Role of the alfalfa mosaic virus movement protein and coat protein in virus transport.
Mol Plant Microbe Interact
; 14(9): 1051-62, 2001 Sep.
Article
de En
| MEDLINE
| ID: mdl-11551070
ABSTRACT
The movement protein (MP) and coat protein (CP) encoded by Alfalfa mosaic virus (AMV) RNA 3 are both required for virus transport. RNA 3 vectors that expressed nonfused green fluorescent protein (GFP), MPGPF fusions, or GFPCP fusions were used to study the functioning of mutant MP and CP in protoplasts and plants. C-terminal deletions of up to 21 amino acids did not interfere with the function of the CP in cell-to-cell movement, although some of these mutations interfered with virion assembly. Deletion of the N-terminal 11 or C-terminal 45 amino acids did not interfere with the ability of MP to assemble into tubular structures on the protoplast surface. Additionally, N- or C-terminal deletions disrupted tubule formation. A GFPCP fusion was targeted specifically into tubules consisting of a wild-type MP. All MP deletion mutants that showed cell-to-cell and systemic movement in plants were able to form tubular structures on the surface of protoplasts. Brome mosaic virus (BMV) MP did not support AMV transport. When the C-terminal 48 amino acids were replaced by the C-terminal 44 amino acids of the AMV MP, however, the BMV/AMV chimeric protein permitted wild-type levels of AMV transport. Apparently, the C terminus of the AMV MP, although dispensable for cell-to-cell movement, confers specificity to the transport process.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Protéines virales
/
Capside
/
Virus de la mosaïque de la luzerne
/
Protéines de capside
Langue:
En
Journal:
Mol Plant Microbe Interact
Sujet du journal:
BIOLOGIA MOLECULAR
/
BOTANICA
/
MICROBIOLOGIA
Année:
2001
Type de document:
Article
Pays d'affiliation:
Pays-Bas