The role of the C-terminal region of olive latent virus 1 coat protein in host systemic infection.

Abstract:

: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.

journal_name

Arch Virol

journal_title

Archives of virology

authors

Pantaleo V,Grieco F,Di Franco A,Martelli GP

doi

10.1007/s00705-006-0767-2

subject

Has Abstract

pub_date

2006-10-01 00:00:00

pages

1973-83

issue

10

eissn

0304-8608

issn

1432-8798

journal_volume

151

pub_type

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