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PubMed2001

Molecular identification of TEM-1 beta-lactamase in a Pasteurella multocida isolate of human origin.

Two clinical strains of Pasteurella multocida were isolated from an HIV-infected patient who developed arthritis. Strain FB-1, which was isolated from a dog-bite wound, was resistant to narrow-spectrum penicillins. The second strain, FB-2, which was present in blood cultures as well as the dog-bite wound, was susceptible to all beta-lactam agents. Arbitrarily primedpolymerase chain reaction and pulsed-field gel electrophoresis revealed that these two isolates were genetically indistinguishable. 16S rDNA gene sequencing facilitated identification at the subspecies level. Amoxicillin resistance determinant was located on a highly unstable 4.3-kb plasmid, pFAB-1. Isoelectrofocusing and polymerase chain reaction amplification followed by sequencing revealed the presence of a pI 5.4 TEM-1 beta-lactamase. This description is the first of a TEM-1 Beta-lactamase' in a Pasteurella multocida strain of human origin.

Acquired Immunodeficiency Syndrome↗

PubMed2005

Genetic diversity on 16S rDNA sequence and phylogenic tree analysis in Pasteurella pneumotropica strains isolated from laboratory animals.

To reveal the genetic diversity of Pasteurella pneumotropica, the 16S rDNA sequence and multiple alignments were performed for 35 strains (from 17 mice, 13 rats, 3 hamsters, 1 rabbit, and 1 guinea pig) identified as P. pneumotropica using a commercial biochemical test kit or PCR test and two reference strains (ATCC 35149 and CNP160). Each strain showed a close similarity with one of the following organisms: P. pneumotropica (M75083), Bisgaard taxon22 (AY172726), Pasteurella sp. MCCM00235 (AF224300), Pasteurellaceae gen. sp. Forsyth A3 (AF224301), and Actinobacillus muris (AF024526) on GenBank, and were divided into six clusters on a phylogenic tree. Two reference strains, P. pneumotropica biotype Jawetz and Heyl, were classified at both ends of the clusters. Our conclusion is that P. pneumotropica should be reclassified because of the very wide genetic diversity that exists.

Animals↗

PubMed1998

Cross-protection studies with three serotypes of Pasteurella haemolytica in the goat model.

Cross-protection studies employing three serotypes of Pasteurella haemolytica (Ph) were performed in goats, with challenge exposure by transthoracic injection. Indirect hemagglutination (IHA) serum titers showed that the herd had been naturally infected with Ph biovar A, serovar 2 (PhA2) prior to the study. Sixty-four weanling male Spanish goats were randomly allotted to 16 groups. Fifteen goats were given two transthoracic injections into the lungs 21 days apart with live Pasteurella haemolytica biovar A, serovar 1 (PhA1) in agar beads. Fifteen goats were given two transthoracic injections into the lungs 21 days apart with live PhA2 in agar beads. Sixteen goats were given two transthoracic injections into the lungs 21 days apart with live P. haemolytica biovar A, serovar 6 (PhA6) in agar beads. Eighteen control (CON) goats were given two transthoracic injections into the lungs 21 days apart with agar beads alone. Fourteen days after the second injection, goats were challenge-exposed to either live PhA1, PhA2, or PhA6 by transthoracic injection into the lung, and 4 days later, all goats were euthanatized and necropsied. Serum antibody to P. haemolytica antigens was measured throughout the experiment. Mean volumes of consolidated lung tissue for the CON goats challenged with PhA1, PhA2, and PhA6 were 28.29 cm3, 8.36 cm3, and 16.29 cm3, respectively. Mean volumes of consolidated lung tissue for the PhA1-immunized goats challenged with PhA1, PhA2, and PhA6 were 4.38 cm3, 0.25 cm3, and 1.90 cm3, respectively. Mean volumes of consolidated lung tissue for the PhA2-immunized goats challenged with PhA1, PhA2, and PhA6 were 9.68 cm3, 0.05 cm3, and 3.39 cm3, respectively. Mean volumes of consolidated lung tissue for the PhA6-immunized goats challenged with PhA1, PhA2, and PhA6 were 14.05 cm3, 1.27 cm3, and 4.53 cm3, respectively. These data demonstrate protection in immunized goats challenged with the homologous serotype of P. haemolytica. PhA1-immunized animals were protected against serotype 2 challenge as well as against serotype 6 challenge. PhA2-immunized animals were not protected against serotype 1 challenge, but were protected against transthoracic PhA6 challenge. PhA6-immunized animals were not protected against serotype 1 challenge, but were protected against transthoracic PhA2 challenge. There appears to be some cross-protection among the P. haemolytica serotypes, and this fact should be taken into consideration when developing vaccines against this organism.

