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PubMed1981

Intranasal immunization of mice against Pasteurella multocida.

A potassium thiocyanate (KSCN) extract of Pasteurella multocida serotype III:A was shown to protect mice from an intranasal challenge with up to 300 50% lethal doses of P. multocida. In addition to preventing death, bacteria were rapidly cleared from the lungs of immunized mice so that by 72 to 96 h postchallenge no bacteria were present in the lungs of immunized mice, whereas up to 10(9) bacteria were present in lungs of nonimmunized mice. Immunization by the intranasal route was slightly better than that by the intramuscular route. Protection was considered specific, since immunization with P. multocida protected only against P. multocida and not against Salmonella agona. Furthermore, a similar KSCN extract from P. haemolytica did not protect against P. multocida challenge. A comparison of the KSCN extract with a Formalin-killed bacterin suggested that the KSCN extract may be superior to the bacterin.

Administration, Intranasal↗
PubMed1981

Neuraminidase activity of Pasteurella haemolytica isolates.

Neuraminidase activities of Pasteurella haemolytica cell suspensions were measured. Type isolates of the 12 established serotypes and bovine and ovine field isolates were included in the study. Neuraminidase activities ranged from 0 to 0.87 U per mg (dry weight) of P. haemolytica. Activity levels among the isolates studied were serotype associated.

Animals↗
PubMed1983

Fate of Pasteurella hemolytica in conventionally raised and germfree mice.

When Pasteurella hemolytica was introduced into conventionally raised ICR mice by a variety of routes (intraperitoneal, aerogenic, and oral), the inoculum was rapidly eliminated, and none of the mice died. Even when the inoculum was injected intraperitoneally into sublethally irradiated (600 rads) mice, the organisms were eliminated rapidly unless suspended in 10% hog gastric mucin. When germfree ICR mice were orally infected with P. hemolytica, the infection established itself in the intestinal tract and spread to the mesenteric lymph nodes but did not progress beyond this point. Despite the inability of P. hemolytica to establish itself systemically, the organism multiplied freely in mouse blood and a homogenate of normal mouse lung in vitro. Normal mouse peritoneal macrophages could phagocytose P. hemolytica in vitro, although not as efficiently as the control Listeria monocytogenes suspensions. The addition of hyperimmune bovine serum (opsonin) to the P. hemolytica suspension increased phagocytosis but did not greatly affect the subsequent bactericidal activity of the macrophages in vitro. The reason for the lack of pathogenicity shown by P. hemolytica in normal mice remains enigmatic.

Animals↗
PubMed1984

Naturally occurring pasteurellosis in laboratory rabbits: chemical and serological studies of whole cells and lipopolysaccharides of Pasteurella multocida.

Whole cells and lipopolysaccharides (LPS) of 10 isolates of Pasteurella multocida from laboratory rabbits were subjected to chemical and serological analysis. LPS of most of these isolates possessed pyrogenic potency comparable to LPS from Salmonella minnesota 9700, although their average ketodeoxyoctonate content was only 18% of that of salmonella. A gel diffusion precipitin test for somatic antigens extracted in a formal-saline solution demonstrated several isolates with three to four somatic antigens, with some variation in the major somatic type from one test to another. Conversely, the use of LPS as antigen in the gel diffusion precipitin test (i) eliminated cross-reactivity with reference antisera and (ii) often resulted in the organism being typed as serotype 12 even when the type 12 antigen was a minor antigen in the formal-saline extracts. Antisera from specific pathogen-free rabbits immunized with either whole cells or LPS of two isolates were tested against whole cells of LPS of the 10 isolates by enzyme immunoassay and indirect hemagglutination. Both whole cells and LPS of one of the isolates (isolate 2) were serologically specific, whereas those of the other isolate (isolate 1) were moderately to strongly cross-reactive with other isolates. The data indicate that although LPS is the major antigen responsible for typing based on the gel diffusion precipitin test, substances other than LPS (probably capsular polysaccharide) are responsible for the type specificity that forms the basis for the A, B, D, or E classification of this organism.

