Protein pI alteration related to strain variation of infectious bronchitis virus, an avian Coronavirus
Identifieur interne : 001B74 ( Main/Exploration ); précédent : 001B73; suivant : 001B75Protein pI alteration related to strain variation of infectious bronchitis virus, an avian Coronavirus
Auteurs : Eileen C. Sadasiv [États-Unis] ; Tamson T. Yeh [États-Unis] ; Pei W. Chang [États-Unis]Source :
- Journal of Virological Methods [ 0166-0934 ] ; 1991.
English descriptors
- Teeft :
- Amino, Amino acids, Antigenic, Antigenic variants, Avian, Avian coronavirus, Avian diseases, Bronchitis, Cavanagh, Charge neutrality, Coronavirus, Doublet band, Electric field, Electron microscopy, Embryonated eggs, Epitope, Glycosylation, Greater number, Infectious bronchitis virus, Isoelectric, Isoelectric points, Isopycnic centrifugation, Kusters, Major proteins, Mass proteins, Minor band, Minor protein bands, Monoclonal antibodies, Northeastern conference, Nucleic acids, Peplomer, Peplomer protein, Peplomer proteins, Persistent infection, Plenum press, Potential glycosylation sites, Protective antibody, Protein, Rhode island, Serological tests, Several copies, Specific reaction, Spike, Spike protein, Strain variation, Structural proteins, Subunit, Sucrose cushion, Tissue affinity, Variant, Variant band, Veterinary science, Viral, Viral proteins, Virus, Virus samples, Visible bands, Western blot.
Abstract
Abstract: Viral proteins of two strains of infectious bronchitis virus (IBV), which have different tissue trophism and serology, were separated on the basis of their isoelectric points (pI). The viruses have four structural proteins; the protein of greatest serological importance is found at the peplomer tip. The viral structural proteins separated by isoelectric focusing were identified by comparison to SDS-PAGE separations. Three protein bands were identical in pI and one protein band showed a difference in pI between strains. When the renatured viral proteins were Western blotted and reacted with strain-specific antiserum, antigen-antibody complexing was seen only at points corresponding to the strain-specific variant bands. For IBV strain Mass-41, antigen-antibody complexing occurred at a pI of 6.8, and, for IBV strain Ark-99, at 7.2. No cross reaction of antisera was observed for either strain.Since tissue affinities are a function of the viral peplomer-mediated attachment of virus to cells and are often directly related to pathogenicity, it appears that altered pathogenicity of strains of IBV may be detected by alteration of pI of the proteins. Classification by pI of proteins of at least the smaller viruses allows untypeable, highly pathogenic or persistent strains of these viruses to be characterized on the basis of variant proteins.
Url:
DOI: 10.1016/0166-0934(91)90012-O
Affiliations:
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Sadasiv</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Fisheries, Animal and Veterinary Science, The University of Rhode Island, Kingston, Rhode Island</wicri:regionArea><placeName><region type="state">Rhode Island</region></placeName></affiliation></author><author><name sortKey="Yeh, Tamson T" sort="Yeh, Tamson T" uniqKey="Yeh T" first="Tamson T." last="Yeh">Tamson T. Yeh</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Fisheries, Animal and Veterinary Science, The University of Rhode Island, Kingston, Rhode Island</wicri:regionArea><placeName><region type="state">Rhode Island</region></placeName></affiliation></author><author><name sortKey="Chang, Pei W" sort="Chang, Pei W" uniqKey="Chang P" first="Pei W." last="Chang">Pei W. Chang</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Fisheries, Animal and Veterinary Science, The University of Rhode Island, Kingston, Rhode Island</wicri:regionArea><placeName><region type="state">Rhode Island</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Virological Methods</title><title level="j" type="abbrev">VIRMET</title><idno type="ISSN">0166-0934</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991">1991</date><biblScope unit="volume">33</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="115">115</biblScope><biblScope unit="page" to="125">125</biblScope></imprint><idno type="ISSN">0166-0934</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0166-0934</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino</term><term>Amino acids</term><term>Antigenic</term><term>Antigenic variants</term><term>Avian</term><term>Avian coronavirus</term><term>Avian diseases</term><term>Bronchitis</term><term>Cavanagh</term><term>Charge neutrality</term><term>Coronavirus</term><term>Doublet band</term><term>Electric field</term><term>Electron microscopy</term><term>Embryonated eggs</term><term>Epitope</term><term>Glycosylation</term><term>Greater number</term><term>Infectious bronchitis virus</term><term>Isoelectric</term><term>Isoelectric points</term><term>Isopycnic centrifugation</term><term>Kusters</term><term>Major proteins</term><term>Mass proteins</term><term>Minor band</term><term>Minor protein bands</term><term>Monoclonal antibodies</term><term>Northeastern conference</term><term>Nucleic acids</term><term>Peplomer</term><term>Peplomer protein</term><term>Peplomer proteins</term><term>Persistent infection</term><term>Plenum press</term><term>Potential glycosylation sites</term><term>Protective antibody</term><term>Protein</term><term>Rhode island</term><term>Serological tests</term><term>Several copies</term><term>Specific reaction</term><term>Spike</term><term>Spike protein</term><term>Strain variation</term><term>Structural proteins</term><term>Subunit</term><term>Sucrose cushion</term><term>Tissue affinity</term><term>Variant</term><term>Variant band</term><term>Veterinary science</term><term>Viral</term><term>Viral proteins</term><term>Virus</term><term>Virus samples</term><term>Visible bands</term><term>Western blot</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Viral proteins of two strains of infectious bronchitis virus (IBV), which have different tissue trophism and serology, were separated on the basis of their isoelectric points (pI). The viruses have four structural proteins; the protein of greatest serological importance is found at the peplomer tip. The viral structural proteins separated by isoelectric focusing were identified by comparison to SDS-PAGE separations. Three protein bands were identical in pI and one protein band showed a difference in pI between strains. When the renatured viral proteins were Western blotted and reacted with strain-specific antiserum, antigen-antibody complexing was seen only at points corresponding to the strain-specific variant bands. For IBV strain Mass-41, antigen-antibody complexing occurred at a pI of 6.8, and, for IBV strain Ark-99, at 7.2. No cross reaction of antisera was observed for either strain.Since tissue affinities are a function of the viral peplomer-mediated attachment of virus to cells and are often directly related to pathogenicity, it appears that altered pathogenicity of strains of IBV may be detected by alteration of pI of the proteins. Classification by pI of proteins of at least the smaller viruses allows untypeable, highly pathogenic or persistent strains of these viruses to be characterized on the basis of variant proteins.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Rhode Island</li></region></list><tree><country name="États-Unis"><region name="Rhode Island"><name sortKey="Sadasiv, Eileen C" sort="Sadasiv, Eileen C" uniqKey="Sadasiv E" first="Eileen C." last="Sadasiv">Eileen C. Sadasiv</name></region><name sortKey="Chang, Pei W" sort="Chang, Pei W" uniqKey="Chang P" first="Pei W." last="Chang">Pei W. Chang</name><name sortKey="Yeh, Tamson T" sort="Yeh, Tamson T" uniqKey="Yeh T" first="Tamson T." last="Yeh">Tamson T. Yeh</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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