Temperature-sensitive mutants of influenza virus
Identifieur interne : 000200 ( 1968/Analysis ); précédent : 000199; suivant : 000201Temperature-sensitive mutants of influenza virus
Auteurs : Brian R. Murphy [États-Unis] ; Susan B. Spring [États-Unis] ; Douglas D. Richman [États-Unis] ; Eveline L. Tierney [États-Unis] ; Julius Kasel [États-Unis] ; Robert M. Chanock [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1975.
English descriptors
- Teeft :
- Allantoic cavity, Chanock, Clone, Complementation, Complementation group, Complementation groups, Genetic, Genetic interaction, Genetic stability, Genome, Glycoprotein, Greater reduction, Hemagglutinin, Hemagglutinin glycoproteins, High titer, Hong virus, Honl, Honl virus, Influenza, Influenza virus, Lesion, Monolayer cultures, Mutant, Neuraminidase, Neuraminidase gene, Neuraminidase glycoprotein, Neuraminidase glycoproteins, Neuraminidase subtype, Pairwise matings, Parent virus, Plaque, Plaque formation, Poisson distribution, Present study, Recombinant, Recombinant clones, Recombinant viruses, Recombination, Same complementation group, Shutoff, Shutoff temperature, Surface antigens, Tissue culture, Vaccine, Virus, Virus genome, Virus titer, Virus vaccine.
Abstract
Abstract: The nature of the genetic defect(s) present in the influenza A/Hong Kong/1968-ts-1[E] (H3N2) candidate vaccine virus, was analyzed by transferring them by genetic recombination to a 1943 HON1 wild-type virus. Three classes of ts viruses bearing the HO hemagglutinin were identified. One class consisted of two clones of virus, R1 and R8, which underwent complementation-recombination with each other but not with the Hong Kong/1968 (H3N2)-ts-1[E] parent virus. The second class consisted of clones of virus, such as R4 and R11, that failed to undergo complementation-recombination with R1, with R8, or with the ts-1[E] parent. These data indicated that the parent Hong Kong ts-1[E] virus possessed two ts lesions that segregated independently of each other and were presumably on different segments of the influenza A virus genome. The third class of ts mutants consisted of a spontaneously occurring ts mutant, clone R9; this clone underwent complementation-recombination with the ts-1[E] parent and other HO-ts recombinants and was shown to belong to a complementation group different than clones R1 and R8. The ts defects present in the Hong Kong-ts-1[E] donor virus segregated independently of the genes that coded for the epidemiologically important surface antigens, i.e., the hemagglutinin and the neuraminidase glycoproteins. The implications of these findings for the development of a live attenuated influenza virus vaccine are discussed.
Url:
DOI: 10.1016/0042-6822(75)90225-1
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 000405
- to stream Istex, to step Curation: 000405
- to stream Istex, to step Checkpoint: 001731
- to stream Main, to step Merge: 002D41
- to stream Main, to step Curation: 002B69
- to stream Main, to step Exploration: 002B69
- to stream 1968, to step Extraction: 000200
Links to Exploration step
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<term>Complementation</term>
<term>Complementation group</term>
<term>Complementation groups</term>
<term>Genetic</term>
<term>Genetic interaction</term>
<term>Genetic stability</term>
<term>Genome</term>
<term>Glycoprotein</term>
<term>Greater reduction</term>
<term>Hemagglutinin</term>
<term>Hemagglutinin glycoproteins</term>
<term>High titer</term>
<term>Hong virus</term>
<term>Honl</term>
<term>Honl virus</term>
<term>Influenza</term>
<term>Influenza virus</term>
<term>Lesion</term>
<term>Monolayer cultures</term>
<term>Mutant</term>
<term>Neuraminidase</term>
<term>Neuraminidase gene</term>
<term>Neuraminidase glycoprotein</term>
<term>Neuraminidase glycoproteins</term>
<term>Neuraminidase subtype</term>
<term>Pairwise matings</term>
<term>Parent virus</term>
<term>Plaque</term>
<term>Plaque formation</term>
<term>Poisson distribution</term>
<term>Present study</term>
<term>Recombinant</term>
<term>Recombinant clones</term>
<term>Recombinant viruses</term>
<term>Recombination</term>
<term>Same complementation group</term>
<term>Shutoff</term>
<term>Shutoff temperature</term>
<term>Surface antigens</term>
<term>Tissue culture</term>
<term>Vaccine</term>
<term>Virus</term>
<term>Virus genome</term>
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<front><div type="abstract" xml:lang="en">Abstract: The nature of the genetic defect(s) present in the influenza A/Hong Kong/1968-ts-1[E] (H3N2) candidate vaccine virus, was analyzed by transferring them by genetic recombination to a 1943 HON1 wild-type virus. Three classes of ts viruses bearing the HO hemagglutinin were identified. One class consisted of two clones of virus, R1 and R8, which underwent complementation-recombination with each other but not with the Hong Kong/1968 (H3N2)-ts-1[E] parent virus. The second class consisted of clones of virus, such as R4 and R11, that failed to undergo complementation-recombination with R1, with R8, or with the ts-1[E] parent. These data indicated that the parent Hong Kong ts-1[E] virus possessed two ts lesions that segregated independently of each other and were presumably on different segments of the influenza A virus genome. The third class of ts mutants consisted of a spontaneously occurring ts mutant, clone R9; this clone underwent complementation-recombination with the ts-1[E] parent and other HO-ts recombinants and was shown to belong to a complementation group different than clones R1 and R8. The ts defects present in the Hong Kong-ts-1[E] donor virus segregated independently of the genes that coded for the epidemiologically important surface antigens, i.e., the hemagglutinin and the neuraminidase glycoproteins. The implications of these findings for the development of a live attenuated influenza virus vaccine are discussed.</div>
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<affiliations><list><country><li>États-Unis</li>
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<name sortKey="Chanock, Robert M" sort="Chanock, Robert M" uniqKey="Chanock R" first="Robert M" last="Chanock">Robert M. Chanock</name>
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<name sortKey="Tierney, Eveline L" sort="Tierney, Eveline L" uniqKey="Tierney E" first="Eveline L" last="Tierney">Eveline L. Tierney</name>
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