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)

Bordetella bronchiseptica is primarily resistant against nitrofurantoin (MIC greater than 200 mug/ml), and this feature can be used for the differentiation of the organism from other gram-negative coccobacteria. Nitrofurantoin paper disks (300 mug) failed to affect the growth of 150 strains of B. bronchiseptica isolated from different animal hosts, but they produced marked inhibition zones in the cultures of the followingspecies: Pasteurella multocida, Pasteurella pneumotropica, Pasteurella haemolytica, Yersinia pseudotuberculosis, Yersinia enterocolitica, Francisella tularensis, Haemophilus influenzae, Haemophilus parainfluenzae, Brucella abortus, Brucella melitensis, Brucella suis and Brucella neotomae.
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PMID:[Nitrofurantoin-test for the differentiation of bordetella bronchiseptica (author's transl)]. 80 44

The minimum inhibitory concentrations (MIC) of ciprofloxacin, enrofloxacin, and norfloxacin were tested for approximately ten clinical isolates of each of Actinobacillus pleuropneumoniae, Actinobacillus suis, Actinomyces pyogenes, Corynebacterium pseudotuberculosis, Erysipelothrix rhusiopathiae, Haemophilus parasuis, Haemophilus somnus, Pasteurella haemolytica, Pasteurella multocida, Rhodococcus equi, Streptococcus equi, Streptococcus suis and Streptococcus zooepidemicus. Ciprofloxacin and enrofloxacin had similar activity and were more active than norfloxacin. All isolates had an MIC of 1.0 microgram/mL or less for ciprofloxacin and enrofloxacin, and these drugs had particularly marked activity against the gram-negative bacteria tested.
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PMID:In vitro susceptibility of selected veterinary bacterial pathogens to ciprofloxacin, enrofloxacin and norfloxacin. 230 72

The resistance to anti-microbial agents of bacteria isolated from pathological conditions of birds in Victoria, 1978 to 1983, was determined for isolates of Escherichia coli, Salmonella species, Staphylococcus aureus, Pasteurella multocida, P. anatipestifer, Yersinia pseudotuberculosis and Haemophilus paragallinarum. The isolates of E. coli had a high prevalence of resistance to tetracycline and sulphonamides, and a lower prevalence of resistance to furazolidone and sulphamethoxazole-trimethoprim. The isolates of Salmonella spp commonly had resistance to tetracycline, sulphonamides, furazolidone and sulphamethoxazole-trimethoprim. Almost half the isolates of S. aureus showed resistance to lincomysin and many showed resistance to penicillin. Resistance to tetracycline was found in isolates of P. multocida, P. anatepestifer and Y. pseudotuberculosis. Some isolates of H. paragallinarum showed resistance to sulphonamides, streptomycin and sulphamethoxazole-trimethoprim.
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PMID:The resistance to anti-microbial agents of bacteria isolated from pathological conditions of birds in Victoria, 1978 to 1983. 391 84

We have cloned the L4 ribosomal protein genes from Morganella morganii and Haemophilus influenza. The sequences of these genes were compared with published sequences for Escherichia coli, Yersinia pseudotuberculosis, and Bacillus stearothermophilus. All five of these L4 genes were expressed in E. coli and shown to function as repressors of both transcription and translation of the E. coli S10 operon. Possible implications for regulation of r-protein synthesis in species other E. coli are discussed.
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PMID:Regulation of the Escherichia coli S10 ribosomal protein operon by heterologous L4 ribosomal proteins. 872 27

A novel antimicrobial agent from Staphylococcus aureus KSI1829, designated Bac1829, was purified by sequential steps of ammonium sulfate precipitation, Sephadex G-50 gel filtration chromatography, and hydrophobic interaction chromatography. Purified Bac1829 has a molecular mass of 6,418 +/- 2 Da. The peptide in heat stable, since full biological activity is retained after heating at 95 degrees C for 15 min, and it is destroyed by digestion with proteases. Amino acid sequence analysis revealed a high concentration of Ala and Gly residues, which respectively comprised 24 and 19% of the total amino acid content. Additionally, high levels of hydrophobic amino acids were present, accounting for the hydrophobic nature of Bac1829. Purified Bac1829 killed exponentially growing Corynebacterium renale in a dose-dependent manner by a bactericidal mode of action. A partial inhibitory spectrum analysis revealed that the following organisms were sensitive to the inhibitory activity of Bac1829: S. aureus RN4220, Streptococcus suis, Corynebacterium pseudotuberculosis, C. renale, Corynebacterium diptheriae, Haemophilus parasuis, Bordetella pertussis, Bordetella bronchoseptica, Moraxella bovis, and Pasteurella multocida.
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PMID:Purification and partial characterization of a novel antibacterial agent (Bac1829) Produced by Staphylococcus aureus KSI1829. 879 6