Animals↗

PubMed1998

In vivo production of neuraminidase by Pasteurella haemolytica in market stressed cattle after natural infection.

Pasteurella haemolytica (Ph) is the most important cause of the bovine acute fibrinohemorrhagic pneumonia that occurs in market stressed calves after shipment to feedyards. Recent characterization of neuraminidase production by these organisms has shown that all 16 serotypes produce an immunologically similar form of the enzyme. Anti-neuraminidase antibody against PhA1 and PhA6 was determined in 101 2- to 5-month-old calves, on their farms of origin, at the order buyer barn (OBB), and through 28 days in the feedyard. Half of the calves were vaccinated with a killed Ph serotype-A1 (PhA1) product. Nasal secretion and tonsil wash specimens were cultured for Ph and Pasteurella multocida (Pm). Serum antibody against PhA1 and PhA6 was measured by indirect hemagglutination (IHA), and anti-neuraminidase antibody was determined by the neutralization assay. At the feedyard, 73 calves had respiratory tract disease. IHA values ranged between 1:2 and 1:1024 for PhA1 and between 1:2 and 1:512 for Ph serotype A6 (PhA6). Forty-two, 24, and 28% of the calves were infected with PhA1, PhA6, and Pm, respectively. Ninety-six percent of the calves experienced an increase in anti-PhA1 neuraminidase antibody when sera drawn on feedyard day 28 were compared with sera drawn on the farm. These data demonstrate that the enzyme neuraminidase is produced in vivo in market stressed cattle after a natural Ph infection.

Animals↗

PubMedDate not supplied

Evaluation of combined Pasteurella vaccines in control of sheep pneumonia.

The effectiveness of an oil adjuvant vaccine (OAV) incorporating locally isolated strains of Pasteurella haemolytica type 7 and Pasteurella multocida types A and D was compared with that of Carovax (Wellcome Laboratories) in imported cross-bred lambs. The criterion of efficacy was the ability of the vaccines to reduce the extent of pneumonic lesions in vaccinated as against unvaccinated control lambs. The OAV produced at this Institute significantly reduced the lung lesions at P less than 0.05 level compared with its control group when challenged with P. haemolytica alone. However, the vaccine was unsatisfactory against P. multocida or combined P. multocida P. haemolytica challenge. Carovax did not produce any significant reduction in the lung lesions caused by P. haemolytica and/or P. multocida.

Adjuvants, Immunologic↗

PubMed1990

Sequence analysis of the potent mitogenic toxin of Pasteurella multocida.

Pasteurella multocida toxin is a potent mitogen for cultured Swiss 3T3 cells where it causes an accumulation of inositol phosphates and activation of protein kinase C. The gene sequence described here coded for a 146 kDa protein. The ORF was preceded by a ribosome binding site and followed by a stem loop. There was no evidence for a signal sequence. The gene had a low G + C base ratio which differs from the rest of the Pasteurella genome. There was no significant homology with other known proteins, although a motif found in certain bacterial toxins which are ADP-ribosyl transferases is present. A recombinant expressing only part of the PMT gene was not mitogenic.

