H2N2V1, Main, Exploration, bibRecord, 002C31

Comparative Studies of Wild-Type and “Cold-Mutant” (Temperature-Sensitive) Influenza Viruses: Polypeptide Synthesis by an Asian (H2N2) Strain and Its Cold-Adapted Variant

Identifieur interne : 002C31 ( Main/Exploration ); précédent : 002C30; suivant : 002C32

Comparative Studies of Wild-Type and “Cold-Mutant” (Temperature-Sensitive) Influenza Viruses: Polypeptide Synthesis by an Asian (H2N2) Strain and Its Cold-Adapted Variant

Auteurs : Alan P. Kendal ; Michael P. Kiley ; H. F. Maassab

Source :

Journal of Virology [ 0022-538X ] ; 1973.

RBID : PMC:356793

Descripteurs français

KwdFr :
- Adaptation biologique, Animaux, Basse température, Biosynthèse des peptides, Embryon de poulet, Hémagglutinines virales, Mutation, Orthomyxoviridae (croissance et développement), Orthomyxoviridae (enzymologie), Orthomyxoviridae (immunologie), Orthomyxoviridae (métabolisme), Poulets, Protéines virales (biosynthèse), Radio-isotopes du carbone, Rein, Réplication virale, Sialidase (biosynthèse), Techniques de culture, Tests d'inhibition de l'hémagglutination, Tritium, Variation génétique, Électrophorèse sur gel de polyacrylamide.
MESH :
- biosynthèse : Protéines virales, Sialidase.
- croissance et développement : Orthomyxoviridae.
- enzymologie : Orthomyxoviridae.
- immunologie : Orthomyxoviridae.
- métabolisme : Orthomyxoviridae.
- Adaptation biologique, Animaux, Basse température, Biosynthèse des peptides, Embryon de poulet, Hémagglutinines virales, Mutation, Poulets, Radio-isotopes du carbone, Rein, Réplication virale, Techniques de culture, Tests d'inhibition de l'hémagglutination, Tritium, Variation génétique, Électrophorèse sur gel de polyacrylamide.

English descriptors

KwdEn :
- Adaptation, Biological, Animals, Carbon Radioisotopes, Chick Embryo, Chickens, Cold Temperature, Culture Techniques, Electrophoresis, Polyacrylamide Gel, Genetic Variation, Hemagglutination Inhibition Tests, Hemagglutinins, Viral, Kidney, Mutation, Neuraminidase (biosynthesis), Orthomyxoviridae (enzymology), Orthomyxoviridae (growth & development), Orthomyxoviridae (immunology), Orthomyxoviridae (metabolism), Peptide Biosynthesis, Tritium, Viral Proteins (biosynthesis), Virus Replication.
MESH :
- chemical , biosynthesis : Neuraminidase, Viral Proteins.
- chemical : Carbon Radioisotopes, Hemagglutinins, Viral, Tritium.
- enzymology : Orthomyxoviridae.
- growth & development : Orthomyxoviridae.
- immunology : Orthomyxoviridae.
- metabolism : Orthomyxoviridae.
- Adaptation, Biological, Animals, Chick Embryo, Chickens, Cold Temperature, Culture Techniques, Electrophoresis, Polyacrylamide Gel, Genetic Variation, Hemagglutination Inhibition Tests, Kidney, Mutation, Peptide Biosynthesis, Virus Replication.

Abstract

The structure and replication of a cold-adapted, temperature-sensitive (TS) mutant of an Asian (H2N2) influenza virus was compared with that of its wild-type (WT) parent. Viruses were grown in a chicken kidney cell system, and at the nonpermissive temperature of 40 C, production of infectious TS virus was about 100,000-fold less than at 35 C, in contrast to WT virus. Major structural polypeptides of each virus grown at 35 C were similar, except that the hemagglutinin glycopolypeptide (HA) of the TS virions was slightly more heterogenous than that of WT virions. Synthesis of viral polypeptides was examined by sodium dodecyl sulfate acrylamide gel electrophoresis of pulse-labeled infected cells. This revealed a defect in the synthesis of TS viral hemagglutinin that was most pronounced at the nonpermissive temperature. Other TS viral polypeptides appeared to be synthesized normally at 40 C. A defect in the TS virus hemagglutinin was also indicated by serological studies that demonstrated that TS virus hemagglutinin had lost antigenic sites present on the WT virus. Thus, it is concluded that the virus mutant examined contains lesions in the hemagglutinin gene, although the possibility of additional unrecognized lesions is not excluded.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC356793

PubMed: 4796900
PubMed Central: 356793

Affiliations:

Le document en format XML

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<term>Cold Temperature</term>
<term>Culture Techniques</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Genetic Variation</term>
<term>Hemagglutination Inhibition Tests</term>
<term>Hemagglutinins, Viral</term>
<term>Kidney</term>
<term>Mutation</term>
<term>Neuraminidase (biosynthesis)</term>
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<term>Embryon de poulet</term>
<term>Hémagglutinines virales</term>
<term>Mutation</term>
<term>Orthomyxoviridae (croissance et développement)</term>
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<front><div type="abstract" xml:lang="en"><p>The structure and replication of a cold-adapted, temperature-sensitive (TS) mutant of an Asian (H2N2) influenza virus was compared with that of its wild-type (WT) parent. Viruses were grown in a chicken kidney cell system, and at the nonpermissive temperature of 40 C, production of infectious TS virus was about 100,000-fold less than at 35 C, in contrast to WT virus. Major structural polypeptides of each virus grown at 35 C were similar, except that the hemagglutinin glycopolypeptide (HA) of the TS virions was slightly more heterogenous than that of WT virions. Synthesis of viral polypeptides was examined by sodium dodecyl sulfate acrylamide gel electrophoresis of pulse-labeled infected cells. This revealed a defect in the synthesis of TS viral hemagglutinin that was most pronounced at the nonpermissive temperature. Other TS viral polypeptides appeared to be synthesized normally at 40 C. A defect in the TS virus hemagglutinin was also indicated by serological studies that demonstrated that TS virus hemagglutinin had lost antigenic sites present on the WT virus. Thus, it is concluded that the virus mutant examined contains lesions in the hemagglutinin gene, although the possibility of additional unrecognized lesions is not excluded.</p>
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Comparative Studies of Wild-Type and “Cold-Mutant” (Temperature-Sensitive) Influenza Viruses: Polypeptide Synthesis by an Asian (H2N2) Strain and Its Cold-Adapted Variant

Comparative Studies of Wild-Type and “Cold-Mutant” (Temperature-Sensitive) Influenza Viruses: Polypeptide Synthesis by an Asian (H2N2) Strain and Its Cold-Adapted Variant

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

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Pour générer des pages wiki

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