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Contribution of topology determinants of a viral movement protein to its membrane association, intracellular traffic and viral cell-to-cell movement

AuthorsGenovés, Ainhoa ; Pallás Benet, Vicente ; Navarro-Bohigues, J. A.
KeywordsSpot-virus MNSV
Water Interface Region
Alfalfa mosaic-virus
Issue DateAug-2011
PublisherAmerican Society for Microbiology
CitationJournal of Virology 85/15:7797-7809 (2011)
AbstractThe p7B movement protein (MP) of Melon necrotic spot virus (MNSV) is a single-pass membrane protein associated with the endoplasmic reticulum (ER), the Golgi apparatus (GA)and plasmodesmata (Pd). Experimental data presented here revealed that the p7B transmembrane domain (TMD) was sufficient to target the green fluorescent protein (GFP) to ER membranes. In addition, the short extramembrane regions of p7B were essential for subsequent ER export and transport to GA and Pd. Microsomal partitioning and bimolecular fluorescence assays supported a type II topology of p7B in planta. Mutations affecting conventional determinants of p7B membrane topology such as TMD secondary structure, overall hydrophobicity profile, the so-called “aromatic belt” and the net charge distribution on either side of the TMD were engineered into infectious RNAs to investigate the relationship between the MP structure and MNSV cell-to-cell movement. Results revealed that: i) the overall hydrophobic profile and the α-helix integrity of the TMD were relevant for virus movement; ii) modification of the net charge balance of the regions flanking both TMD sides drastically reduced cell-to-cell movement; iii) localization of p7B to GA was necessary but not sufficient for virus movement and iv) membrane insertion was essential for p7B function in virus movement. Our results therefore indicate that MNSV cell-to-cell movement requires a sequential transport of p7B from the ER via the GA to Pd, which is modulated by a combination of several signals with different strengths in the extramembrane regions and TMD of the MP.
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