique of equivalent sensitivity to culture for the detection of H. influenzae in CSF.
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PMID:Detection of Haemophilus influenzae in cerebrospinal fluids by polymerase chain reaction DNA amplification. 225 14

The outer-membrane protein (OMP) profiles of four isolates of Haemophilus paragallinarum (0083, 0222, Modesto, and HP31) were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. OMPs were isolated by sonic disruption followed by differential centrifugation and selective solubilization in Triton X-100. Although the isolates had similar profiles overall, two distinct OMP profile types, based on the variable molecular weight of a protein termed OMP C (39,000 or 38,000), were found. In addition, OMP C was found to be a heat-modifiable protein--being either absent or present in only minor amounts if the preparations were not heated at 100 C. Major and minor OMPs, some common to all four isolates, were recognized in immunoblots by an immune serum to isolate HP31.
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PMID:Outer-membrane proteins of Haemophilus paragallinarum. 228 17

A 78-kilodalton (kDa) outer membrane protein (OMP) of Haemophilus somnus was one of the two antigens most consistently and most intensely immunoreactive in Western immunoblots of whole cells of H. somnus reacted with convalescent-phase serum obtained from cattle with experimental H. somnus pneumonia. This antigen was isolated by gel filtration chromatography of sodium dodecyl sulfate-solubilized OMP. Reactions of Western blots with bovine monospecific antiserum prepared against the 78-kDa antigen indicated that this 78-kDa OMP was present in each of 22 isolates of H. somnus obtained from cattle with pneumonia, thromboembolic meningoencephalitis, and abortion as well as from vaginal or preputial carriers. The 78-kDa OMP was also present in each isolate obtained weekly throughout the course of experimental H. somnus pneumonia in a calf. Monospecific antiserum to the 78-kDa OMP also reacted with proteins from closely related bacterial species in the family Pasteurellaceae but not with bacteria of 13 other genera. The 78-kDa OMP of H. somnus is of interest because it is surface accessible, highly conserved, immunogenic, cross-reactive with other members of the family Pasteurellaceae, and reactive with convalescent-phase serum which is passively protective against H. somnus pneumonia.
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PMID:Characterization of a 78-kilodalton outer membrane protein of Haemophilus somnus. 229 52

To analyze whether exacerbations in chronic obstructive pulmonary disease (COPD) coincide with reinfection by Haemophilus influenzae, 16 COPD patients were studied longitudinally for 3 years. Exacerbations coincided with reinfection by H. influenzae, either endogenous, by a strain with a DNA fingerprint indistinguishable from the strain previously present but with another major outer membrane protein (MOMP) pattern (2 patients), or exogenous, by a strain with a different DNA fingerprint and MOMP pattern (3 patients). The other patients, remaining in an infectious state without clear exacerbations for longer periods, were persistently infected by a particular H. influenzae strain (median persistence time, 5.5 months; range, 2-23 months). Of 8 antibiotic-treated patients, 7 remained infected by H. influenzae with the same DNA fingerprint, although all strains were sensitive to the antibiotics prescribed. Results of the study suggested that exacerbations in COPD patients coincide with endogenous or exogenous reinfection by H. influenzae, persistently infected patients keep the same H. influenzae strain for longer periods, and antibiotic treatment was not effective in eradicating H. influenzae.
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PMID:Endogenous and exogenous reinfections by Haemophilus influenzae in patients with chronic obstructive pulmonary disease: the effect of antibiotic treatment on persistence. 231 30

Porphyrin ring source appears to alter the outer membrane protein (OMP) profile of some, but not all, non-typable (NT) Haemophilus influenzae strains isolated from sputum. When haemin was replaced with protoporphyrin IX, 41% of strains examined produced increased amounts of a polypeptide of 84 Kda and new OMPs of either 120 or 150 Kda. Immunoblotting with paired patient's sera revealed that antibodies reactive with these proteins were present, demonstrating OMP antigenicity and expression in vivo and indicating that these isolates of NT H. influenzae may display an altered OMP phenotype when growing in the human lung.
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PMID:Porphyrin ring source can alter the outer membrane protein profile of non-typable Haemophilus influenzae. 231 82

Using idiotypic analysis, we examined the variable (V) region diversity of human antibodies specific for the capsular polysaccharide of Haemophilus influenzae b (Hib PS). A goat anti-idiotypic serum (anti-Id) was prepared against anti-Hib PS antibodies isolated from the serum of an adult immunized with Hib PS. The anti-Id bound donor anti-Hib PS antibodies and inhibited Hib PS binding of donor anti-Hib PS. In contrast, the anti-Id did not bind donor or pooled Ig depleted of Hib PS antibodies, nor did it inhibit antigen binding of human antibodies to pneumococcal PS's, meningococcal A PS or diphtheria toxoid. Crossreactive idiotype (CRI), as measured by anti-Id inhibition of Hib PS binding, was found in 74 of 98 subjects (76%) vaccinated with Hib PS at 1.7-57 yr of age. 60 of these 74 subjects had greater than 50% of their serum Hib PS-binding activity inhibited by anti-Id. No correlation was found between age and CRI expression. In subjects showing both IgG1 and IgG2 antibody responses, CRI was most frequently detected in both subclasses (71% of subjects). CRI was limited to either IgG1 or IgG2 in 19% of subjects, a finding suggestive of independent B cell lineages. 13 of 15 infants less than 17 mo of age, who responded to Hib PS-outer membrane protein conjugate vaccine, had greater than 50% of their serum anti-Hib PS antibody activity inhibited by anti-Id. The ability of native Hib PS and Hib PS oligomer to partially inhibit (60 and 35%, respectively) the binding between anti-Id and heterologous anti-Hib PS, indicated that some CRI determinants are in or near the combining site. In summary, our findings demonstrate a highly penetrant and frequently predominant CRI, which is expressed in both infants and adults. The results underscore the limited V region diversity of anti-Hib PS antibodies and indicate that CRI predominance is manifest early in ontogeny and is induced by both TI and TD forms of the Hib PS antigen.
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PMID:A major crossreactive idiotype associated with human antibodies to the Haemophilus influenzae b polysaccharide. Expression in relation to age and immunoglobulin G subclass. 231 71

