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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We investigated the following six Haemophilus species from man for the both enzymes neuraminidase and N-acetylneuraminate pyruvate lyase: H. aegypticus, H. aphrophilus, H. influenzae. H. parahaemolyticus, H. parainfluenzae and H. vaginalis. It is shown that H. vaginalis does not produce either neuraminidase or N-acetylneuraminate pyruvate lyase. He differs, therefore, from all other investigated haemophili producing both enzymes, neuraminidase and N-acetylneuraminate pyruvate lyase. Colominic acid, Na-salt, is splitted better than N-acetylneuraminyllactose. It can be concluded, therefore, some substrate specificity of the neuramindase of Haemophili in the sense that the alpha, 2 leads to 8 linkage of neuraminic acid is cleaved quicker than the alpha, 2 leads to 3 linkage. The physiological and pathologenic role of the both enzymes is discussed.
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PMID:[The occurrence of neuraminidase and N-acetylneuraminate-pyruvate lyase in pathogenic haemophili of man (author's transl)]. 30 52

The mean concentration of haemophili in 31 specimens of plaque was 1.23 times 10(6) per milligram or approximately 4.4% of the viable bacteria present. Occurrence of different species was similar to saliva with Haemophilus parainfluenzae constituting 87.8%. Most haemophili produced neuraminidase and appeared to be primarily responsible for the small amounts of this enzyme in plaque.
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PMID:Occurrence of haemophili in dental plaque and their association with neuraminidase activity. 105 57

The lipooligosaccharides (LOS) of strains of Haemophilus ducreyi, Neisseria gonorrhoeae, Neisseria meningitidis, and Neisseria lactamica contain epitopes that are antigenically and structurally similar to carbohydrates present in human glycosphingolipids. LOS from strains of Haemophilus influenzae and H. influenzae biogroup aegyptius were tested for the binding of monoclonal antibodies (MAbs) that bind to human glycosphingolipids possessing Gal beta 1-4GlcNAc (MAb 3F11) and Gal alpha 1-4Gal beta 1-4Glc (MAb anti-Pk). In solid-phase radioimmunoassays, the LOS of 18 of 19 H. influenzae type b (Hib), 8 of 19 nontypeable H. influenzae, and 10 of 20 H. influenzae biogroup aegyptius strains bound MAb anti-Pk. The LOS of 13 of 19 Hib, 10 of 16 nontypeable H. influenzae, and 2 of 18 H. influenzae biogroup aegyptius strains bound MAb 3F11. Neuraminidase treatment of the strains increased the binding of MAb 3F11 by more than twofold in 47% of the H. influenzae strains, suggesting that sialic acid occluded the LOS structure recognized by MAb 3F11. The material released from neuraminidase-treated Hib LOS was confirmed to be sialic acid by high-performance anion-exchange chromatography. A recombinant plasmid containing genes involved in Hib LOS biosynthesis directed the expression (assembly) of the 3F11 epitope in Escherichia coli. These studies demonstrate that H. influenzae and H. influenzae biogroup aegyptius express at least two LOS epitopes that are similar to those present in human glycosphingolipids. Sialic acid was present on the LOS of some H. influenzae strains and prevented the binding of MAb 3F11 to its epitope. The oligosaccharide portion of sialylated LOS may also resemble sialylated oligosaccharides present in human glycosphingolipids (gangliosides).
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PMID:Lipooligosaccharides (LOS) of some Haemophilus species mimic human glycosphingolipids, and some LOS are sialylated. 137 91

Haemophilus parainfluenzae synthesizes an outer membrane protein adhesin which mediates binding to oral streptococci, salivary pellicle, and neuraminidase-treated erythrocytes. An indirect gold labeling technique and immunoelectron microscopy verified the location of this outer membrane protein. Further, a clustering of gold particles was observed in irregular patches at the cell surface.
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PMID:Clustering of an outer membrane adhesin of Haemophilus parainfluenzae. 173 May 5

The relation of neuraminidase to morbidity and mortality was examined in patients with Haemophilus influenzae, meningococcal, and pneumococcal meningitis. Ten strains of H. influenzae and eight strains of meningococci from infected cerebrospinal fluid (CSF) did not elaborate neuraminidase. Each of 27 strains of pneumococci from infected CSF elaborated both neuraminidase and N-acetylneuraminic acid (NANA) aldolase. There was no correlation between amount of neuraminidase secreted in vitro and survival of patients. Values for free and total NANA concentrations were derived from admission CSF samples of 63 patients with meningitis; 18 patients infected with Neisseria meningitidis, 10 with H. influenzae and 35 with Diplococcus pneumoniae. Mean values for total NANA were elevated in each type of bacterial meningitis; however, abnormal concentrations of free CSF NANA were detected only in 17 patients with pneumococcal meningitis. 11 of 18 patients with pneumococcal meningitis showing normal free CSF NANA concentrations were cured, whereas only 4 patients with abnormal free NANA levels survived without residua. Both coma and bacteremia occurred significantly more often among patients with elevated concentrations of free CSF NANA. The association of elevated concentrations of free CSF NANA with coma and with an adverse prognosis suggested that neuraminidase may be a factor in the pathogenesis of penumococcal meningitis.
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PMID:Neuraminidase activity in bacterial meningitis. 439 34

