| Literature DB >> 11907339 |
Jan E Carette1, Jan Verver1, Joost Martens1, Tony van Kampen1, Joan Wellink1, Ab van Kammen1.
Abstract
Cowpea mosaic virus (CPMV) replication occurs in close association with small membranous vesicles in the host cell. The CPMV RNA1-encoded 60 kDa nucleotide-binding protein ('60K') plays a role in the formation of these vesicles. In this study, five cellular proteins were identified that interacted with different domains of 60K using a yeast two-hybrid search of an Arabidopsis cDNA library. Two of these host proteins (termed VAP27-1 and VAP27-2), with high homology to the VAP33 family of SNARE-like proteins from animals, interacted specifically with the C-terminal domain of 60K and upon transient expression colocalized with 60K in CPMV-infected cowpea protoplasts. eEF1-beta, picked up using the central domain of 60K, was also found to colocalize with 60K. The possible role of these host proteins in the viral replicative cycle is discussed.Entities:
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Year: 2002 PMID： 11907339 DOI： 10.1099/0022-1317-83-4-885
Source DB: PubMed Journal: J Gen Virol ISSN： 0022-1317 Impact factor: 3.891