To assess the immunogenicity of HIB vaccines in patients in whom hepatoportoenterostomies were performed for biliary atresia, eight such children received Haemophilus influenzae type b-polyribosylribitol phosphate (HIB-PRP) vaccine and had pre- and postvaccination total serum anti-PRP antibody concentrations determined by radioimmunoassay. Preimmunization anti-PRP antibody levels ranged from less than 0.125 to 0.40 microgram/ml [geometric mean antibody titer (GMT) 0.106 microgram/ml], while postvaccination levels ranged from 0.161 to 1.192 micrograms/ml (GMT = 0.489 microgram/ml). Five children who did not achieve postimmunization anti-PRP antibody levels greater than 1.0 microgram/ml received 15 micrograms of either PRP coupled to diphtheria toxoid (PRP-D) or PRP coupled to an outer membrane protein complex of Neisseria meningitidis group B (PRP-NOMP) conjugate vaccine. Anti-PRP antibody levels 1 month after immunization with HIB conjugate vaccines ranged from 1.51 to 10.35 micrograms/ml (GMT = 3.386 micrograms/ml). Patients with extrahepatic biliary atresia and hepatoportoenterostomies who previously received the HIB-PRP vaccine should be revaccinated with PRP protein conjugate vaccines to ensure adequate protection against H. influenzae type b disease.
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PMID:Immunogenicity of Haemophilus influenzae type B vaccines in children with hepatoportoenterostomies. 239 59

The major outer membrane proteins of Haemophilus influenzae type b (Hib), designated P5 and P6 (R.S. Munson, Jr., J.L. Shenep, S.J. Barenkamp, and D.M. Granoff, J. Clin. Invest. 72:677-684, 1983), were purified to homogeneity and partially characterized. P5 was insoluble in octylglucoside-NaCl and could be extracted with 1% sodium dodecyl sulfate (SDS) in 20 mM phosphate (pH 7.5). Solubilized P5 was further purified on hydroxylapatite in 0.1% SDS. The purified protein had an apparent molecular weight of 27,000 as determined by SDS-polyacrylamide gel electrophoresis after sample preparation at room temperature. The protein migrated with an apparent molecular weight of 35,000 after heating for 30 min at 100 degrees C in the presence of 10% beta-mercaptoethanol (beta ME). Rabbit antisera prepared against the purified preparation immunoprecipitated solubilized protein P5 but had no protective activity in the infant rat bacteremic model. The SDS-insoluble residue was further extracted with 1% SDS-0.5 M NaCl-0.1% beta ME at 37 degrees C. A single outer membrane protein, designated P6, with an apparent molecular weight of 16,000, remained insoluble under these conditions. Antiserum prepared against this insoluble fraction contained antibodies which, after removal of anti-lipopolysaccharide antibody, immunoprecipitated P6 and protected infant rats challenged with Hib. Protein P6 could be released from the insoluble cell wall in the presence of SDS-NaCl-beta ME at 60 degrees C. Thus, proteins P5 and P6 could be purified from the cell envelope of Hib. Based on the results from infant rat passive protection experiments, antigens in the P6-cell wall fraction merit further investigation as possible vaccine components. In contrast, epitopes on protein P5 did not appear to elicit protective antibody.
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PMID:Purification and partial characterization of outer membrane proteins P5 and P6 from Haemophilus influenzae type b. 241 57

A mouse monoclonal antibody that recognizes an epitope on a 16,600-dalton outer membrane protein was developed to nontypable Haemophilus influenzae. This epitope was present on all 115 isolates of H. influenzae tested, including typable and nontypable strains. Screening of 89 strains of other bacteria demonstrated that this epitope is a highly specific marker for H. influenzae because the epitope was absent in virtually all other bacterial species tested. Western blot assays were performed with two normal human serum samples and convalescent-phase serum from an adult with bacteremia due to nontypable H. influenzae. Antibody to the 16,600-dalton outer membrane protein was present in all three human serum samples.
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PMID:Identification of a specific epitope of Haemophilus influenzae on a 16,600-dalton outer membrane protein. 241 44

A 16,600-D outer membrane protein is present in all strains of Haemophilus influenzae and antibodies to this protein are present in human serum. This study was designed to assess the role of this outer membrane protein (P6) in nontypeable H. influenzae as a target for human serum bactericidal antibody. P6 was isolated and coupled to an affinity column. Depleting normal human serum of antibodies to P6 by affinity chromatography resulted in reduced bactericidal activity of that serum for nontypeable H. influenzae. Immunopurified antibodies to P6 from human serum were bactericidal. Finally, preincubation of bacteria with a monoclonal antibody that recognizes a surface epitope on P6, inhibited human serum bactericidal killing. Taken together, these experiments establish that P6 is a target for human bactericidal antibodies. This observation provides evidence that P6 plays a potentially important role in human immunity to infection by nontypeable H. influenzae.
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PMID:Identification of a 16,600-dalton outer membrane protein on nontypeable Haemophilus influenzae as a target for human serum bactericidal antibody. 242 38


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