Animal Diseases↗
PubMed1984

Atrophic rhinitis in swine: correlation of Pasteurella multocida pathogenicity with membrane protein and lipopolysaccharide patterns.

Cell envelope proteins and lipopolysaccharides (LPS) of Pasteurella multocida strains associated with atrophic rhinitis in swine were compared by using sodium dodecyl sulfate gel electrophoresis. Among 34 strains, three different types of cell envelope protein patterns, named I (16 strains), II (3 strains), and III (15 strains), could be distinguished. These differences were based on the electrophoretic mobility of the major protein, designated as protein H. Comparison of cell envelope protein type and pathogenicity of the strain, the latter property predicted by the guinea pig skin test, revealed that all type I strains, 6 of 15 type III strains, and none of the type II strains were pathogenic. Although pathogenicity has been correlated with extracellular toxin activity, no protein could be detected in either the cell envelopes or in the extracellular fluid that absolutely correlated with pathogenic strains. Electrophoretic analysis of the LPS revealed that all strains possessed low-molecular-weight LPS, which is inconsistent with the presence of a classical O antigen. The method allowed the detection of at least six types of LPS, which often coincided with a certain cell envelope protein type and with the presence or absence of the pathogenic character of the strain. These results strongly suggest that the sampled swine carry a limited number of P. multocida clones, in each of which the patterns of cell envelope proteins and LPS, as well as the presence or absence of the ability to produce extracellular toxin, are well conserved. Therefore, the possibility is discussed that sodium dodecyl sulfate gel electrophoresis of cell envelope proteins and LPS may be used for the prediction of the pathogenic character of part of the strains. Finally, the typing of strains based on cell envelope protein patterns might contribute to the development of vaccines containing outer membrane proteins as protective antigens.

Animals↗
PubMed1986

Pasteurellosis in laboratory rabbits: characterization of lipopolysaccharides of Pasteurella multocida by polyacrylamide gel electrophoresis, immunoblot techniques, and enzyme-linked immunosorbent assay.

The lipopolysaccharides (LPSs) of five isolates of Pasteurella multocida from rabbits were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunoblots, and enzyme-linked immunosorbent assay. Silver-stained sodium dodecyl sulfate-polyacrylamide gel electrophoresis profiles of purified unaggregated LPSs resembled those of semirough strains of gram-negative enterobacteria and consisted of one or two bands that migrated within an interval just ahead or slightly behind the migration of the Ra chemotype of "Salmonella minnesota," which has a molecular size of 4.3 kilodaltons. Polyclonal rabbit antisera to P. multocida whole cells used in Western blots and enzyme-linked immunosorbent assays of unabsorbed and LPS-absorbed antisera revealed that the LPS of these isolates of P. multocida contained at least two types of antigens: a nonserospecific antigen and a serospecific antigen. The LPSs of four isolates each had a different serospecific antigen. The nonserospecific antigen was expressed in two isolates and was the only demonstrable LPS antigen in one other isolate.

Animals↗
PubMed1987

A potassium thiocyanate extract vaccine prepared from Pasteurella multocida 3:A protects rabbits against homologous challenge.

Potassium thiocyanate extracts of a virulent Pasteurella multocida 3:A rabbit isolate were prepared and used as a vaccine in rabbits. The extract contained protein, carbohydrate, hyaluronic acid, lipopolysaccharide, DNA, and RNA. The protein and lipopolysaccharide profiles of the extract were similar to those of the P. multocida cell membrane. Rabbits were vaccinated intranasally (i.n.) or intramuscularly (i.m.) four times at 1- or 3-week intervals and challenged i.n. with the homologous P. multocida 2 weeks after the last vaccination. Rabbits vaccinated with the extract by the i.n. route developed persisting serum immunoglobulin G (IgG) and nasal IgA antibodies, whereas rabbits immunized by the i.m. route produced persisting serum IgG and transient nasal IgA antibodies. The extract prevents the death of rabbits which were vaccinated by either route and challenged. Vaccination by the i.n. route in rabbits reduced the numbers of virulent P. multocida in nasal cavities and lungs and the prevalence and severity of rhinitis and pneumonia. These i.n.-vaccinated rabbits were also resistant to virulent P. multocida colonization in liver, spleen, uterus, and tympanic bullae. Similarly, i.m. vaccination in rabbits resulted in a reduction in the severity of rhinitis; the numbers of virulent P. multocida in lungs; and the prevalence of colonization in liver, spleen, uterus, and tympanic bullae. Vaccination by the i.n. route was superior to that by the i.m. route in that there was a significant reduction in the severity of pneumonia and numbers of virulent P. multocida in nasal cavities and lungs. Rabbits vaccinated with the extract without challenge showed no lesions.

