http://www.cnr.it/ontology/cnr/individuo/prodotto/ID173506
The role of the C-terminal region of Olive latent virus 1 coat protein in host systemic infection (Articolo in rivista)
- Type
- Label
- The role of the C-terminal region of Olive latent virus 1 coat protein in host systemic infection (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s00705-006-0767-2 (literal)
- Alternative label
Pantaleo, V., Grieco, F., Di Franco, A., Martelli, G.P. (2006)
The role of the C-terminal region of Olive latent virus 1 coat protein in host systemic infection
in Archives of virology; Springer Wien, Wien (Austria)
(literal)
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- Pantaleo, V., Grieco, F., Di Franco, A., Martelli, G.P. (literal)
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- http://www.springerlink.com/content/b87520t22063p216/ (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- PV, GF: Istituto di Virologia Vegetale del CNR, Sezione di Bari. DFA, MGP: Dipartimento di Protezione delle Piante e Microbiologia Applicata, Università degli Studi, Bari, Italy (literal)
- Titolo
- The role of the C-terminal region of Olive latent virus 1 coat protein in host systemic infection (literal)
- 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 3297, 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 3297 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. (literal)
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