Glycosylation and antigenic variation among Kunjin virus isolates
Identifieur interne : 004177 ( Main/Exploration ); précédent : 004176; suivant : 004178Glycosylation and antigenic variation among Kunjin virus isolates
Auteurs : S. C. Adams [Australie] ; A. K. Broom [Australie] ; L. M. Sammels [Australie] ; A. C. Hartnett [Australie] ; M. J. Howard [Australie] ; R. J. Coelen [Australie] ; J. S. Mackenzie [Australie] ; R. A. Hall [Australie]Source :
- Virology [ 0042-6822 ] ; 1995.
English descriptors
- Teeft :
- Acid sequence, Aedes albopictus cells, Amino acids, Annulirostris, Antigenic, Antigenic type, Antigenic types, Antigenic variation, Assay, Binding pattern, Boort, Cell culture, Digestion, East kimberley, Encephalitis, Envelope protein, Enzyme activity, Epitope, Epitope analysis, Fiavivirus kunjin, Final concentration, Flavivirus, Glycosylated, Glycosylation, Glycosylation site, Glycosylation status, Host cell type, Huxsmb, Immunoperoxidase, Immunoperoxidase assay, Kimberley, Kunjin, Kunjin virus, Kunjin viruses, Mabs, Mitchell river mission, Monoclonal antibodies, Murray valley encephalitis virus, Nucleotide, Nucleotide sequence, Other flaviviruses, Passage experiments, Passage history, Phenotypic variation, Pngase, Potential glycosylation site, Room temperature, Same dilution, Sarafend strain, Sarawak, Serial passage, Single base substitution, Suckling, Suckling mouse brain, Suckling mouse brain passage, Tqtgaa tveshg, Tveshg, Undigested control, Undigested samples, Unglycosylated, Vero, Vero cells, Vero culture, Virol, Virus, Virus dilution, Wash buffer, West nile, West nile virus, Western australia, Western blot, Western blot analysis.
Abstract
Abstract: Previous studies have found Kunjin (KUN) virus isolates from within Australia to be genetically homogenous and that the envelope protein of the type strain (MRM61C) was unglycosylated and lacked a potential glycosylation site. We investigated the extent of antigenic variation between KUN virus isolates from Australia and Sarawak using an immunoperoxidase assay and a panel of six monoclonal antibodies. The glycosylation status of the E protein of each virus was also determined by N glycosidase F (PNGase F) digestion and limited sequence analysis. The results showed that KUN viruses isolated within Australia oscillated between three antigenic types defined by two epitopes whose expression was influenced by passage history and host cell type. In contrast an isolate from Sarawak formed a stable antigenic type that was not influenced by passage history and was distinct from all Australian isolates. PNGase F digestions of KUN isolates indicated that 19 of the 33 viruses possessed a glycosylated E protein. Nucleotide sequence of the 5′ third of the E gene of selected KUN isolates revealed that a single base change in PNGase F sensitive strains changed the tripeptide N-Y-F (amino acids 154–156 of the published sequence) to the potential glycosylation site N-Y-S. Further analysis revealed that passage history also had a significant influence on glycosylation.
Url:
DOI: 10.1016/S0042-6822(95)80018-2
Affiliations:
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C." last="Adams">S. C. Adams</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, The University of Western Australia, QEII Medical Centre, Nedlands WA 6009</wicri:regionArea><wicri:noRegion>Nedlands WA 6009</wicri:noRegion></affiliation></author><author><name sortKey="Broom, A K" sort="Broom, A K" uniqKey="Broom A" first="A. K." last="Broom">A. K. Broom</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, The University of Western Australia, QEII Medical Centre, Nedlands WA 6009</wicri:regionArea><wicri:noRegion>Nedlands WA 6009</wicri:noRegion></affiliation></author><author><name sortKey="Sammels, L M" sort="Sammels, L M" uniqKey="Sammels L" first="L. M." last="Sammels">L. M. Sammels</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, The University of Western Australia, QEII Medical Centre, Nedlands WA 6009</wicri:regionArea><wicri:noRegion>Nedlands WA 6009</wicri:noRegion></affiliation></author><author><name sortKey="Hartnett, A C" sort="Hartnett, A C" uniqKey="Hartnett A" first="A. C." last="Hartnett">A. C. Hartnett</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, The University of Western Australia, QEII Medical Centre, Nedlands WA 6009</wicri:regionArea><wicri:noRegion>Nedlands WA 6009</wicri:noRegion></affiliation></author><author><name sortKey="Howard, M J" sort="Howard, M J" uniqKey="Howard M" first="M. J." last="Howard">M. J. Howard</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, The University of Western Australia, QEII Medical Centre, Nedlands WA 6009</wicri:regionArea><wicri:noRegion>Nedlands WA 6009</wicri:noRegion></affiliation></author><author><name sortKey="Coelen, R J" sort="Coelen, R J" uniqKey="Coelen R" first="R. J." last="Coelen">R. J. Coelen</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, The University of Western Australia, QEII Medical Centre, Nedlands WA 6009</wicri:regionArea><wicri:noRegion>Nedlands WA 6009</wicri:noRegion></affiliation></author><author><name sortKey="Mackenzie, J S" sort="Mackenzie, J S" uniqKey="Mackenzie J" first="J. S." last="Mackenzie">J. S. Mackenzie</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, The