Replacement of the tyrosine residue that links a potyviral VPg to the viral RNA is lethal.
Virology
; 220(2): 535-8, 1996 Jun 15.
Article
em En
| MEDLINE
| ID: mdl-8661407
ABSTRACT
Mutants of tobacco vein mottling virus (TVMV) were constructed in which the tyrosine residue (Tyr1860) that links the VPg to the viral RNA was changed to phenylalanine or serine or was inverted in position with the adjacent glycine residue. In another mutant, the tyrosine residue nearest to Tyr1860 (Tyr1867) was changed to a phenylalanine residue. The resulting mutants were tested for their ability to infect Nicotiana tabacum plants or protoplasts. The Tyr1860 mutants did not accumulate to detectable levels in infected plants when tested by ELISA and Northern blot analysis. Moreover, the Tyr1860-associated mutants were not infectious in protoplasts, indicating that mutations involving the linking amino acid of the TVMV VPg abolished viral replication. In contrast to the Tyr1860 mutants, transcripts from the mutation of Tyr1867 to a phenylalanine residue infected both protoplasts and plants. Analysis of progeny RNA from plants inoculated with the Tyr1867 mutant indicated that a reversion to wild type had occurred in systemically infected leaves.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Tirosina
/
RNA Viral
/
Proteínas do Core Viral
/
Potyvirus
Idioma:
En
Revista:
Virology
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Estados Unidos