A sialidase (neuraminidase, acylneuraminosyl hydrolase, EC 3.2.1.18) has been discovered and isolated from Gardnerella vaginalis (ex. Haemophilus vaginalis), a possibly pathogenic inhabitant of the female genital tract. Bacteria were grown in peptone-yeast-extract medium with 2.0 mM N-acetylmannosamine as enzyme inductor under CO2 atmosphere. Sialidase activity was found in the bacterial sediment and in the culture medium. The enzyme was liberated from the cells by ultrasonic treatment. Purification was performed by 60-80% ammonium sulfate precipitation and by column chromatography on Sepharose CL-6B and Sephadex G 200. The enzyme revealed a molecular weight in the range of Mr 75 000 and a pH optimum at 5.5. Among the different types of NeuAc-containing glycoconjugates, the enzyme exhibits its highest activities towards the globular glycoproteins alpha 1-acid glycoprotein and fetuin. Taking their cleavage rate as 100, it is around 55 for II3NeuAc-Lac, 45 for bovine submaxillary mucin, 35 for II6NeuAc-Lac and IV3, III6NeuAc2-LcOse4. The rates for III8,II3NeuAc2-Lac, gangliosides and colominic acid are below 20. Due to its specificity pattern, the enzyme may play a role in the pathogenic process of G. vaginalis infections.
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PMID:A newly discovered sialidase from Gardnerella vaginalis. 633 32

Hemagglutinating properties of Haemophilus paragallinarum serotype 2 and serotype C against freshly collected and glutaraldehyde (GA)- fixed chicken RBC were investigated. Different from serotype 1, the nontreated organisms of serotype 2 and serotype C lacked hemagglutinating activity. However, when the organisms were treated with potassium thiocyanate (KSCN) and/or sonication, activity occurred not only against GA-fixed chicken RBC, but also against GA-fixed RBC of various animal species. The maximum hemagglutination titer (1:64 to 1:256) was obtained against GA-fixed RBC with the KSCN-treated organisms that were also sonicated. The activity was inactivated by heating at 100 C or by treatments with formalin or trypsin, but not by treatments with hyaluronidase or neuraminidase. By using KSCN-treated and sonicated organisms and GA-fixed chicken RBC, a detection of hemagglutination-inhibition (HI) antibody was possible. The HI tests showed that serotype 2 hemagglutinin was immunologically distinct from serotype 1 and that the HI antibody correlated to protective activity against challenge exposure with serotype 2 and serotype C. Chicks having HI antibody greater than 1:5 were protected against challenge exposure with homologous type, but were not protected with serotype 1. Applicability of the HI test was also shown for evaluating protective potency in the serotype 2 vaccine, as well as in the serotype 1 vaccine.
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PMID:Hemagglutinin of Haemophilus paragallinarum serotype 2 organisms: occurrence and immunologic properties of hemagglutinin. 680 71

Haemophilus avium hemagglutinin properties were studied. Hemagglutination titer was decreased by proteolytic enzyme treatments, but was not affected by glycosidase, lipase, phospholipase, and neuraminidase treatments. Cell-free hemagglutinin was found in supernatants of centrifuged sonicate and centrifuged agitate of H avium and was precipitated with ammonium sulfate with no loss of hemagglutinating activity. The H avium hemagglutinin showed different patterns of activity against the RBC of different avian species. Hemagglutination of chicken RBC was not inhibited by D-mannose.
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PMID:Characterization and chemical nature of Haemophilus avium hemagglutinin. 707 65

Hemagglutinin (HA) of Haemophilus paragallinarum was purified, and its immunologic, chemical, and morphologic properties were studied. The HA was purified by gel filtration on Sepharose 6B and by subsequent ultracentrifugation of trypsinized cells after pretreatment with neuraminidase. After gel filtration, the HA component (fractioned HA) gave 1 precipitin line by gel diffusion, and after inoculation in chickens, hemagglutinination-inhibition antibody to trypsin-sensitive HA antigen was found. Chickens inoculated with the fractionated HA were protected from challenge exposure with H paragallinarum. In a sample further purified by ultracentrifugation (purified HA), a single protein band was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; it had a molecular weight of approximately 39,000. A molecular weight of several hundred thousand to several million was observed by gel filtration. Seemingly, HA of H paragallinarum is an aggregate of more than 20 HA sub-units. The purified HA included protein and some sugars, and according to electron microscopic observation, had a filamentous structure.
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PMID:Purification and properties of Haemophilus paragallinarum hemagglutinin. 721 46

According to the genetic relationships among Gram-negative bacilli the genus Pasteurella is included with the genus Haemophilus and the genus Acinobacillus within the family Pasteurellacae. Pasteurella multocida, the type species, is responsible for the majority of human Pasteurella infections. P. multocida is a member of the normal flora in the upper respiratory tract of many mammals or birds. It causes sporadic or epidemic diseases among different animal species, particularly pneumonia and atrophic rhinitis in swine in intensive breeding stations. The most common human infection with P. multocida is a local cellulitis following dog or cat bites and scratches. Serious local complications are sometimes responsible for prolonged disability. The respiratory tract is the second human source of P. multocida isolates. The frequency of recovery of P. multocida from oropharynx of apparently healthy pig breeders suggests that respiratory pasteurellosis could be an occupational disease. The mechanisms of virulence of P. multocida are unclear. Several factors are involved: capsules preventing phagocytosis, a dermonecrotic toxin causing experimental atrophic rhinitis, hyaluronidase, neuraminidase and proteases. Penicillin is considered to be the drug of choice for Pasteurella infection. Tetracyclin is efficient for bites but has no bactericidal effect. Oxacillin, first-generation cephalosporins, macrolides and aminoglycosides have poor activities. In the case of beta-lactamase producing strains a bactericidal effect could be achieved with fluoroquinolones or third generation cephalosporins.
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PMID:[Pasteurelloses]. 777 Mar 88


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