Genomic Distribution of a Serotype 1‐Specific Antigen‐Coding DNA Fragment of <i>Pasteurella Haemolytica</i>

Gonzalez, Cynthia; Murtaugh, Michael P.; Maheswaran, S. K.

doi:10.1111/j.1439-0450.1991.tb00917.x

Cited by 11 publications

(19 citation statements)

References 17 publications

(16 reference statements)

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“…The gene encoding a serotype-specific outer membrane protein of P. haemolytica Al has also been isolated (6,12). Here, we report the cloning, * Corresponding author.…”

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confidence: 99%

“…P. haemolytica Al produces a number of antigens which are secreted into the culture supernatant during its growth. Some of these antigens include a heat-labile cytotoxin specific for ruminant leukocytes (24), a serotype-specific outer membrane protein (6,12), a glycoprotease specific for sialoglycoproteins (1,2,21), and a neuraminidase (5). Vaccination of calves with a bacterium-free culture supernatant from logarithmic-phase cultures induces resistance to experimental challenge, and a vaccine based on the culture supernatant has been developed (Presponse) (23,25).…”

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confidence: 99%

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Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene

Abdullah

Mellors

1991

J Bacteriol

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Pasteurella haemolytica serotype Al secretes a glycoprotease which is specific for 0-sialoglycoproteins such as glycophorin A. The gene encoding the glycoprotease enzyme has been cloned in the recombinant plasmid pPHl, and its nucleotide sequence has been determined. The gene (designated gcp) codes for a protein of 35.2 kDa, and an active enzyme protein of this molecular mass can be observed in Escherichia coli clones carrying pPHl. In vivo labeling of plasmid-encoded proteins in E. coli maxicells demonstrated the expression of a 35-kDa protein from pPHl. The amino-terminal sequence of the heterologously expressed protein corresponds to that predicted from the nucleotide sequence. The glycoprotease is a neutral metalloprotease, and the predicted amino acid sequence of the glycoprotease contains a putative zinc-binding site. The gene shows no significant homology with the genes for other proteases of procaryotic or eucaryotic origin. However, there is substantial homology between gcp and an E. coli gene, orJX, whose product is believed to function in the regulation of macromolecule biosynthesis.

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“…The gene encoding a serotype-specific outer membrane protein of P. haemolytica Al has also been isolated (6,12). Here, we report the cloning, * Corresponding author.…”

mentioning

confidence: 99%

mentioning

confidence: 99%

Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene

Abdullah

Mellors

1991

J Bacteriol

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“…We therefore undertook the goal of immunologically studying other OMPs identified through immunoproteomic analyses of M. haemolytica outer membrane preparations (4). These include SSA-1, OmpP2, OmpD15, and OmpA (6,19,22,31). M. haemolytica SSA-1 is an approximately 104-kDa OMP, and its gene was previously cloned and sequenced (19)(20)(21).…”

Section: Discussionmentioning

confidence: 99%

“…These include SSA-1, OmpP2, OmpD15, and OmpA (6,19,22,31). M. haemolytica SSA-1 is an approximately 104-kDa OMP, and its gene was previously cloned and sequenced (19)(20)(21). Sequence comparisons of that antigen demonstrated it to be an autotransporter serine protease belonging to the peptidase S8 or subtilase family (18,44).…”

Section: Discussionmentioning

confidence: 99%

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Immunogenicity of Mannheimia haemolytica Recombinant Outer Membrane Proteins Serotype 1-Specific Antigen, OmpA, OmpP2, and OmpD15