University of Western Australia, QEII Medical Centre, Nedlands WA 6009</wicri:regionArea><wicri:noRegion>Nedlands WA 6009</wicri:noRegion></affiliation></author><author><name sortKey="Hall, R A" sort="Hall, R A" uniqKey="Hall R" first="R. A." last="Hall">R. A. Hall</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, The University of Western Australia, QEII Medical Centre, Nedlands WA 6009</wicri:regionArea><wicri:noRegion>Nedlands WA 6009</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="1995">1995</date><biblScope unit="volume">206</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="49">49</biblScope><biblScope unit="page" to="56">56</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>Acid sequence</term><term>Aedes albopictus cells</term><term>Amino acids</term><term>Annulirostris</term><term>Antigenic</term><term>Antigenic type</term><term>Antigenic types</term><term>Antigenic variation</term><term>Assay</term><term>Binding pattern</term><term>Boort</term><term>Cell culture</term><term>Digestion</term><term>East kimberley</term><term>Encephalitis</term><term>Envelope protein</term><term>Enzyme activity</term><term>Epitope</term><term>Epitope analysis</term><term>Fiavivirus kunjin</term><term>Final concentration</term><term>Flavivirus</term><term>Glycosylated</term><term>Glycosylation</term><term>Glycosylation site</term><term>Glycosylation status</term><term>Host cell type</term><term>Huxsmb</term><term>Immunoperoxidase</term><term>Immunoperoxidase assay</term><term>Kimberley</term><term>Kunjin</term><term>Kunjin virus</term><term>Kunjin viruses</term><term>Mabs</term><term>Mitchell river mission</term><term>Monoclonal antibodies</term><term>Murray valley encephalitis virus</term><term>Nucleotide</term><term>Nucleotide sequence</term><term>Other flaviviruses</term><term>Passage experiments</term><term>Passage history</term><term>Phenotypic variation</term><term>Pngase</term><term>Potential glycosylation site</term><term>Room temperature</term><term>Same dilution</term><term>Sarafend strain</term><term>Sarawak</term><term>Serial passage</term><term>Single base substitution</term><term>Suckling</term><term>Suckling mouse brain</term><term>Suckling mouse brain passage</term><term>Tqtgaa tveshg</term><term>Tveshg</term><term>Undigested control</term><term>Undigested samples</term><term>Unglycosylated</term><term>Vero</term><term>Vero cells</term><term>Vero culture</term><term>Virol</term><term>Virus</term><term>Virus dilution</term><term>Wash buffer</term><term>West nile</term><term>West nile virus</term><term>Western australia</term><term>Western blot</term><term>Western blot analysis</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Previous studies have found Kunjin (KUN) virus isolates from within Australia to be genetically homogenous and that the envelope protein of the type strain (MRM61C) was unglycosylated and lacked a potential glycosylation site. We investigated the extent of antigenic variation between KUN virus isolates from Australia and Sarawak using an immunoperoxidase assay and a panel of six monoclonal antibodies. The glycosylation status of the E protein of each virus was also determined by N glycosidase F (PNGase F) digestion and limited sequence analysis. The results showed that KUN viruses isolated within Australia oscillated between three antigenic types defined by two epitopes whose expression was influenced by passage history and host cell type. In contrast an isolate from Sarawak formed a stable antigenic type that was not influenced by passage history and was distinct from all Australian isolates. PNGase F digestions of KUN isolates indicated that 19 of the 33 viruses possessed a glycosylated E protein. Nucleotide sequence of the 5′ third of the E gene of selected KUN isolates revealed that a single base change in PNGase F sensitive strains changed the tripeptide N-Y-F (amino acids 154–156 of the published sequence) to the potential glycosylation site N-Y-S. Further analysis revealed that passage history also had a significant influence on glycosylation.</div></front></TEI><affiliations><list><country><li>Australie</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Adams, S C" sort="Adams, S C" uniqKey="Adams S" first="S. C." last="Adams">S. C. Adams</name></noRegion><name sortKey="Broom, A K" sort="Broom, A K" uniqKey="Broom A" first="A. K." last="Broom">A. K. Broom</name><name sortKey="Coelen, R J" sort="Coelen, R J" uniqKey="Coelen R" first="R. J." last="Coelen">R. J. Coelen</name><name sortKey="Hall, R A" sort="Hall, R A" uniqKey="Hall R" first="R. A." last="Hall">R. A. Hall</name><name sortKey="Hartnett, A C" sort="Hartnett, A C" uniqKey="Hartnett A" first="A. C." last="Hartnett">A. C. Hartnett</name><name sortKey="Howard, M J" sort="Howard, M J" uniqKey="Howard M" first="M. J." last="Howard">M. J. Howard</name><name sortKey="Mackenzie, J S" sort="Mackenzie, J S" uniqKey="Mackenzie J" first="J. S." last="Mackenzie">J. S. Mackenzie</name><name sortKey="Sammels, L M" sort="Sammels, L M" uniqKey="Sammels L" first="L. M." last="Sammels">L. M. Sammels</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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