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

The role of the C-terminal region of olive latent virus 1 coat protein in host systemic infection 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 Δ3297, 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 Δ3297 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

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

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Publisher
Springer-Verlag
Copyright
Copyright © 2006 by Springer-Verlag
Subject
Biomedicine; Medical Microbiology; Virology; Infectious Diseases
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-006-0767-2
Publisher site
See Article on Publisher Site

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 Δ3297, 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 Δ3297 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

Archives of VirologySpringer Journals

Published: Oct 1, 2006

References

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