@article{tremblay_vaewhongs_turner_sit_lommel_2005, title={Cell wall localization of Red clover necrotic mosaic virus movement protein is required for cell-to-cell movement}, volume={333}, ISSN={["0042-6822"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-13644249879&partnerID=MN8TOARS}, DOI={10.1016/j.virol.2004.12.019}, abstractNote={The Red clover necrotic mosaic virus movement protein (MP) is essential for cell-to-cell movement. Eight previously characterized alanine-scanning mutants of the MP were fused to the green fluorescent protein (GFP) and expressed from viral infectious transcripts. Inoculated plants were assayed for movement and intracellular accumulation of MP by confocal laser-scanning microscopy. A strict correlation was observed between the targeting to the cell wall (presumably the plasmodesmata) and cell-to-cell movement. Complementation of dysfunctional MP mutants with either wild-type MP or other null mutants in some cases rescued intracellular targeting and movement. The data suggest the presence of distinct domains in the MP for virus movement (near residues 27–31), complementarity (near residues 122 and 128), and intracellular localization (near residue 161). These data support a model of MP interacting cooperatively with itself to bind viral RNA, localize to and modify plasmodesmata and effect virus movement.}, number={1}, journal={VIROLOGY}, publisher={Elsevier BV}, author={Tremblay, D and Vaewhongs, AA and Turner, KA and Sit, TL and Lommel, SA}, year={2005}, month={Mar}, pages={10–21} }
 @article{turner_sit_callaway_allen_lommel_2004, title={Red clover necrotic mosaic virus replication proteins accumulate at the endoplasmic reticulum}, volume={320}, ISSN={["0042-6822"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-1542285421&partnerID=MN8TOARS}, DOI={10.1016/j.virol.2003.12.006}, abstractNote={Red clover necrotic mosaic virus (RCNMV) encodes N-terminally overlapping proteins of 27 and 88 kDa (p27 and p88) known to be required for replication. Green fluorescent protein (GFP) fusions were used to visualize the location of p27 and p88 within Nicotiana benthamiana cells. GFP:p27 fusions localized to the endoplasmic reticulum (ER), co-localized with ER-targeted yellow fluorescent protein and caused membrane restructuring and proliferation. Cellular fractionation of virus-inoculated N. benthamiana leaves confirmed the association of p27 with ER membranes. GFP:p88 fusions also localized to the ER and co-localized with GFP:p27. Both fusion proteins co-localize to the cortical and cytoplasmic ER and were associated with invaginations of the nuclear envelope. Independent accumulation in, and perturbation of, the ER suggests that p27 and p88 function together in the replication complex. This is the first report of a member of the Tombusviridae replicating in association with the ER.}, number={2}, journal={VIROLOGY}, publisher={Elsevier BV}, author={Turner, KA and Sit, TL and Callaway, AS and Allen, NS and Lommel, SA}, year={2004}, month={Mar}, pages={276–290} }