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

By using the Kume hemagglutinin serotyping scheme, 13 Australian isolates of Haemophilus paragallinarum were shown to constitute a new serovar within the presently termed serogroup II. Because of the likelihood that new serovars will continue to be established, we propose a rationalization of the nomenclature of the Kume scheme. Under this altered scheme, the three recognized serogroups I, II, and III are renamed A, C, and B, respectively. Within each of the serogroups, the serovars are numbered sequentially, allowing new serovars to be added in numerical order. Thus, the nine currently recognized Kume serovars are termed A-1, A-2, A-3, A-4, B-1, C-1, C-2, C-3, and C-4.
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PMID:Proposal of a new serovar and altered nomenclature for Haemophilus paragallinarum in the Kume hemagglutinin scheme. 219 92

Two monoclonal antibodies (MAbs) were evaluated for their ability to serotype 108 isolates of Haemophilus paragallinarum. One MAb (E5C12D10) was raised against a Page serovar A strain and the other (F2E6) against a Page serovar C strain. In both dot blot and hemagglutination-inhibition tests, MAb E5C12D10 recognized the type strains of Page serovar A and Kume serovars A-1, A-2, A-3, and A-4. MAb F2E6 recognized the type strains of Page serovar C and Kume serovars C-1, C-2, and C-3. Neither antibody recognized the type strains of Page serovar B or Kume serovars B-1 and C-4. When evaluated with 97 field isolates in a dot blot test, the MAbs serotyped 81 isolates, which was better than agglutinin typing by the Page scheme (69 isolates serotyped). The field isolates that did not react with the MAbs were either Page serovar B/Kume serovar B-1 (three isolates), Page serovar C/Kume serovar C-4 (12 isolates), or nontypable by either the Page or Kume scheme (one isolate).
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PMID:Evaluation of two monoclonal antibodies for serotyping Haemophilus paragallinarum. 228 16

The chemical structure of the lipopolysaccharide of a deep-rough mutant (strain I-69 Rd-/b+) of Haemophilus influenzae was investigated. The hydrophilic backbone of lipid A was shown to consist of a beta-(1',6)-linked D-glucosamine disaccharide with phosphate groups at C-1 of the reducing D-glucosamine and at C-4' of the non-reducing one. Four molecules of (R)-3-hydroxytetradecanoic acid were found directly linked to the lipid A backbone, two by amide and two by ester linkage (positions 2,2' and 3,3', respectively). Laser-desorption mass spectrometry showed that both 3-hydroxytetradecanoic acids linked to the non-reducing glucosamine carry tetradecanoic acid at their 3-hydroxyl group, so that altogether six molecules of fatty acid are present in lipid A. The lipopolysaccharide was the first described to contain only one sugar unit linked to lipid A. This, sugar in accordance with a previous report [Zamze et al. (1987) Biochem. J. 245, 583-587], was shown to be a dOclA phosphate. The phosphate group was found at position 4, but the analytical procedures employed (permethylation and methanolysis followed by gas-liquid chromatography/mass spectrometry) also revealed dOclA 5-phosphate. Since a cyclic 4,5-phosphate could be ruled out by 31P-NMR, we conclude that, in this lipopolysaccharide, a mixture of dOclA 4- and 5-phosphate is present. By methylation analysis of the dephosphorylated, deacylated and reduced lipopolysaccharide the attachment site of the dOclA was assigned to position C-6' of the non-reducing glucosamine of lipid A. The anomeric linkages present in the lipopolysaccharide were assessed by 1H-NMR and 13C-NMR of deacylated lipopolysaccharide. The saccharide backbone of this Haemophilus influenzae lipopolysaccharide possesses the following structure: (Formula; see text)
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PMID:Chemical structure of the lipopolysaccharide of Haemophilus influenzae strain I-69 Rd-/b+. Description of a novel deep-rough chemotype. 326 41

Haemophilus influenzae type b capsular polysaccharide [repeating unit, leads to 3)-beta-D-Ribf-(1 leads to 1)-D-Ribol-5-(PO2H leads to] was partially hydrolyzed with HCl to give oligosaccharides that were isolated by size-exclusion chromatography, and then characterized by 31P- and 13C-n.m.r.-spectral and chemical methods, in order to determine the end-group composition and, hence, the number-average chain-length (L). The ratio (approximately 17:8) of monophosphate end-groups to D-ribofuranose end-groups revealed the relative rates of hydrolysis of the phosphoric diester linkage and the glycosidic linkage in the repeating-unit structure. Cleavage of the phosphoric diester linkage was approximately 92% regioselective, as indicated by the approximately 12:1 ratio of D-ribofuranose monophosphate end-groups to D-ribitol monophosphate end-groups. The n.m.r. spectra of the oligosaccharide repeating-unit provided evidence for partial stereomutation (approximately 3-8%) that involved rearrangement of the D-ribofuranose phosphoric diester linkage and anomerization at C-1 of D-ribofuranose. Variously sized oligosaccharides (L = 4, 7, and 12), that had D-ribofuranose end-groups reacted with bovine serum albumin that had an average of approximately 9 adipyl hydrazide functionalities, to give, within experimental error, quantitative yields of the corresponding hydrazone-linked, oligosaccharide-protein conjugates.
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PMID:31P- and 13C-n.m.r.-spectral and chemical characterization of the end-group and repeating-unit components of oligosaccharides derived by acid hydrolysis of Haemophilus influenzae type b capsular polysaccharide. 660 88