We have cloned and sequenced the 5.2 kb EcoRI fragment that contained part of the S10 operon from Actinobacillus actinomycetemcomitans FDC Y4. The order of the ribosomal protein genes was identical to that of the S10 operon of Haemophilus influenzae and Escherichia coli. The deduced amino acid sequences of ribosomal proteins in this operon displayed significant homologies (65.3%-100%) to those of H. influenzae, E. coli, Yersinia enterocolitica and Yersinia pseudotuberculosis. Phylogenetic trees obtained for these ribosomal proteins were similar to that obtained for 16S rRNA.
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PMID:Cloning and sequencing of part of the S10 operon from Actinobacillus actinomycetemcomitans FDC Y4. 946 4

Otitis externa in cattle has a significant impact in tropical and subtropical regions, and the aetiological agents are predominantly rhabditiform nematodes and mites of the genus Raillietia. Its prevalence is higher in mature and Zebu cattle. In advanced clinical cases there can be irreversible and fatal neural lesions. Ear infection in calves has been associated with concurrent respiratory diseases and mixed infection. The principal reported agents of otitis in calves are bacteria such as Actinomyces spp., Corynebacterium pseudotuberculosis, Escherichia coli, Haemophilus somnus, Pasteurella multocida, Mannheimia haemolytica, Pseudomonas spp., Streptococcus spp. and Mycoplasma bovis. The control and treatment of bovine otitis is not standardized and there is little evidence-based support for the diverse treatments available in the literature.
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PMID:Otitis in cattle, an aetiological review. 1499 70

In the bacterial periplasm the co-existence of a catalyst of disulfide bond formation (DsbA) that is maintained in an oxidized state and of a reduced enzyme that catalyzes the rearrangement of mispaired cysteine residues (DsbC) is important for the folding of proteins containing multiple disulfide bonds. The kinetic partitioning of the DsbA/DsbB and DsbC/DsbD pathways partly depends on the ability of DsbB to oxidize DsbA at rates >1000 times greater than DsbC. We show that the resistance of DsbC to oxidation by DsbB is abolished by deletions of one or more amino acids within the alpha-helix that connects the N-terminal dimerization domain with the C-terminal thioredoxin domain. As a result, mutant DsbC carrying alpha-helix deletions could catalyze disulfide bond formation and complemented the phenotypes of dsbA cells. Examination of DsbC homologues from Haemophilus influenzae, Pseudomonas aeruginosa, Erwinia chrysanthemi, Yersinia pseudotuberculosis, Vibrio cholerae (30-70% sequence identity with the Escherichia coli enzyme) revealed that the mechanism responsible for avoiding oxidation by DsbB is a general property of DsbC family enzymes. In addition we found that deletions in the linker region reduced, but did not abolish, the ability of DsbC to assist the formation of active vtPA and phytase in vivo, in a DsbD-dependent manner, revealing that interactions between DsbD and DsbC are also conserved.
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PMID:Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. 1628 Mar 24

The Oca family is a novel class of autotransporter-adhesins with highest structural similarity in their C-terminal transmembrane region, which supposedly builds a beta-barrel pore in the outer membrane (OM). The prototype of the Oca family is YadA, an adhesin of Yersinia enterocolitica and Yersinia pseudotuberculosis. YadA forms a homotrimeric lollipop-like structure on the bacterial surface. The C-terminal regions of three YadA monomers form a barrel in the OM and translocate the trimeric N-terminal passenger domain, consisting of stalk, neck, and head region to the exterior. To elucidate the structural and functional role of the C-terminal translocator domain (TLD) and to assess its promiscuous capability with respect to transport of related passenger domains, we constructed chimeric YadA proteins, which consist of the N-terminal YadA passenger domain and C-terminal TLDs of Oca family members UspA1 (Moraxella catarrhalis), EibA (Escherichia coli), and Hia (Haemophilus influenzae). These constructs were expressed in Y. enterocolitica and compared for OM localization, surface exposure, oligomerization, adhesion properties, serum resistance, and mouse virulence. We demonstrate that all chimeric YadA proteins translocated the YadA passenger domain across the OM. Y. enterocolitica strains producing YadA chimeras or wild-type YadA showed comparable binding to collagen and epithelial cells. However, strains producing YadA chimeras were attenuated in serum resistance and mouse virulence. These results demonstrate for the first time that TLDs of Oca proteins of different origin are efficient translocators of the YadA passenger domain and that the cognate TLD of YadA is essential for bacterial survival in human serum and mouse virulence.
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PMID:Contribution of trimeric autotransporter C-terminal domains of oligomeric coiled-coil adhesin (Oca) family members YadA, UspA1, EibA, and Hia to translocation of the YadA passenger domain and virulence of Yersinia enterocolitica. 1848 27