Administration, Intranasal↗
PubMed1989

Pasteurella haemolytica antigens associated with resistance to pneumonic pasteurellosis.

Antigens associated with whole Pasteurella haemolytica biotype A serotype 1, a capsular carbohydrate-protein extract of the organism, and P. haemolytica leukotoxin were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Antigens of the electrophoresed preparations were detected by Western blotting (immunoblotting) with sera from cattle which were either nonvaccinated or vaccinated with live or killed P. haemolytica vaccines and had variable degrees of resistance to experimental pneumonic pasteurellosis. Distinct, easily recognizable antigens of these preparations were identified, and the antibody responses to these antigens were quantified by densitometry. To determine their importance to disease resistance, we then compared antibody responses with experimental lesion scores. Antibody reactivity to surface antigens which were significantly correlated with resistance and present in two or more of the preparations were detected at 86, 66, 51, 49, 34, 31, and 16 kilodaltons (kDa). Of these, antibody responses to antigens at 86, 49, and 31 kDa appeared most important based on their concentration and significance levels. Antibody reactivity to leukotoxin antigens which were significantly correlated with resistance and common with important surface antigens were detected at 86, 66, and 49 kDa. Antibody responses to unique leukotoxin antigens which were significantly correlated with resistance were present at 92 and 58 kDa.

Animals↗
PubMed1990

Bovine pulmonary endothelial cell damage mediated by Pasteurella haemolytica pathogenic factors.

The in vitro effects of Pasteurella haemolytica components on bovine pulmonary endothelial monolayers were investigated to determine the relative role of individual bacterial factors in the pathogenesis of bovine pulmonary pasteurellosis. Bovine pulmonary endothelial monolayers were treated with P. haemolytica bacterial culture supernatant (CS) and P. haemolytica lipopolysaccharide. At 22 h postinoculation, the CS produced severe damage to the endothelial cells, indicated by high 51Cr release, extensive cellular detachment, and morphologic changes characterized by cell contraction, cytoplasmic blebbing, and loss of monolayer confluency. The neutralization of leukotoxin activity of the CS by heat inactivation was ineffective in decreasing the damage to endothelial cells; however, leukotoxin-neutralizing monoclonal antibody slightly diminished the toxic effect. P. haemolytica lipopolysaccharide by itself or as a supplement to CS produced endothelial cell damage similar to that of CS. The preincubation of CS dilutions (10(-1) and 10(-2)) or P. haemolytica lipopolysaccharide with polymyxin B almost completely eliminated cell toxicity. These studies show that P. haemolytica produces a soluble factor that is consistent with bacterial lipopolysaccharide and that is directly toxic to bovine pulmonary endothelial cells in vitro.

Animals↗
PubMed1991

A monoclonal antibody against a Pasteurella multocida outer membrane protein protects rabbits and mice against pasteurellosis.