Two monoclonal antibodies (MAbs) raised against a serovar A Haemophilus paragallinarum were evaluated for their ability to react with 11 reference strains that represented all the recognized serovars and with 27 field isolates of Page serovar A collected from around the world. The MAbs were used in a hemagglutination-inhibition assay. Both MAbs recognized type strains of Page serovar A and Kume serovars A-1 and A-2 but not the type strains of Kume serovars A-3 and A-4. Neither MAb recognized the type strains of Page serovars B and C or Kume serovars B-1, C-1, C-2, C-3, or C-4. When evaluated with the 27 Page serovar A field isolates, both MAbs recognized only 10 isolates. All of the recognized isolates belonged to Kume serovars A-1 (nine isolates) or A-2 (one isolate). All of the field isolates that were not recognized by one or the other of the MAbs either were Kume serovar A-4 (seven isolates) or could not be placed in an existing Kume A serovar (10 isolates). The results indicate that the epitope recognized by these MAbs is present only in strains of H. paragallinarum that belong to Kume serovars A-1 and A-2.
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PMID:Characterization of two monoclonal antibodies directed against serovar A Haemophilus paragallinarum. 798 Feb 89

The effect of 2,3 modifications on the antibacterial activity of ketolides was evaluated by introducing substituents in position 2 and converting the C-1, C-2, C-3 beta-keto-ester into stable 2,3 enol-ether or 2,3 anhydro derivatives. Introduction of a fluorine in C-2 is beneficial with regard to the overall antibacterial spectrum whereas the enol-ether and 2,3 unsaturated compounds, as well as the bulky gem dimethyl or 2-chloro derivatives, are less active particularly against erythromycin resistant strains. A 2-fluoro ketolide derivative demonstrates good antibacterial activity and in vivo efficacy against multi-resistant Streptococcus pneumoniae. Compared to azithromycin against Haemophilus influenzae, this compound is equivalent in vitro and slightly more active in vivo. These results demonstrate that within the ketolide class, to retain good antibacterial activity, position 2 needs to remain tetrahedral and tolerates only very small substituents such as fluorine.
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PMID:Beta-keto-ester chemistry and ketolides. Synthesis and antibacterial activity of 2-halogeno, 2-methyl and 2,3 enol-ether ketolides. 1098 40

The virulence of the reference strains of the nine currently recognized Kume serovars of Haemophilus paragallinarum was investigated. The capacity of the H. paragallinarum strains to cause the typical clinical signs of upper respiratory tract disease associated with infectious coryza in unvaccinated, nasal-challenged chickens was assessed. Differences in virulence were assessed by means of a standardized scoring system for clinical signs. All nine strains were pathogenic to chickens, producing typical clinical signs of infectious coryza. The highest clinical signs score was obtained for serovar C-1 (1.72), while the lowest clinical signs score was obtained for serovar C-4 (0.32). Our results indicate that virulence differences exist among the serovars of H. paragallinarum.
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PMID:Virulence of the nine serovar reference strains of Haemophilus paragallinarum. 1566 70

The protection and level of hemagglutination-inhibition (HI) antibodies conferred in infectious coryza bivalent- and trivalent-immunized chickens against Avibacterium (Haemophilus) paragallinarum field isolates of the prevalent serovars in Mexico (A-1, A-2, B-1, and C-2) were investigated. The bivalent bacterin (A-1 and C-1) conferred significant protection and increased HI antibodies against isolates of serovars A-1, A-2, and C-2, but not against a serovar B-1 isolate. The trivalent bacterin (A-1, B-1, and C-2) conferred protection and increased HI antibodies against all four of the isolates. The results confirmed that in poultry areas where serovar B-1 is prevalent, the inclusion of this serovar in bacterins is needed to confer protection against infectious coryza caused by A. (H.) paragallinarum isolates of serovar B-1.
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PMID:Protection conferred by bivalent and trivalent infectious coryza bacterins against prevalent serovars of Avibacterium (Haemophilus) paragallinarum in Mexico. 1640 4

The pathway for synthesis of the peptidoglycan precursor UDP-N-acetylmuramyl pentapeptide is essential in Gram-positive and Gram-negative bacteria. This pathway has been exploited in the recent past to identify potential new antibiotics as inhibitors of one or more of the Mur enzymes. In the present study, a high-throughput screen was employed to identify potential inhibitors of the Escherichia coli MurC (UDP-N-acetylmuramic acid:L-alanine ligase), the first of four paralogous amino acid-adding enzymes. Inhibition of ATP consumed during the MurC reaction, using an adaptation of a kinase assay format, identified a number of potential inhibitory chemotypes. After nonspecific inhibition testing and chemical attractiveness were assessed, C-1 emerged as a compound for further characterization. The inhibition of MurC by this compound was confirmed in both a kinetic-coupled enzyme assay and a direct nuclear magnetic resonance product detection assay. C-1 was found to be a low micromolar inhibitor of the E. coli MurC reaction, with preferential inhibition by one of two enantiomeric forms. Experiments indicated that it was a competitive inhibitor of ATP binding to the MurC enzyme. Further work with MurC enzymes from several bacterial sources revealed that while the compound was equally effective at inhibiting MurC from genera (Proteus mirabilis and Klebsiella pneumoniae) closely related to E. coli, MurC enzymes from more distant Gram-negative species such as Haemophilus influenzae, Acinetobacter baylyi, and Pseudomonas aeruginosa were not inhibited.
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PMID:Identification of an inhibitor of the MurC enzyme, which catalyzes an essential step in the peptidoglycan precursor synthesis pathway. 1831 98