Journal
JOURNAL OF VIROLOGY
Volume 83, Issue 11, Pages 5535-5543Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00393-09
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Funding
- Spanish MEC [BMC2006-08542, BIO2005-07331, BIO2006-03130, CSD2007-00010]
- Generalitat Valenciana [GV04B-183]
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The cell-to-cell transport of plant viruses depends on one or more virus-encoded movement proteins (MPs). Some MPs are integral membrane proteins that interact with the membrane of the endoplasmic reticulum, but a detailed understanding of the interaction between MPs and biological membranes has been lacking. The cell-to-cell movement of the Prunus necrotic ringspot virus (PNRSV) is facilitated by a single MP of the 30K superfamily. Here, using a myriad of biochemical and biophysical approaches, we show that the PNRSV MP contains only one hydrophobic region (HR) that interacts with the membrane interface, as opposed to being a transmembrane protein. We also show that a proline residue located in the middle of the HR constrains the structural conformation of this region at the membrane interface, and its replacement precludes virus movement.
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