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 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.
Pantaleo
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V
Istituto di Virologia Vegetale del CNR, Sezione di Bari and Dipartimento di Protezione delle Piante e Microbiologia Applicata, Università degli Studi, Bari, Italy. v.pantaleo@ba.ivv.cnr.it
Grieco
F
F
Di Franco
A
A
Martelli
G P
GP
D000595:Amino Acid Sequence; D036022:Capsid Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D016368:Frameshift Mutation; D008124:Locomotion; D008969:Molecular Sequence Data; D010935:Plant Diseases / Q000821:virology*; D017354:Point Mutation; D017434:Protein Structure, Tertiary / Q000502:physiology; D012327:RNA Virus Infections / Q000821:virology*; D014026:Nicotiana; D019183:Tombusviridae / Q000737:chemistry* / Q000472:pathogenicity / Q000502:physiology; D014774:Virulence
D036022:Capsid Proteins