Genetic variability of the glycoprotein genes of current wild-type measles isolates
Identifieur interne : 000D02 ( Istex/Checkpoint ); précédent : 000D01; suivant : 000D03Genetic variability of the glycoprotein genes of current wild-type measles isolates
Auteurs : Jennifer S. Rota [États-Unis] ; Kimberly B. Hummel [États-Unis] ; Paul A. Rota [États-Unis] ; William J. Bellini [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1992.
English descriptors
- Teeft :
- Academic press, Acute infections, Additional base change, Amino, Amino acid, Amino acid changes, Amino acid sequence, Amino acid substitutions, Base changes, Base substitutions, Canine distemper virus, Cell lysates, Coding, Coding changes, Coding region, Coding regions, Coding sequence, Disease control, Edmonston, Edmonston strain, Fusion gene sequence, Gene, Gene sequence, Genetic changes, Genetic relationships, Genetic variation, Glycoprotein, Glycoprotein genes, Glycosylation, Hemagglutinin, Hemagglutinin gene sequence, Immunologic pressure, Initial infection, Measles, Measles cases, Measles virus, Measles viruses, Monoclonal antibodies, Moraten, Moraten sequence, Moraten vaccine strain, Mrna, Nucleotide, Nucleotide changes, Nucleotide positions, Nucleotide sequence, Other morbilliviruses, Other paramyxoviruses, Parental edmonston strain, Peptide, Persistent cases, Persistent measles strains, Persistent strains, Potential glycosylation site, Potential glycosylation sites, Putative signal peptide, Raven press, Rinderpest virus, Selective pressure, Separate lineage, Sequence analysis, Sequencing, Sequencing reactions, Vaccine, Vaccine strain, Vaccine strain moraten, Viral, Virology, Virus, Wild type, Wild types.
Abstract
Abstract: The glycoprotein coding sequences from three wild-type measles viruses isolated in the United States during 1988–1989 were examined by mRNA templated sequencing to determine whether contemporary strains have undergone genetic changes relative to the vaccine strain, Moraten. These studies revealed variation in the hemagglutinin (HA) gene and, to a far lesser degree, the fusion (F) gene. The F protein coding region was highly conserved with only three predicted amino acid changes. Among the predicted amino acid changes identified in the HA was a new potential glycosylation site at residue 416, located toward the carboxy-terminal end of the HA peptide. Eighty percent of the predicted amino acid changes in the HA shared by the three wild-type isolates were clustered near the five previously identified potential glycosylation sites. A linear pattern of evolutionary change was observed after comparing the predicted amino acid HA changes from the 1988–1989 viruses to those predicted in the HA protein from U.S. wild types isolated in 1977 and 1983.
Url:
DOI: 10.1016/0042-6822(92)90742-8
Affiliations:
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Rota</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral and Rickettsial Diseases, National Center for Infectious Diseases, Centers for Disease Control, Atlanta, Georgia 30333</wicri:regionArea><wicri:noRegion>Georgia 30333</wicri:noRegion></affiliation></author><author><name sortKey="Hummel, Kimberly B" sort="Hummel, Kimberly B" uniqKey="Hummel K" first="Kimberly B." last="Hummel">Kimberly B. Hummel</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral and Rickettsial Diseases, National Center for Infectious Diseases, Centers for Disease Control, Atlanta, Georgia 30333</wicri:regionArea><wicri:noRegion>Georgia 30333</wicri:noRegion></affiliation></author><author><name sortKey="Rota, Paul A" sort="Rota, Paul A" uniqKey="Rota P" first="Paul A." last="Rota">Paul A. 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Bellini</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral and Rickettsial Diseases, National Center for Infectious Diseases, Centers for Disease Control, Atlanta, Georgia 30333</wicri:regionArea><wicri:noRegion>Georgia 30333</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="1992">1992</date><biblScope unit="volume">188</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="135">135</biblScope><biblScope unit="page" to="142">142</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>Academic press</term><term>Acute infections</term><term>Additional base change</term><term>Amino</term><term>Amino acid</term><term>Amino acid changes</term><term>Amino acid sequence</term><term>Amino acid substitutions</term><term>Base changes</term><term>Base substitutions</term><term>Canine distemper virus</term><term>Cell lysates</term><term>Coding</term><term>Coding changes</term><term>Coding region</term><term>Coding regions</term><term>Coding sequence</term><term>Disease control</term><term>Edmonston</term><term>Edmonston strain</term><term>Fusion gene sequence</term><term>Gene</term><term>Gene sequence</term><term>Genetic changes</term><term>Genetic relationships</term><term>Genetic variation</term><term>Glycoprotein</term><term>Glycoprotein genes</term><term>Glycosylation</term><term>Hemagglutinin</term><term>Hemagglutinin gene sequence</term><term>Immunologic pressure</term><term>Initial infection</term><term>Measles</term><term>Measles cases</term><term>Measles virus</term><term>Measles viruses</term><term>Monoclonal antibodies</term><term>Moraten</term><term>Moraten sequence</term><term>Moraten vaccine strain</term><term>Mrna</term><term>Nucleotide</term><term>Nucleotide changes</term><term>Nucleotide positions</term><term>Nucleotide sequence</term><term>Other morbilliviruses</term><term>Other paramyxoviruses</term><term>Parental edmonston strain</term><term>Peptide</term><term>Persistent cases</term><term>Persistent measles strains</term><term>Persistent strains</term><term>Potential glycosylation site</term><term>Potential glycosylation sites</term><term>Putative signal peptide</term><term>Raven press</term><term>Rinderpest virus</term><term>Selective pressure</term><term>Separate lineage</term><term>Sequence analysis</term><term>Sequencing</term><term>Sequencing reactions</term><term>Vaccine</term><term>Vaccine strain</term><term>Vaccine strain moraten</term><term>Viral</term><term>Virology</term><term>Virus</term><term>Wild type</term><term>Wild types</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The glycoprotein coding sequences from three wild-type measles viruses isolated in the United States during 1988–1989 were examined by mRNA templated sequencing to determine whether contemporary strains have undergone genetic changes relative to the vaccine strain, Moraten. These studies revealed variation in the hemagglutinin (HA) gene and, to a far lesser degree, the fusion (F) gene. The F protein coding region was highly conserved with only three predicted amino acid changes. Among the predicted amino acid changes identified in the HA was a new potential glycosylation site at residue 416, located toward the carboxy-terminal end of the HA peptide. Eighty percent of the predicted amino acid changes in the HA shared by the three wild-type isolates were clustered near the five previously identified potential glycosylation sites. A linear pattern of evolutionary change was observed after comparing the predicted amino acid HA changes from the 1988–1989 viruses to those predicted in the HA protein from U.S. wild types isolated in 1977 and 1983.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Rota, Jennifer S" sort="Rota, Jennifer S" uniqKey="Rota J" first="Jennifer S." last="Rota">Jennifer S. Rota</name></noRegion><name sortKey="Bellini, William J" sort="Bellini, William J" uniqKey="Bellini W" first="William J." last="Bellini">William J. Bellini</name><name sortKey="Hummel, Kimberly B" sort="Hummel, Kimberly B" uniqKey="Hummel K" first="Kimberly B." last="Hummel">Kimberly B. Hummel</name><name sortKey="Rota, Paul A" sort="Rota, Paul A" uniqKey="Rota P" first="Paul A." last="Rota">Paul A. Rota</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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