Monoclonal antibodies (MAbs) directed against the 37.5-kDa outer membrane protein were produced by fusing myeloma cells with spleen cells obtained from mice immunized with a pathogenic strain of Pasteurella multocida isolated from a rabbit. Desirable MAbs were selected by enzyme-linked immunosorbent assay, whole-cell radioimmunoprecipitation (WC-RIP), and Western blot (immunoblot) analysis. WC-RIP and Western blot analyses, using MAb 1608 adsorbed with intact P. multocida cells and the eluted MAb, demonstrated that the antigen recognized by this MAb is exposed on the cell surface, is antibody accessible, and has an estimated molecular mass of 37.5 kDa. Treatment of outer membrane vesicles of P. multocida with proteinase K totally abrogated the MAb 1608 activity, indicating that this MAb binds to a protein antigenic determinant. Furthermore, MAb 1608 was nonreactive to purified lipopolysaccharide in Western blot analysis. Passive transfer studies showed that nine rabbits inoculated intranasally with MAb 1608 and homologously challenged intranasally had significantly reduced mortality, severity of pneumonia, prevalence of P. multocida colonization in nonrespiratory organs, and numbers of P. multocida in nasal cavities compared with the controls. Furthermore, the number of P. multocida in lungs was reduced 84,750-fold. Similarly, passive transfer experiments indicated that MAb 1608 protected mice against homologous and heterologous challenges with P. multocida strains bearing the antigenic determinant recognized by MAb 1608. However, no protection was afforded by MAb 1608 when mice were challenged with a P. multocida strain lacking the antigenic determinant recognized by MAb 1608. This study establishes that the 37.5-kDa outer membrane protein is the target for a protective MAb.

Animals↗
PubMed1991

The outer membrane of Pasteurella multocida 3:A protects rabbits against homologous challenge.

The protective efficacy of a vaccine purified from the Pasteurella multocida 3:A outer membrane (OM) was evaluated in rabbits by homologous challenge. Twenty-seven rabbits were divided into four groups: 1, vaccinated with OM and challenged; 2, nonvaccinated and challenged; 3, vaccinated with OM only; and 4, nonvaccinated and not challenged. Rabbits were immunized intranasally with 1 mg of OM protein on days 0, 7, 14, and 35, challenged intranasally on day 49, and killed on day 63. Mortality rates were 0, 67, 0, and 0% for groups 1 through 4, respectively. The prevalence of pneumonia was reduced from 73 (group 2) to 20% (group 1). The severity of pneumonia was reduced from 0.62 (group 2) to 0.07 (group 1), as measured by the group lesion index. The number of P. multocida in nasal cavities was reduced from 3.89 x 10(5) (group 2) to 6.19 x 10(2) (group 1). The geometric mean number of P. multocida in lungs was 8,360,000-fold less in group 1 than in group 2. Similarly, the prevalence of P. multocida colonization in nonrespiratory organs was reduced from 47 (group 2) to 4% (group 1). Furthermore, group 1 and 3 rabbits developed significantly elevated immunoglobulin A antibodies in nasal secretions and lung lavages and significantly elevated immunoglobulin G antibodies in lung lavages and sera. In addition, rabbit immune sera contained antibodies against P. multocida OM proteins and lipopolysaccharides and inhibited P. multocida proliferation in mouse lungs. These results indicate that a vaccine prepared from the OM of P. multocida provides a significant protection in rabbits against homologous challenge.

Animals↗
PubMed1992

Use of restriction endonuclease analysis and ribotyping to study epidemiology of Pasteurella multocida in closed swine herds.

One hundred and sixty-four clinical isolates of Pasteurella multocida recovered from two swine herds in Minnesota were characterized by restriction endonuclease analysis (REA) and rRNA gene restriction fragment length patterns. Bacterial DNA was digested with HpaII and electrophoresed in 0.55% agarose. Restriction fragments were transferred by Southern blot to nylon membranes and then hybridized with digoxigenin-dUTP-labeled Escherichia coli rRNA. Four different REA patterns were observed among the 156 serotype A strains isolated from herds A and B. The two most common REA types (1 and 2) represented 92% of the strains analyzed, while REA types 3 and 4 were observed only in lung samples and accounted for 8% of the isolates. Two different ribotypes were observed for these serotype A isolates. Ribotype I consisted of the most common types, 1 and 2, found by DNA fingerprinting. Ribotype II included REA types 3 and 4. Results from both herds suggest that in closed swine populations, a single strain of P. multocida predominates and causes disease. It is concluded that these genomic fingerprinting techniques were highly discriminatory and that capsular serotyping in combination with REA or ribotyping is an appropriate technique for epidemiological studies of P. multocida of swine origin.