Ayalew

Shrestha

Montelongo

et al. 2011

Clin Vaccine Immunol

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We previously identified Mannheimia haemolytica outer membrane proteins (OMPs) that may be important immunogens by using immunoproteomic analyses. Genes for serotype 1-specific antigen (SSA-1), OmpA, OmpP2, and OmpD15 were cloned and expressed, and recombinant proteins were purified. Objective 1 of this study was to demonstrate immunogenicity of the four recombinant OMPs in mice and cattle. Objective 2 was to determine if the addition of individual recombinant OMPs or combinations of them would modify immune responsiveness of mice to the recombinant chimeric protein SAC89, containing the main epitope from M. haemolytica outer membrane lipoprotein PlpE and the neutralizing epitope of M. haemolytica leukotoxin. Mice vaccinated with recombinant OmpA (rOmpA), rSSA-1, rOmpD15, and rOmpP2 developed significant antibody responses to M. haemolytica outer membranes and to the homologous recombinant OMP. Cattle vaccinated with rOmpA and rSSA-1 developed significant antibodies to M. haemolytica outer membranes by day 28, whereas cattle vaccinated with rOmpD15 and rOmpP2 developed only minimal responses. Sera from cattle vaccinated with each of the recombinant proteins stimulated complement-mediated killing of the bacterium. Concurrent vaccination with SAC89 plus any of the four rOMPs singly resulted in increased endpoint anti-SAC89 titers, and for the SAC89/rSSA-1 vaccinees, the response was increased significantly. In contrast, the SAC89/P2/SSA-1 and SAC89/OmpA/P2/D15/SSA-1 combination vaccines resulted in significant decreases in anti-SAC89 antibodies compared to SAC89 vaccination alone. In conclusion, under the conditions of these experiments, vaccination of mice and cattle with rOmpA and rSSA-1 stimulated high antibody responses and may have protective vaccine potential.The major cause of severe bacterial pneumonia in cattle is Mannheimia haemolytica serotype 1 (S1), and current vaccines against M. haemolytica are only moderately efficacious (9, 36). Shewen and Wilkie (43) demonstrated that immunity against M. haemolytica requires antibodies against leukotoxin (LKT), which causes necrosis, apoptosis, or activation of ruminant leukocytes, as well as antibodies against bacterial cell surface antigens. The important surface immunogens needed to stimulate protective immunity against M. haemolytica appear to be outer membrane proteins (OMPs) (13,33,34,37,38).Our laboratory demonstrated that high antibody responses to a major 45-kDa outer membrane lipoprotein, PlpE, correlated with resistance against experimental challenge, and PlpE proteins were nearly identical among serotype 1 and serotype 6 isolates (2). Cattle vaccinated with commercial M. haemolytica vaccines to which 100 g of recombinant M. haemolytica S1 PlpE (rPlpE) was added had significantly greater resistance against experimental challenge with either S1 or S6 than did cattle vaccinated with the commercial vaccine alone (11, 12). The major epitope region of M. haemolytica S1 PlpE, designated region 2 (R2), consists of 8 imperfect hexapeptide repeats of QAQNAP loc...

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Immunoproteomic analyses of outer membrane proteins ofMannheimia haemolyticaand identification of potential vaccine candidates

et al. 2010

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Immunoproteomic analyses were used to characterize the outer membrane proteome of Mannheimia haemolytica, formerly Pasteurella haemolytica, serotype 1, and determine potential vaccine candidate proteins. 2-DE of M. haemolytica outer membranes was followed by immunoblot analyses using naïve and convalescent bovine sera. Proteins were identified using MALDI-TOF and LC-MS/MS. Spectral data was used to mine M. haemolytica protein database and 132 immunoreactive proteins were identified. Bioinformatic analysis using PSORTb, SubLoc, LipoP, BOMP, MCMBB, and TMB-Hunt/BBTM to predict subcellular localization of immunoreactive proteins and beta-barrels narrowed the list down to 55 candidates. Functional characterization of 55 proteins predicted 16 (29%) are involved in cell structure, 13 (23.6%) in transport/virulence, ten (18.2%) as unknown, six (10.9%) in general metabolism, four (7.27%) in cell process, two (3.64%) in translation, and one (1.8%) each in DNA replication, regulation, transcription, and virulence. Prediction of beta-barrel formation was between 11 and 31 immunoreactive proteins depending on the bioinformatic tool employed. Some of these proteins have potentials to be developed into stand-alone vaccines or components of vaccines. Of those proteins, several have already been characterized. Finally, although characteristics of many of M. haemolytica immunoreactive proteins identified in this study were obtained from published data and predictions using bioinformatics tools, five proteins previously listed in the published M. haemolytica sequence as unidentified were found to have correlates with functional proteins in other bacterial species.

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Genomic Distribution of a Serotype 1‐Specific Antigen‐Coding DNA Fragment of Pasteurella Haemolytica

Cited by 11 publications

References 17 publications

Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene

Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene

Immunogenicity of Mannheimia haemolytica Recombinant Outer Membrane Proteins Serotype 1-Specific Antigen, OmpA, OmpP2, and OmpD15

Immunoproteomic analyses of outer membrane proteins ofMannheimia haemolyticaand identification of potential vaccine candidates

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