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Journal of General Virology, Vol 80, 1347-1356, Copyright © 1999 by Society for General Microbiology

ARTICLES

The nine C-terminal residues of the grapevine fanleaf nepovirus movement protein are critical for systemic virus spread

C Belin, C Schmitt, F Gaire, B Walter, G Demangeat and L Pinck
INRA, Unite de Recherches Vigne et Vin, Laboratoire de Pathologie Vigne, 28 rue de Herrlisheim, 68021 Colmar cedex, France

The grapevine fanleaf virus (GFLV) RNA2-encoded polyprotein P2 is proteolytically cleaved by the RNA1-encoded proteinase to yield protein 2A, 2B(MP) movement protein and 2C(CP) coat protein. To further investigate the role of the 2B(MP) and 2C(CP) proteins in virus movement, RNA2 was engineered related Arabis mosaic virus (ArMV). Transcripts of all chimeric RNA2s were able to replicate in Chenopodium quinoa protoplasts and form tubules in tobacco BY-2 protoplasts in the presence of the infectious transcript of GFLV RNA1. Virus particles were produced when the GFLV 2C(CP) gene In addition, chimeric RNA2 containing the complete ArMV 2B(MP) gene was neither encapsidated nor infectious on plants, probably because polyprotein P2 was incompletely processed. However, chimeric RNA2 encoding ArMV 2B(MP), in which the nine C-terminal residues were those of GFLV 2B(MP), formed virus particles and were infectious in the presence of GFLV but not ArMV 2C(CP). These results suggest that the nine C-terminal residues of 2B(MP) must be of the same virus origin as the proteinase for efficient proteolytic processing of polyprotein P2 and from the same virus origin as the 2C(CP) for systemic virus spread.


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Copyright © 1999 by the Society for General Microbiology.