Journal
JOURNAL OF GENERAL VIROLOGY
Volume 94, Issue -, Pages 2117-2128Publisher
MICROBIOLOGY SOC
DOI: 10.1099/vir.0.053256-0
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Funding
- Scottish Government Rural and Environment Science and Analytical Services (RESAS)
- Wellcome Trust [090005]
- ZAAS
- Program for Zhejiang Leading Team of Science and Technology Innovation [2011R09032-10]
- Program for Leading Team of Agricultural Research and Innovation of Ministry of Agriculture, China
- Modern Agricultural Biotechnology and Crop Disease Control from Key Subject Construction Program of Zhejiang Province, China
- Project of Molecular Mechanism of Plant Defence to Pests and Diseases from the Ministry of Science and Technology, China [2012CB722504]
- State Basic Research Program of China [2012CB722504, 2010CB126203]
- International Science & Technology Cooperation Program of China [2012DFA30900]
- China Agriculture Research System from the Ministry of Agriculture of the People's Republic of China [CARS-3-1]
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Emaravirus is a recently described genus of negative-strand RNA plant viruses. Emaravirus P4 protein localized to plasmodesmata, suggesting that it could be a viral movement protein (MP). In the current study, we showed that the P4 protein of raspberry leaf blotch emaravirus (RLBV) rescued the cell-to-cell movement of a defective potato virus X (PVX) that had a deletion mutation in the triple gene block 1 movement-associated protein. This demonstrated that RLBV P4 is a functional MP. Sequence analyses revealed that P4 is a distant member of the 30K superfamily of MPs. All MPs of this family contain two highly conserved regions predicted to form beta-strands, namely beta 1 and beta 2. We explored by alanine mutagenesis the role of two residues of P4 (Ile106 and Asp127) located in each of these strands. We also made the equivalent substitutions in the 29K MP of tobacco rattle virus, another member of the 30K superfamily. All substitutions abolished the ability to complement PVX movement, except for the l106A substitution in the beta 1 region of P4. This region has been shown to mediate membrane association of 30K MPs; our results show that it is possible to make non-conservative substitutions of a well-conserved aliphatic residue within beta 1 without preventing the membrane association or movement function of P4.
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