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)

Only scanty data are available on the susceptibility of Haemophilus influenzae in Italy. The in vitro activity of ampicillin, ampicillin-sulbactam, cefaclor, cefuroxime, cefotaxime, chloramphenicol, erythromycin and trimethoprim-sulfamethoxazole against 327 strains of Haemophilus influenzae (55 encapsulated, 272 non-typeable) isolated from adults and children in northern Italy, between January 1984 and December 1989, was compared. Patients were affected by meningitis or other invasive infections, conjunctivitis, otitis, sinusitis, pneumonia or bronchitis. Minimal inhibiting concentrations were determined by a microdilution technique in Mueller Hinton broth supplemented with 10 microliters/ml NAD and 2-5% lysed horse blood. A concentration of 1 x 10(5) to 5 x 10(5) CFU/ml was used as the inoculum. The antibiotics were tested at concentrations ranging from 0.03 to 64 microliters/ml with the exception of trimethoprim-sulfamethoxazole, for which the range of concentrations examined were 0.01/0.25 to 32/512 microliters/ml. All the strains tested were susceptible to ampicillin-sulbactam, cefuroxime and cefotaxime, and more than 95% were susceptible to ampicillin, cefaclor and chloramphenicol. Only 4% were susceptible to erythromycin but most minimal inhibiting concentrations fell into the intermediate category. Strains isolated from adults were more susceptible to trimethoprim-sulfamethoxazole than strains isolated from children (85% vs 66%; p = 0.011).
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PMID:Antimicrobial resistance among clinical isolates of Haemophilus influenzae in northern Italy. Collaborative Study on Pediatric Infectious Diseases. 847 3

Infectious coryza remains an important disease in the poultry industry despite the long-term and widespread use of vaccines against its causative agent, Haemophilus paragallinarum, in South Africa. In order to detect antigenic changes between populations of H. paragallinarum isolated before the use of vaccines against infectious coryza in this country, and field isolates obtained after the introduction of infectious coryza vaccines, 106 different NAD-dependent isolates (of which 93 were identified as H. paragallinarum) from 63 different farms, and dating from 1972 to March 1995, were identified by means of rabbit antisera against serogroups A, B and C. Serogroup C isolates show weaker cross-protection, requiring the further subdivision of this serogroup into its four different serovars. The percentages of the different serovars obtained in the 1970s, confirmed previously published data on South African isolates. A tendency towards a decrease in the number of serogroup A and serovar C-2 isolates, and an increase in the percentage of serovar C-3 isolates, was noted among isolates of the 1980s. These changes were markedly enhanced in the isolates obtained from 1990 to March 1995. The percentage of serogroup A isolates decreased significantly from 34% in the 1970s to only 5% in the 1990s, and that of serovar C-2 isolates, from 31-18%, while the abundance of serovar C-3 isolates increased significantly from 31% in the 1970s to 73% in the 1990s. Serogroup B remained more or less constant and never reached more than 10% of the population. These results indicate the need for the incorporation of serovar C-3 in a vaccine for use in South Africa, particularly in those areas of the country from which isolates were collected during this study. Some of the NAD-dependent isolates obtained from poultry in South Africa between 1970 and 1995, were biochemically identified as Pasteurella avium and P. volantium. As H. avium has been subdivided and reclassified into the genus Pasteurella, this represents the first report of the identification of P. avium and P. volantium in South Africa.
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PMID:Changes in the incidences of the different serovars of Haemophilus paragallinarum in South Africa: a possible explanation for vaccination failures. 891 59

Haemophilus paragallinarum causes infectious coryza in poultry, and a panel of monoclonal antibodies (Mabs) were established, which detect surface antigens of this bacterium. It was postulated that these Mabs could be used to detect antigenic differences between strains of H. paragallinarum used in infectious coryza (IC) vaccines, and isolates made from the field, from poultry vaccinated against IC. It has previously been reported that in South Africa there are three different Mab patterns that have been common to H. paragallinarum isolates for the past three decades. The effects of different growth conditions such as duration of incubation, inoculum size, levels of NAD or NaCl in the medium, and the pH of the medium on these Mab patterns were investigated. It was found that many different factors appear to influence the expression of the antigens detected by the panel of Mabs. It was found that at different stages during the growth cycles, the isolates could be classified into different Mab groups. It was also found that alteration of the inoculum size resulted in Mab-pattern switches. Addition of extra NaCl to the medium, in order to slow the growth rate, was found to result in Mab-pattern switches. pH was found to have significant effects on the levels of expression of the antigens detected by the Mabs, although these changes did not result in Mab-pattern switches. The effects of pH were also found to be highly strain dependent. The use of NAD, rather than sterile chicken serum, in the medium did not significantly alter the levels of expression of these antigens. Alterations of the growth conditions greatly affected the levels of expression of the antigens detected by the Mabs, and were highly strain dependent. It was not possible to predict the effects of a particular growth condition on a particular strain or isolate of H. paragallinarum.
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PMID:Effects of growth conditions and incubation times on the expression of antigens of Haemophilus paragallinarum which are detected by monoclonal antibodies. 920 5

