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Central domain of a potyvirus VPg is involved in the interaction with the host translation initiation factor eIF4E and the viral protein HcPro

E. Redondo

IPV, UMR GDPP INRA-Bordeaux 2, IBVM, BP 81, F-33883 Villenave d’Ornon Cedex, France

Correspondence
Olivier Le Gall
olegall{at}bordeaux.inra.fr

Using recombinant proteins produced in bacteria or in infected plants, interactions between the VPg and HcPro of Lettuce mosaic potyvirus (LMV) and between LMV VPg and the lettuce translation initiation factor 4E, the cap-binding protein (eIF4E), were demonstrated in vitro. Interaction with eIF4E and HcPro both involved the same VPg central domain. The structure of this domain in the VPg context was predicted to include an amphiphilic -helix, with the amino acids related to biological functions in various potyviruses exposed at the hydrophilic side.

Present address: BIOGEMMA, 24 avenue des Landais, F-63170 Aubière, France.

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