Amino Acid Sequence↗

PubMed1994

Mutation of a putative ADP-ribosylation motif in the Pasteurella multocida toxin does not affect mitogenic activity.

Pasteurella multocida toxin (PMT) is a potent mitogen for Swiss 3T3 fibroblasts and cytotoxic to embryonic bovine lung cells. Site-directed mutagenesis was used to investigate the functional significance of a three amino acid motif in PMT that is present in five other bacterial protein toxins which exhibit ADP-ribosyl transferase activity. Crude lysates of mutant clones were fully cytotoxic for embryonic bovine lung cells. Purified mutant toxin was also as effective at stimulating inositol phosphate turnover and nucleic acid synthesis as wild type toxin. We conclude that this motif has no functional significance in Pasteurella multocida toxin.

3T3 Cells↗

PubMed1982

Otogenic pasteurella multocida brain abscess and glomus jugulare tumour.

We report the occurrence of a Pasteurella multocida temporal lobe abscess in an elderly woman who had a history of neglected chronic purulent otitis and in whom an extensive ipsilateral glomus tumour invading the petrous bone was found. We believe this is the first report in the literature of an otogenic cerebral abscess associated with a glomus jugulare tumour and the fifth report of a Pasteurella multocida brain abscess. The synergistic pathogenesis of the otitis and the glomus tumour in the evolution of the abscess is hypothesized.

Aged↗

PubMed1994

Construction of conjugative shuttle and suicide vectors for Pasteurella haemolytica and P. multocida.

A shuttle cloning vector, pAKA16, and suicide derivatives pAKA19 and pAKA22 have been developed for gene transfer to Pasteurella haemolytica and P. multocida. pAKA16 was constructed by insertion of the lacZ alpha-peptide-encoding region and a multiple cloning site into a plasmid which was originally isolated from P. haemolytica serotype A1. The vector encodes ampicillin resistance, and contains at least 14 unique restriction sites and the property of phenotypic identification of recombinant clones in Escherichia coli by insertional inactivation of beta-galactosidase activity. It can be transferred by conjugation to P. haemolytica or P. multocida and is stably maintained in both species. The type-II chloramphenicol acetyltransferase-encoding gene (cat), cloned into pAKA16, was stably expressed in both P. haemolytica and P. multocida. Plasmids pAKA19 and pAKA22 were constructed by replacement of the origin of DNA replication (ori) of pAKA16 with a ColE1-type ori from pBR322 or an ori of plasmid R6K (oriR6K) from pJM703.1, respectively. These derivatives replicate in E. coli, but not in either P. haemolytica or P. multocida, and are suitable for use as suicide vectors for these Pasteurella species.

Chloramphenicol O-Acetyltransferase↗

PubMed1984

A test in vero cell monolayers for toxin production by strains of Pasteurella multocida isolated from pigs suspected of having atrophic rhinitis.

Monolayers of Vero cells showed a morphological change after exposure to supernatants of certain porcine Pasteurella multocida cultures. It appeared possible to screen Pasteurella multocida isolates for their ability to produce toxin and to cause atrophic rhinitis in pigs. A close correlation with the guinea pig skin test was demonstrated.

Animals↗

PubMed1991

Resistance to trimethoprim and 2,4-diamino-6,7-diisopropyl-pteridine (0/129) in Pasteurella haemolytica.

Thirteen strains of Pasteurella haemolytica resistant to moderate levels of trimethoprim (MICs from 8 to 64 micrograms/ml) and 0/129 (MICs from 16 to 64 micrograms/ml) were isolated from bovine specimens. Two strains, CNP330 and CNP334, were studied and found to harbour various plasmids but all attempts to cure trimethoprim resistance were unsuccessful. Resistance characters were not transferable to Escherichia coli or to Pasteurella multocida by conjugation and to E. coli by transformation. The resistance gene(s) was therefore tentatively assigned to a chromosomal location and cloned into E. coli where it conferred trimethoprim resistance. Trans-complementation analysis of a dihydrofolate reductase-deficient mutant of E. coli showed that trimethoprim resistance was secondary to synthesis of a dihydrofolate reductase. DNA/DNA hybridization of the hybrid plasmid and of strains CNP330 and CNP334 with probes specific for dihydrofolate reductase types I to V were negative, indicating that cross-resistance to trimethoprim and 0/129 in P. haemolytica was due to the acquisition by P. haemolytica of a new resistance determinant.

