Recombinant Bovine Adenovirus Type 3 Expressing Bovine Viral Diarrhea Virus Glycoprotein E2 Induces an Immune Response in Cotton Rats
Identifieur interne : 001154 ( Main/Exploration ); précédent : 001153; suivant : 001155Recombinant Bovine Adenovirus Type 3 Expressing Bovine Viral Diarrhea Virus Glycoprotein E2 Induces an Immune Response in Cotton Rats
Auteurs : Mohit K. Baxi [Canada] ; Dirk Deregt [Canada] ; Jill Robertson [Canada] ; Lorne A. Babiuk [Canada] ; Tobias Schlapp [Allemagne] ; Suresh K. Tikoo [Canada]Source :
- Virology [ 0042-6822 ] ; 2000.
English descriptors
- Teeft :
- Adenovirus, Animal vaccination, Antibody response, Assay, Babiuk, Baxi, Bovine, Bovine adenovirus, Bovine adenovirus type, Bvdv, Complete medium, Cotton rats, Cytopathic effects, Diarrhea virus, E2ori, E2ori gene, Early region, Elisa, Elisa titers, Foreign gene, Genome, Glycoprotein, Harpin, Hcmv, Hcmv promoter, Immune, Immune response, Immune responses, Immunization, Immunoprecipitated, Immunoprecipitation, Immunoprecipitation analysis, Intranasal immunization, Ligated, Mdbk, Mdbk cells, Monoclonal antibodies, Mucosal, Mucosal immunization, Mucosal surfaces, Nasal washes, Nucleotide sequence, Plasmid, Postinfection, Promoter, Recombinant, Recombinant virus, Recombinant viruses, Reddy, Signal sequence, Splice sites, Tikoo, Vaccine, Viral, Virol, Virology, Zakhartchouk.
Abstract
Abstract: Recombinant bovine adenovirus is being developed as a live vector for animal vaccination and for human gene therapy. In this study, two replication-competent bovine adenovirus 3 (BAV-3) recombinants (BAV331 and BAV338) expressing bovine viral diarrhea virus (BVDV) glycoprotein E2 in the early region 3 (E3) of BAV-3 were constructed. Recombinant BAV331 contains chemically synthesized E2 gene (nucleotides modified to remove internal cryptic splice sites) under the control of BAV-3 E3/major late promoter (MLP), while recombinant BAV338 contains original E2 gene under the control of human cytomegalovirus immediate early promoter. Since E2, a class I membrane glycoprotein, does not contain its own signal peptide sequence at the 5′ end, the bovine herpesvirus 1 (BHV-1) glycoprotein D signal sequence was fused in frame to the E2 open reading frame (ORF) for proper processing of the E2 glycoprotein in both the recombinant viruses. Recombinant E2 protein expressed by BAV331 and BAV338 recombinant viruses was recognized by E2-specific monoclonal antibodies as a 53-kDa protein, which also formed dimer with an apparent molecular weight of 94 kDa. Insertion of an E2-expression cassette in the E3 region did not effect the replication of recombinant BAV-3s. Intranasal immunization of cotton rats with these recombinant viruses generated E2-specific IgA and IgG responses at the mucosal surfaces and in the serum. In summary, these results show that the pestivirus glycoprotein can be expressed efficiently by BAV-3. In addition, mucosal immunization with replication-competent recombinant bovine adenovirus 3 can induce a specific immune response against the expressed antigen.
