The movement protein (MP) of necrotic ringspot virus (PNRSV) is required for viral transport. Previous analysis with MPs of other members of the family has shown that the C-terminal part of these MPs plays a critical role in the interaction with the cognate coat protein (CP) and in cell-to-cell transport. Bimolecular fluorescence complementation and overlay analysis confirm an interaction between the C-terminal 38 aa of PNRSV MP and its cognate CP. Mutational analysis of the C-terminal region of the PNRSV MP revealed that its C-terminal 38 aa are dispensable for virus transport, however, the 4 aa preceding the dispensable C terminus are necessary to target the MP to the plasmodesmata and for the functionality of the protein. The capacity of the PNRSV MP to use either a CP-dependent or a CP-independent cell-to-cell transport is discussed.


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vol. , part 7, pp. 1865 - 1870

Average size of twenty infection foci of chimeric AMV RNA 3 [PDF](44 KB)

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