Haemophilus parasuis malate dehydrogenase ((S)-malate:NAD+ oxidoreductase; EC 1.1.1.37) isolated from cell sonicates was purified 584-fold to electrophoretic homogeneity with a 19% recovery and a specific activity of 222 units/mg protein. SDS-polyacrylamide gel electrophoresis and molecular exclusion chromatography indicated the purified enzyme to be a dimer composed of 34,600 molecular weight subunits. Kinetic parameters for all four substrates in the forward and reverse reactions indicated a sequential mechanism for this enzymic process. Product and dead-end inhibition studies were consistent with an ordered bi-bi mechanism in which NAD is the first substrate bound to the enzyme and NADH the second product released. Protection against thermodenaturation of the enzyme by NAD and not by malate was supportive of this mechanism. A pronounced product inhibition by NADH (K(i) = 9.0 microM) was observed. Although NADP did not serve as a coenzyme, a number of analogs of NAD structurally altered in the nitrogen base moieties were observed to function as coenzymes in the oxidation of malate catalyzed by the purified malate dehydrogenase. Coenzyme-competitive inhibition of the malate dehydrogenase was observed with five adenosine derivatives and six structural analogs of NAD. Of the NAD analogs studied as inhibitors, 3-pyridylcarbinol adenine dinucleotide was the most effective (K(i) = 18 microM). Although inhibition of growth of H. parasuis by this analog was observed, it was less effective (K(i) = 136 microM) than the inhibition of the purified dehydrogenase.
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PMID:Purification and kinetic characterization of Haemophilus parasuis malate dehydrogenase. 924 95

The periplasmic nucleotide pyrophosphatase from Haemophilus parasuis was purified 750-fold to electrophoretic homogeneity through salt fractionation and ion-exchange and affinity chromatography. The purified enzyme was monomeric with an apparent M(r) of 70,000 and catalyzed the hydrolysis of the pyrophosphate bond of NAD to yield NMN and AMP as products. The enzyme exhibited negative cooperativity in the hydrolysis of a number of pyridine dinucleotides and structurally-related pyrophosphate compounds as indicated by biphasic double-reciprocal plots and Hill coefficients of 0.5. The kinetic parameters, K(m) and Vm, determined titrimetrically and analyzed through computer programs, were used to compare the relative effectiveness of dinucleotides containing nitrogen bases other than nicotinamide or adenine to that of NAD. Effective substrate-competitive inhibition of the pyrophosphatase was observed with purine and pyrimidine nucleoside diphosphates in the low micromolar concentration range. Although less effective, N1-alkylnicotinamide chlorides also inhibited competitively with respect to the substrate, NAD. In addition to being an effective inhibitor of the purified enzyme, adenosine diphosphate also inhibited growth of H. parasuis at a low micromolar concentration. This inhibition of growth correlates well with inhibition of the periplasmic pyrophosphatase which is supported by the fact that adenosine diphosphate does not effectively inhibit growth when the pyrophosphatase is by-passed by growth on nicotinamide mononucleotide. These observations are all consistent with the periplasmic nucleotide pyrophosphatase being essential for the growth of the organism on NAD and therefore, a very important enzyme with respect to the pathogenesis of the organism. 3-Aminopyridine mononucleotide, which also inhibited growth of H. parasuis at a low micromolar concentration, did not effectively inhibit the purified pyrophosphatase and a different target enzyme needs to be considered to explain growth inhibition by this derivative.
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PMID:Characterization of H. parasuis periplasmic nucleotide pyrophosphatase as a potential target enzyme for inhibition of growth. 945 36

Azithromycin has in vitro activity which includes important respiratory pathogens and is successful in treatment of respiratory tract infections. We assessed postantibiotic effect (PAE) of azithromycin against 3 stains of Streptococcus pneumoniae, 2 strains of Haemophilus influenzae and 2 strains of Moraxella catarrhalis. The strains were exposed for 2 hours to an azithromycin concentration of 0.5 mg/L (maximum serum concentration achieved by azithromycin after the usual dosing regimen). A stationary phase inoculum of 1 x 10(6)-5 x 10(6) UFC/ml in IsoSensitest Broth with 5% lysed horse blood and 20 mg/L NAD was used and shaken for the duration of the experiment. Antibiotic was neutralised by dilution 1:1000 into pre-warmed medium. Viable counts were determined before and after antibiotic exposure and then hourly for 7 hours by Miles and Misra method. The experiment was performed in triplicate. Even at such low concentration as that achieved in serum, azithromycin exhibits a PAE of 119 min for pneumococci, 130 min for haemophili and 155 min for moraxellae, fact which could allow the use of usual oral regimen in bacteraemic respiratory infection, as well.
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PMID:[The postantibiotic effect of azithromycin on respiratory pathogens]. 945 50