Url:
DOI: 10.1006/viro.2000.0661
Affiliations:
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Tikoo</name><affiliation wicri:level="1"><country xml:lang="fr">Canada</country><wicri:regionArea>Virology Group, Veterinary Infectious Disease Organization, University of Saskatchewan, Saskatoon, Saskatchewan, S7N 5E3</wicri:regionArea><wicri:noRegion>S7N 5E3</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="2000">2000</date><biblScope unit="volume">278</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="234">234</biblScope><biblScope unit="page" to="243">243</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Adenovirus</term><term>Animal vaccination</term><term>Antibody response</term><term>Assay</term><term>Babiuk</term><term>Baxi</term><term>Bovine</term><term>Bovine adenovirus</term><term>Bovine adenovirus type</term><term>Bvdv</term><term>Complete medium</term><term>Cotton rats</term><term>Cytopathic effects</term><term>Diarrhea virus</term><term>E2ori</term><term>E2ori gene</term><term>Early region</term><term>Elisa</term><term>Elisa titers</term><term>Foreign gene</term><term>Genome</term><term>Glycoprotein</term><term>Harpin</term><term>Hcmv</term><term>Hcmv promoter</term><term>Immune</term><term>Immune response</term><term>Immune responses</term><term>Immunization</term><term>Immunoprecipitated</term><term>Immunoprecipitation</term><term>Immunoprecipitation analysis</term><term>Intranasal immunization</term><term>Ligated</term><term>Mdbk</term><term>Mdbk cells</term><term>Monoclonal antibodies</term><term>Mucosal</term><term>Mucosal immunization</term><term>Mucosal surfaces</term><term>Nasal washes</term><term>Nucleotide sequence</term><term>Plasmid</term><term>Postinfection</term><term>Promoter</term><term>Recombinant</term><term>Recombinant virus</term><term>Recombinant viruses</term><term>Reddy</term><term>Signal sequence</term><term>Splice sites</term><term>Tikoo</term><term>Vaccine</term><term>Viral</term><term>Virol</term><term>Virology</term><term>Zakhartchouk</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Recombinant bovine adenovirus is being developed as a live vector for animal vaccination and for human gene therapy. In this study, two replication-competent bovine adenovirus 3 (BAV-3) recombinants (BAV331 and BAV338) expressing bovine viral diarrhea virus (BVDV) glycoprotein E2 in the early region 3 (E3) of BAV-3 were constructed. Recombinant BAV331 contains chemically synthesized E2 gene (nucleotides modified to remove internal cryptic splice sites) under the control of BAV-3 E3/major late promoter (MLP), while recombinant BAV338 contains original E2 gene under the control of human cytomegalovirus immediate early promoter. Since E2, a class I membrane glycoprotein, does not contain its own signal peptide sequence at the 5′ end, the bovine herpesvirus 1 (BHV-1) glycoprotein D signal sequence was fused in frame to the E2 open reading frame (ORF) for proper processing of the E2 glycoprotein in both the recombinant viruses. Recombinant E2 protein expressed by BAV331 and BAV338 recombinant viruses was recognized by E2-specific monoclonal antibodies as a 53-kDa protein, which also formed dimer with an apparent molecular weight of 94 kDa. Insertion of an E2-expression cassette in the E3 region did not effect the replication of recombinant BAV-3s. Intranasal immunization of cotton rats with these recombinant viruses generated E2-specific IgA and IgG responses at the mucosal surfaces and in the serum. In summary, these results show that the pestivirus glycoprotein can be expressed efficiently by BAV-3. In addition, mucosal immunization with replication-competent recombinant bovine adenovirus 3 can induce a specific immune response against the expressed antigen.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Canada</li></country></list><tree><country name="Canada"><noRegion><name sortKey="Baxi, Mohit K" sort="Baxi, Mohit K" uniqKey="Baxi M" first="Mohit K." last="Baxi">Mohit K. Baxi</name></noRegion><name sortKey="Babiuk, Lorne A" sort="Babiuk, Lorne A" uniqKey="Babiuk L" first="Lorne A." last="Babiuk">Lorne A. Babiuk</name><name sortKey="Deregt, Dirk" sort="Deregt, Dirk" uniqKey="Deregt D" first="Dirk" last="Deregt">Dirk Deregt</name><name sortKey="Robertson, Jill" sort="Robertson, Jill" uniqKey="Robertson J" first="Jill" last="Robertson">Jill Robertson</name><name sortKey="Tikoo, Suresh K" sort="Tikoo, Suresh K" uniqKey="Tikoo S" first="Suresh K." last="Tikoo">Suresh K. Tikoo</name></country><country name="Allemagne"><noRegion><name sortKey="Schlapp, Tobias" sort="Schlapp, Tobias" uniqKey="Schlapp T" first="Tobias" last="Schlapp">Tobias Schlapp</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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