Animals↗

PubMed1995

Partial characterization of the leukotoxin of Pasteurella haemolytica-like bacteria isolated from swine enteritis.

Pasteurella haemolytica-like (PHL) strains isolated from diarrheic pigs are known to produce a leukotoxin that is lethal to ruminant leukocytes. In the present study, 12 PHL strains were screened for leukotoxin production using a tetrazolium dye-reduction assay. Sterile culture supernatant from strain 6213A, the maximum leukotoxin producer, was used as the crude leukotoxin for characterization studies. The leukotoxin was inactivated by heat at 60 degrees C and by trypsin, protease, and amylase. Toxicity was retained over a pH range of 3.0-11.0. The leukotoxin was lethal to polymorphoneutrophils (PMNs) of cattle, sheep, goat, and swine. Chromosomal DNA of all 12 PHL strains hybridized with a 3.9 kb Pasteurella haemolytica A1 leukotoxin probe, indicating similarities between the leukotoxin genes of P. haemolytica and PHL strains.

Animals↗

PubMed1996

Tn10 insertional mutagenesis in Pasteurella multocida.

The objective of this study was to identify a transposon that will randomly and stably integrate in the genome of Pasteurella multocida. Using the suicide conjugative delivery system, pLOF, containing a kanamycin resistance marked Tn10 insertion element, we determined that Tn10 is effective in producing insertional mutations in this species. Combined conjugation/transposition events occurred once per 10,000 donor cells. Only 1.4% of the isolates resulted from vector integration and the genomic insertions were random and stable as determined by DNA/DNA hybridization after 10 serial subcultures lacking antibiotic selection. Twenty-two percent of the isolates were auxotrophic, 4% were tryptophan auxotrophs. Mutants derived by this method will be useful for studying putative virulence determinants of Pasteurella.

DNA Transposable Elements↗

PubMed1988

Purification of fimbriae from Pasteurella haemolytica A-1.

Pasteurella haemolytica A-1 produces large, rigid fimbriae with a diameter of 12 nm and a denisty of 1.32. Their subunit molecular weight was 35,000 as determined by SDS-polyacrylamide gel electrophoresis and immunoblotting with monoclonal antibodies raised against native fimbriae. The isoelectric point of the purified fimbriae was 4.8. While Pasteurella haemolytica whole cells plus a crude shear fraction were capable of agglutinating bovine erythrocytes, purified fimbriae exhibited no such activity.

Animals↗

PubMed1991

In vivo expression of iron regulated outer-membrane proteins in Pasteurella haemolytica-A1.

Pasteurella haemolytica-A1 was grown in vitro under iron-rich conditions, iron-depleted conditions, and in vivo within a chamber implanted in the peritoneal cavity of a rabbit to determine if iron regulated outer-membrane proteins were expressed in vivo. The antigenicity of outer membrane (OM) proteins from bacteria grown under these conditions was assessed by immunoblotting with pooled serum from convalescent bovine calves experimentally infected with P. haemolytica-A1 and serum from the implanted rabbit. Pasteurella haemolytica-A1 grown under iron-depleted conditions showed three distinct OM protein bands (71, 77, and 100 kDa) that were present in much lesser amounts when the organism was grown under iron-rich conditions. These same three bands were evident in OM protein preparations from bacteria grown in vivo. Western blotting indicated that these protein bands were recognized immunologically by the convalescent bovine serum and by serum from the implanted rabbit, in cells grown under the iron-depleted conditions and in vivo, but not if the bacteria were grown under the in vitro iron-rich conditions.