Animals↗
PubMed1996

Cloning, sequencing, expression, and protective capacity of the oma87 gene encoding the Pasteurella multocida 87-kilodalton outer membrane antigen.

Membrane proteins of Pasteurella multocida have been shown previously to elicit protective immunity. We have identified an 87-kDa outer membrane antigen, Oma87, which is present in all 16 serotypes of P. multocida. The gene encoding this protein was cloned and sequenced and found to have significant similarity to the D15 protective surface antigen of Haemophilus influenzae. Oma87 was localized to the outer membrane of the cell, and proteinase K treatment suggested that the protein is surface exposed. Native and recombinant Oma87 were strongly immunostained by convalescent-phase antiserum, indicating that the protein is expressed in vivo. Specific Oma87 antiserum protected mice against homologous, lethal P. multocida challenge. These results suggest that Oma87 is a protective outer membrane antigen of P. multocida.

Amino Acid Sequence↗
PubMed1998

Induction of protective immunity in rabbits by coadministration of inactivated Pasteurella multocida toxin and potassium thiocyanate extract.

Pasteurella multocida is a bacterial pathogen that causes rhinitis (snuffles), pneumonia, otitis media, septicemia, metritis, and death in domestic rabbits. Currently, there are no effective vaccines to prevent infection by this organism. Subcutaneous (s.c.) immunization with either exotoxin or thiocyanate extracts of P. multocida induces partial protection in rabbits. Since disease begins at mucosal sites, induction of local immunity may be important in preventing systemic disease. Little is known concerning the efficacy of intranasal (i.n. ) administration of these antigens in inducing protective mucosal immunity to P. multocida in rabbits. The purpose of this study was twofold: (i) to investigate the effectiveness of vaccination with purified P. multocida toxin (PMT) and a potassium thiocyanate extract of P. multocida (CN) in combination and (ii) to evaluate the efficacy of administration of these antigens i.n. versus s.c. Forty-eight rabbits were randomly divided into eight different treatment groups. Rabbits received either one or both antigens by either s.c. or i.n. administration. Following vaccination, each group received an i.n. challenge of P. multocida. Rabbits vaccinated with both antigens i.n. or s.c. had a 100% survival rate, few or no bacteria in the liver and lungs, high serum immunoglobulin G (IgG) and IgM antibody titers, and significant numbers of IgG antibody-secreting cells (ASC) in the spleen and tracheobronchial lymph node. Rabbits vaccinated i.n. had significant nasal and bronchoalveolar lavage IgA antibody levels. Rabbits vaccinated with only one antigen, either PMT or CN, had lower antibody titers, moderate to severe liver and lung infections, and fewer ASC compared to rabbits receiving both antigens. Rabbits in the control groups had moderate to severe liver and lung infections. This study indicates that i.n. immunization with both PMT and CN induces an effective response against homologous P. multocida challenge.

Animals↗
PubMed2000

The capsule is a virulence determinant in the pathogenesis of Pasteurella multocida M1404 (B:2).

Capsules from a range of pathogenic bacteria are key virulence determinants, and the capsule has been implicated in virulence in Pasteurella multocida. We have previously identified and determined the nucleotide sequence of the P. multocida M1404 (B:2) capsule biosynthetic locus (J. D. Boyce, J. Y. Chung, and B. Adler, Vet. Microbiol. 72:121-134, 2000). The cap locus consists of 15 genes, which can be grouped into three functional regions. Regions 1 and 3 contain genes proposed to encode proteins involved in capsule export, and region 2 contains genes proposed to encode proteins involved in polysaccharide biosynthesis. In order to construct a mutant impaired in capsule export, the final gene of region 1, cexA, was disrupted by insertion of a tetracycline resistance cassette by allelic replacement. The genotype of the tet(M) OmegacexA mutant was confirmed by Southern hybridization and PCR. The acapsular phenotype was confirmed by immunofluorescence, and the strain could be complemented and returned to capsule production by the presence of a cloned uninterrupted copy of cexA. Wild-type, mutant, and complemented strains were tested for virulence by intraperitoneal challenge of mice; the presence of the capsule was shown to be a crucial virulence determinant. Following intraperitoneal challenge of mice, the acapsular bacteria were removed efficiently from the blood, spleen, and liver, while wild-type bacteria multiplied rapidly. Acapsular bacteria were readily taken up by murine peritoneal macrophages, but wild-type bacteria were significantly resistant to phagocytosis. Both wild-type and acapsular bacteria were resistant to complement in bovine and murine serum.