We assessed the post-antibiotic effect (PAE) of azithromycin against 3 strains of Streptococcus pneumoniae 2 strains of Haemophilus influenzae and 2 strains of Moraxella catarrhalis. The strains were exposed for 2 hours to a concentration of 0.5 mg/l. A stationary phase inoculum of 1 x 10(6)-5 x 10(6) CFU/ml in IsoSensitest Broth with 5% lysed horse blood and 20 mg/l NAD was used and shaken for the duration of the experiment. Antibiotic was neutralised by dilution 1:1000 into pre-warmed medium. [table: see text] In conclusion, even at such low concentration as achieved in serum, azithromycin has a PAE against the respiratory pathogens studied. In our opinion this could allow the use of azithromycin, in the usual regimen even in bacteremic respiratory infections.
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PMID:[The postantibiotic effect of azithromycin on respiratory pathogens]. 1075 61

Culture of guinea pig and rabbit respiratory tracts for bacteria using X- (haemin) and V- (NAD) factor in agar media detected infection by V-factor dependent Pasteurellaceae (Haemophilus sp.) in three colonies of guinea pigs and a group of rabbits. The 12 Haemophilus strains comprised three API NH codes classed as Haemophilus parainfluenzae and two codes classed as Haemophilus aphrophilus/paraphrophilus. Six cell wall lipid profiles were detected, but these were not related to API NH codes. Both bacteriological properties were used to select strains for serological studies but any relationship between bacteriological and serological properties of the Haemophilus strains was not evident. Varying serological relationships occurred between the newly isolated Haemophilus strains, [Pasteurella] pneumotropica NCTC 8284 and Haemophilus strains previously isolated from rats.
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PMID:Serological relationship of some V-factor dependent Pasteurellaceae (Haemophilus sp.) from guineapigs and rabbits. 1075 99

Exogenous NAD utilization or pyridine nucleotide cycle metabolism is used by many bacteria to maintain NAD turnover and to limit energy-dependent de novo NAD synthesis. The genus Haemophilus includes several important pathogenic bacterial species that require NAD as an essential growth factor. The molecular mechanisms of NAD uptake and processing are understood only in part for Haemophilus. In this report, we present data showing that the outer membrane lipoprotein e(P4), encoded by the hel gene, and an exported 5'-nucleotidase (HI0206), assigned as nadN, are necessary for NAD and NADP utilization. Lipoprotein e(P4) is characterized as an acid phosphatase that uses NADP as substrate. Its phosphatase activity is inhibited by compounds such as adenosine or NMN. The nadN gene product was characterized as an NAD-nucleotidase, responsible for the hydrolysis of NAD. H. influenzae hel and nadN mutants had defined growth deficiencies. For growth, the uptake and processing of the essential cofactors NADP and NAD required e(P4) and 5'-nucleotidase. In addition, adenosine was identified as a potent growth inhibitor of wild-type H. influenzae strains, when NADP was used as the sole source of nicotinamide-ribosyl.
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PMID:NADP and NAD utilization in Haemophilus influenzae. 1076 Jan 56

Our laboratory has previously reported a structurally and mechanistically related family of beta-hydroxyacid dehydrogenases with significant homology to beta-hydroxyisobutyrate dehydrogenase. A large number of the members of this family are hypothetical proteins of bacterial origin with unknown identity in terms of their substrate specificities and metabolic roles. The Escherichia coli beta-hydroxyacid dehydrogenase homologue corresponding to the locus was cloned and expressed with a 6-histidine tag for specific purification. The purified recombinant protein very specifically catalyzed the NAD(+)-dependent oxidation of d-glycerate and the NADH-dependent reduction of tartronate semialdehyde, identifying this protein as a tartronate semialdehyde reductase. Further evidence for identification as tartronate semialdehyde reductase is the observation that the coding region for this protein is directly preceded by genes coding for hydroxypyruvate isomerase and glyoxylate carboligase, two enzymes that synthesize tartronate semialdehyde, producing an operon clearly designed for d-glycerate biosynthesis from tartronate semialdehyde. The single beta-hydroxyacid dehydrogenase homologue from Haemophilus influenzae was also cloned, expressed, and purified with a 6-histidine tag. This protein also catalyzed the NAD(+)-dependent oxidation of d-glycerate but was significantly more efficient in the oxidation of four-carbon beta-hydroxyacids like d-hydroxybutyrate and d-threonine. This enzyme differs from all the presently known beta-hydroxybutyrate dehydrogenases which are well established members of the short chain dehydrogenase/reductase superfamily.
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PMID:Novel beta -hydroxyacid dehydrogenases in Escherichia coli and Haemophilus influenzae. 1097 49


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