Molecular Characterization and Baculovirus Expression of the Glycoprotein B of a Seal Herpesvirus (Phocid Herpesvirus-1)
Identifieur interne : 003D45 ( Main/Exploration ); précédent : 003D44; suivant : 003D46Molecular Characterization and Baculovirus Expression of the Glycoprotein B of a Seal Herpesvirus (Phocid Herpesvirus-1)
Auteurs : T. C. Harder [Pays-Bas] ; A. D. M. E. Osterhaus [Pays-Bas]Source :
- Virology [ 0042-6822 ] ; 1997.
English descriptors
- Teeft :
- Academic press, Amino, Amino acid sequence, Amino acid sequences, Antarctic seals, Assay, Bacpbgb, Baculovirus, Baculovirus system, Bamhi fragment, Boehringer mannheim, Cell lysates, Cell surface, Cell surface expression, Cleavage, Cleavage products, Crfk, Crfk cells, Different species, Endo, Equivalent gene, Erasmus university rotterdam, Eukaryotic cells, Evolutionary relationship, Exocytic pathway, Facs analysis, Gene homologue, Genus, Glycoprotein, Glycosylated molecule, Golgi apparatus, Harbour seals, Herpes, Herpes simplex virus, Herpes simplex virus type, Herpesvirus, Herpesviruses, High fidelity, Important pathogen, Insect cells, Kidney cells, Lebich, Limbach, Ling chan, Mabs, Molecular masses, Neutralizing antibodies, Nucleic acids, Nucleotide, Nucleotide sequence, Open reading frames, Osterhaus, Other members, Partial characterization, Phoca, Phoca fasciata, Phoca vitulina, Phocid, Phocid herpesvirus, Pinniped, Polyadenylation signal, Polyhedrin promoter, Precursor, Precursor molecules, Proteolytic, Proteolytic cleavage, Proteolytic fragments, Pseudorabies virus, Recombinant, Recombinant bacpbgb, Ribbon seal, Seal herpesvirus, Seal sera, Sequence analysis, Simplex, Software package, Specific primers, Standard procedures, Vaccine, Varicellovirus, Varicellovirus genus, Various pinniped sera, Vira, Viral, Viral glycoproteins, Virol, Virology, Virology phocid glycoprotein.
Abstract
Abstract: A glycoprotein B (gB) gene homologue was identified in a 5.4-kbBamHI genomic fragment of the phocid herpesvirus type-1 (PhHV-1) which represents a widespread and important pathogen of pinnipeds. Sequence analysis revealed a gB-specific open-reading frame comprising 881 amino acids. Phylogenetic analysis gave evidence for a close evolutionary relationship between PhHV-1 and members of theVaricellovirusgenus of the α-Herpesvirinaeand canid herpesvirus in particular. In PhHV-1-infected Crandell feline kidney cells gB is expressed as a 113-kDa glycosylated molecule which is proteolytically cleaved into at least two fragments of 67 and 53–59 kDa apparently forming disulfide-linked heterodimers of 140 kDa. Cell surface expression of PhHV-1 gB was confirmed by FACS analysis. Thus, synthesis and processing of the gB protein of PhHV-1 follows a pattern also observed in otherVaricelloviruses.Since the gB protein of herpesviruses, expressed in the baculovirus system, has been shown to be a suitable target for vaccine design, we used this system for expression of PhHV-1 gB. Recombinant (rec) baculovirus-expressed gB was identified as a 105-kDa glycosylated molecule. Proteolytic cleavage into fragments of 62 and 52 kDa was markedly delayed compared to wild-type (wt) gB. Wt and rec gB harbored endoglycosidase H (precursor)- as well as N-glycosidase F-sensitive N-glycans (proteolytic fragments). Baculovirus-expressed gB appeared to be antigenically authentic, since it was recognized in radioimmunoprecipitation and immune peroxidase monolayer assays by PhHV-1-neutralizing seal sera and by gB-specific neutralizing murine monoclonal antibodies. Furthermore, PhHV-1-neutralizing antibodies were induced in mice following immunization with baculovirus-expressed gB, indicating its suitability for incorporation in a candidate vaccine for seals.
Url:
DOI: 10.1006/viro.1996.8332
Affiliations:
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Sequence analysis revealed a gB-specific open-reading frame comprising 881 amino acids. Phylogenetic analysis gave evidence for a close evolutionary relationship between PhHV-1 and members of theVaricellovirusgenus of the α-Herpesvirinaeand canid herpesvirus in particular. In PhHV-1-infected Crandell feline kidney cells gB is expressed as a 113-kDa glycosylated molecule which is proteolytically cleaved into at least two fragments of 67 and 53–59 kDa apparently forming disulfide-linked heterodimers of 140 kDa. Cell surface expression of PhHV-1 gB was confirmed by FACS analysis. Thus, synthesis and processing of the gB protein of PhHV-1 follows a pattern also observed in otherVaricelloviruses.Since the gB protein of herpesviruses, expressed in the baculovirus system, has been shown to be a suitable target for vaccine design, we used this system for expression of PhHV-1 gB. Recombinant (rec) baculovirus-expressed gB was identified as a 105-kDa glycosylated molecule. Proteolytic cleavage into fragments of 62 and 52 kDa was markedly delayed compared to wild-type (wt) gB. Wt and rec gB harbored endoglycosidase H (precursor)- as well as N-glycosidase F-sensitive N-glycans (proteolytic fragments). Baculovirus-expressed gB appeared to be antigenically authentic, since it was recognized in radioimmunoprecipitation and immune peroxidase monolayer assays by PhHV-1-neutralizing seal sera and by gB-specific neutralizing murine monoclonal antibodies. Furthermore, PhHV-1-neutralizing antibodies were induced in mice following immunization with baculovirus-expressed gB, indicating its suitability for incorporation in a candidate vaccine for seals.</div></front></TEI><affiliations><list><country><li>Pays-Bas</li></country><region><li>Hollande-Méridionale</li></region><settlement><li>Rotterdam</li></settlement></list><tree><country name="Pays-Bas"><region name="Hollande-Méridionale"><name sortKey="Harder, T C" sort="Harder, T C" uniqKey="Harder T" first="T. C." last="Harder">T. C. Harder</name></region><name sortKey="Osterhaus, A D M E" sort="Osterhaus, A D M E" uniqKey="Osterhaus A" first="A. D. M. E." last="Osterhaus">A. D. M. E. Osterhaus</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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