The role of the C-terminal region of olive latent virus 1 coat protein in host systemic infection.
Arch Virol
; 151(10): 1973-83, 2006 Oct.
Article
en En
| MEDLINE
| ID: mdl-16699830
A full-length cDNA clone of olive latent virus 1 (OLV-1), a member of the genus Necrovirus, family Tombusviridae, was subjected to site-directed mutagenesis, and coat protein gene mutants were constructed. A mutant clone, denoted Delta3297, was obtained by deleting the nucleotide in position 3297, thus inducing a frameshift and replacing the last 49 amino acids of the viral coat protein (CP) by a shorter sequence of 39 amino acids. This mutant was viable, stable, able to synthesize a smaller CP, and able to give rise to the formation of apparently intact virus particles. Cell-to-cell movement of Delta3297 in Nicotiana benthamiana leaves was not affected, but, contrary to wild type OLV-1, it failed to spread systemically. These results indicate that virion formation is necessary but not sufficient for long-distance movement for OLV-1 and highlights the role of the CP carboxy-terminal domain in systemic infection.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Enfermedades de las Plantas
/
Infecciones por Virus ARN
/
Tombusviridae
/
Proteínas de la Cápside
Idioma:
En
Revista:
Arch Virol
Año:
2006
Tipo del documento:
Article
País de afiliación:
Italia
Pais de publicación:
Austria