Disease relevance of Pasteurella

• These include Pasteurella multocida toxin, which uniquely acts as a mitogen, and Escherichia coli cytotoxic necrotizing factor, which activates Rho family signalling [1].
• Transferrin binding activity was present in all H. influenzae isolates tested but not detected in other Haemophilus species or in species of Pasteurella or Actinobacillus [2].
• Pharmacokinetic and pharmacodynamic profiles of danofloxacin administered by two dosing regimens in calves infected with Mannheimia (Pasteurella) haemolytica [3].
• All members of the genus Bordetella and Pasteurella multocida (a gram-negative bacillus genetically unrelated to Bordetella spp., yet often sharing the same ecological niche) produce a dermonecrotic toxin (DNT) [4].
• Lung lysophospholipase activity in specific-pathogen-free rats infected with Pasteurella pneumotropica or Mycoplasma pulmonis [5].

High impact information on Pasteurella

• Pasteurella canis was the most common isolate of dog bites, and Past. multocida subspecies multocida and septica were the most common isolates of cat bites [6].
• More from the pesky Pasteurella [7].
• The N-terminal half of CNF2 showed striking homology (27% identity and 80% conserved residues) to the N-terminal portion of Pasteurella multocida toxin [8].
• We show that the C-terminal 70 amino acids of leukotoxin from Pasteurella hemolytica can substitute functionally for the HlyA signal sequence [9].
• Treatment of the cells with O-sialoglycoprotease from Pasteurella haemolytica, an enzyme that selectively cleaves mucin-type O-linked glycoproteins, reduced binding to purified P- and L-selectin in all cases [10].

Chemical compound and disease context of Pasteurella

• Molecular directionality of polysaccharide polymerization by the Pasteurella multocida hyaluronan synthase [11].
• The sequence of the pmHS enzyme is not very similar to the vertebrate heparin/heparan sulfate glycosyltransferases, EXT1 and 2, or to other Pasteurella glycosaminoglycan synthases that produce hyaluronan or chondroitin [12].
• Treatment of Swiss 3T3 cells with a subsaturating concentration of recombinant Pasteurella multocida toxin (rPMT) markedly potentiated the production of inositol phosphates induced by bombesin, vasopressin, and endothelin but not by platelet-derived growth factor (PDGF) (AA and BB homodimers) [13].
• Crystal structure of Pasteurella haemolytica ferric ion-binding protein A reveals a novel class of bacterial iron-binding proteins [14].
• The intracellularly acting Pasteurella multocida toxin (PMT) is a potent mitogen that stimulates Gq-dependent formation of inositol trisphosphate [15].

Biological context of Pasteurella

• The Pasteurella multocida HA synthase, pmHAS, a polymerizing enzyme that normally elongates HA chains rapidly (approximately 1-100 sugars/s), was converted by mutagenesis into two single-action glycosyltransferases (glucuronic acid transferase and N-acetylglucosamine transferase) [16].
• The aroA gene from Pasteurella multocida was cloned by complementation of the Escherichia coli aroA mutant AB2829 with a DNA library constructed in pUC18 [17].
• In this study, we used Pasteurella multocida toxin (PMT), a unique bacterial toxin that activates the small GTPase Rho, and specific Rho inhibitors to investigate the role of Rho in osteoblast differentiation and bone formation in vitro [18].
• The tetracycline resistance determinant on plasmid pVM111 from an avian strain of Pasteurella multocida mediates tetracycline resistance by a regulated active efflux mechanism [19].
• A heptosyltransferase mutant of Pasteurella multocida produces a truncated lipopolysaccharide structure and is attenuated in virulence [20].

Anatomical context of Pasteurella

• Exposure of bovine neutrophils to Pasteurella haemolytica leukotoxin (LKT) stimulates the production of leukotriene B4 (LTB4), which is believed to be an important chemotactic agent in the development of acute fibrinopurulent pneumonic infection in cattle [21].
• Induction of inflammatory cytokines in bovine alveolar macrophages following stimulation with Pasteurella haemolytica lipopolysaccharide [22].
• Capsular hyaluronic acid (HA) mediates adhesion of serogroup A strains of Pasteurella multocida to elicited turkey air sac macrophages (TASM) [23].
• In addition, the proportions of free erythromycin in bovine serum and tissue chamber fluid before and 4 days after inoculation of subcutaneous tissue chambers with Pasteurella haemolytica were measured [24].
• Lipopolysaccharides (LPS) from Pasteurella multocida or Brucella abortus were complexed with Aspergillus fumigatus ribosomes by mixing and fixation for 3 days in 3.8% formaldehyde [25].

Gene context of Pasteurella

• Novel spectinomycin/streptomycin resistance gene, aadA14, from Pasteurella multocida [26].
• MHCII, Tlr4 and Nramp1 genes control host pulmonary resistance against the opportunistic bacterium Pasteurella pneumotropica [27].
• The biphasic mRNA expression pattern of bovine interleukin-8 in Pasteurella haemolytica lipopolysaccharide-stimulated alveolar macrophages is primarily due to tumor necrosis factor alpha [28].
• We performed cDNA and genomic cloning, sequencing and promoter analysis of the putative human O-sialoglycoprotein endopeptidase gene OSGEP (a homologue of gcp, a Pasteurella haemolytica A1 glycoprotease) [29].
• Cloning and characterization of the exbB-exbD-tonB locus of Pasteurella haemolytica A1 [30].

Analytical, diagnostic and therapeutic context of Pasteurella

• Tetracycline-resistant Pasteurella aerogenes isolates obtained from the intestinal tract of swine were investigated for their tet genes by PCR analysis and hybridization experiments [31].
• Detection of immunoglobulin G to Pasteurella haemolytica capsular polysaccharide by enzyme-linked immunosorbent assay [32].
• We purified an adhesin from Pasteurella. haemolytica by affinity chromatography using glutaraldehyde treated rabbit erythrocytes stroma [33].
• An exotoxin, called leukotoxin (LKT), from Pasteurella haemolytica, which had previously proved difficult to purify, was purified by high-performance liquid chromatography using rigid highly hydrophilic microparticulate anion-exchange columns [34].
• RESULTS: Serum tilmicosin concentration reached 1.91 +/- 0.18 micrograms/ml after 2 hours, decreased to 0.77 +/- 0.07 microgram/ml by 8 hours, and was below minimum inhibitory concentrations for Pasteurella multocida at 24 hours [35].

References