Animals↗

PubMed1992

Conditions for transformation of Pasteurella multocida by electroporation.

Conditions for electroporation of plasmid DNA into Pasteurella multocida were determined for use in developing a cloning system to study virulence factors of P. multocida. The highest efficiency of transformation (1.25 x 10(7) cfu/micrograms DNA) was obtained when 7.6 x 10(10) cells of P. multocida strain R473 were electroporated at 12.5 kV/cm (10 ms, 5 ng of pVM109). Transformation efficiencies of cells prepared at mid-log-phase were approximately 0.5 log10 lower than early, late, or stationary phases. Neither pBR322 nor pUC-19 were able to transform strain R473 under these conditions, even when DNA concentrations were increased to 1 microgram. When pBR322 was ligated with a Pasteurella plasmid, pLAR-1, the hybrid was able to transform strain R473 at an efficiency between 4.5 x 10(2) and 8 x 10(4) cfu/micrograms DNA. Six strains of P. multocida including serotypes A, B, D, and E were transformed successfully.

Electric Stimulation↗

PubMed2006

The functional molecular mass of the Pasteurella hyaluronan synthase is a monomer.

Hyaluronan (HA), a linear polysaccharide composed of beta1,3-GlcNAc-beta1,4-GlcUA repeats, is found in the extracellular matrix of vertebrate tissues as well as the capsule of several pathogenic bacteria. All known HA synthases (HASs) are dual-action glycosyltransferases that catalyze the addition of two different sugars from UDP-linked precursors to the growing HA chain. The bacterial hyaluronan synthase, PmHAS from Gram-negative Pasteurella multocida, is a 972-residue membrane-associated protein. Previously, the Gram-positive Streptococcus pyogenes enzyme, SpHAS (419 residues), and the vertebrate enzyme, XlHAS1 (588 residues), were found to function as monomers of protein, but the PmHAS is not similar at the protein sequence level and has quite different enzymological properties. We have utilized radiation inactivation to measure the target size of recombinant full-length and truncated PmHAS. The target size of HAS activity was confirmed using internal enzyme standards of known molecular weight. We found that the Pasteurella HA synthase protein functions catalytically as a monomer. Functional truncated soluble PmHAS also behaves as a polypeptide monomer as assessed by gel filtration chromatography and light scattering.

Bacterial Proteins↗

PubMed2005

Structural analysis of the lipopolysaccharide of Pasteurella multocida strain VP161: identification of both Kdo-P and Kdo-Kdo species in the lipopolysaccharide.

The structure of the lipopolysaccharide from the Pasteurella multocida strain VP161 was elucidated. The lipopolysaccharide was subjected to a variety of degradative procedures. The structures of the purified products were established by monosaccharide and methylation analyses, NMR spectroscopy and mass spectrometry. The following structures for the lipopolysaccharides were determined on the basis of the combined data from these experiments. [structure: see text]. Based on the NMR data, all sugars were found in pyranose ring forms, and Kdo is 2-keto-3-deoxy-octulosonic acid, L-alpha-D-Hep is L-glycero-D-manno-heptose, PPEtn is pyrophosphoethanolamine and PCho is phosphocholine. Intriguingly, when the O- and fully deacylated LPS was examined, it was evident that there was variability in the arrangement of the Kdo region of the molecule. Glycoforms were found with a Kdo-P moiety, as well as glycoforms elaborating a Kdo-Kdo group. Furthermore the Glc II residue was not attached to Hep I when two Kdo residues were present, but it was attached when the Kdo-P arrangement was elaborated, suggesting a biosynthetic incompatibility due to either steric hindrance or an inappropriate acceptor conformation. This variation in the Kdo region of the LPS was also observed in several other Pasteurella multocida strains investigated including the genome strain Pm70.

Carbohydrate Sequence↗