Animals↗
PubMed2001

Acapsular Pasteurella multocida B:2 can stimulate protective immunity against pasteurellosis.

We have previously shown that a Pasteurella multocida cexA mutant (PBA875) was impaired in capsule export and highly attenuated in virulence for mice (J. D. Boyce and B. Adler, Infect. Immun. 68:3463-3468, 2000). In this study we show that immunization with high, but not low, doses of PBA875 can confer significant protection against wild-type challenge. We have also constructed a genetically defined acapsular P. multocida strain (AL18) by inactivation of bcbH, a gene predicted to be involved in polysaccharide biosynthesis. AL18 failed to produce immunoreactive polysaccharide as determined by immunofluorescence and Western immunoblot. Immunization of mice with live AL18 conferred significant protection against wild-type challenge, while immunization with similar doses of either killed wild-type or killed AL18 failed to confer protection.

Animals↗
PubMed2001

Role of capsule in the pathogenesis of fowl cholera caused by Pasteurella multocida serogroup A.

We have constructed a defined acapsular mutant in Pasteurella multocida X-73 (serogroup A:1) by disrupting the hexA gene through the insertion of a tetracycline resistance cassette. The genotype of the hexA::tet(M) strain was confirmed by PCR and Southern hybridization, and the acapsular phenotype of this strain was confirmed by electron microscopy. The hexA::tet(M) strain was attenuated in both mice and chickens. Complementation of the mutant with an intact hexAB fragment restored lethality in mice but not in chickens. In contrast to the results described previously for P. multocida serogroup B (J. D. Boyce and B. Adler, Infect. Immun. 68:3463-3468, 2000), the hexA::tet(M) strain was sensitive to the bactericidal action of chicken serum, whereas the wild-type and complemented strains were both resistant. Following inoculation into chicken muscle, the bacterial count of the hexA::tet(M) strain decreased significantly, while the wild-type and complemented strains both grew rapidly over 4 h. The capsule is thus an essential virulence determinant in the pathogenesis of fowl cholera.

Animals↗
PubMed2002

Characterization of the Pasteurella multocida hgbA gene encoding a hemoglobin-binding protein.

Reverse transcriptase PCR analyses have demonstrated that open reading frames (ORFs) PM0298, PM0299, and PM0300 of the animal pathogen Pasteurella multocida constitute a single transcriptional unit. By cloning and overexpression studies in Escherichia coli cells, the product of ORF PM0300 was shown to bind hemoglobin in vitro; this ORF was therefore designated hgbA. In vitro and in vivo quantitative assays demonstrated that the P. multocida hgbA mutant bound hemoglobin to the same extent as the wild-type strain, although the adsorption kinetics was slightly slower for the hgbA cells. In agreement with this, the virulence of P. multocida hgbA cells was not affected, suggesting that other functional hemoglobin receptor proteins must be present in this organism. On the other hand, P. multocida mutants defective in PM0298 and PM0299 could be isolated only when a plasmid containing an intact copy of the gene was present in the cells, suggesting that these genes are essential for the viability of this bacterial pathogen. By adapting the recombinase-based expression technology in vivo to P. multocida, we also demonstrated that the transcriptional PM0298-PM0299-hgbA unit is iron regulated and that its expression is triggered in the first 2 h following infection in a mouse model. Furthermore, hybridization experiments showed that the hgbA gene is widespread in P. multocida strains regardless of their serotype or the animal from which they were isolated.

Bacterial Outer Membrane Proteins↗