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Journal of Virology, August 2008, p. 7601-7612, Vol. 82, No. 15
0022-538X/08/$08.00+0     doi:10.1128/JVI.00209-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Mutational Analysis of Plant Cap-Binding Protein eIF4E Reveals Key Amino Acids Involved in Biochemical Functions and Potyvirus Infection{triangledown}

Sylvie German-Retana,1* Jocelyne Walter,1 Bénédicte Doublet,1 Geneviève Roudet-Tavert,1 Valérie Nicaise,3 Cécile Lecampion,2 Marie-Christine Houvenaghel,1 Christophe Robaglia,2 Thierry Michon,1 and Olivier Le Gall1

Interactions Plante-Virus, UMR GDPP 1090, INRA Université de Bordeaux 2, BP 81, F-33883 Villenave d'Ornon Cedex, France,1 UMR 6191 CEA-CNRS-Aix-Marseille Université, Laboratoire de Génétique et Biophysique des Plantes, Faculté des Sciences de Luminy, 13009, Marseille, France,2 Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, United Kingdom3

Received 30 January 2008/ Accepted 6 May 2008

The eukaryotic translation initiation factor 4E (eIF4E) (the cap-binding protein) is involved in natural resistance against several potyviruses in plants. In lettuce, the recessive resistance genes mo11 and mo12 against Lettuce mosaic virus (LMV) are alleles coding for forms of eIF4E unable, or less effective, to support virus accumulation. A recombinant LMV expressing the eIF4E of a susceptible lettuce variety from its genome was able to produce symptoms in mo11 or mo12 varieties. In order to identify the eIF4E amino acid residues necessary for viral infection, we constructed recombinant LMV expressing eIF4E with point mutations affecting various amino acids and compared the abilities of these eIF4E mutants to complement LMV infection in resistant plants. Three types of mutations were produced in order to affect different biochemical functions of eIF4E: cap binding, eIF4G binding, and putative interaction with other virus or host proteins. Several mutations severely reduced the ability of eIF4E to complement LMV accumulation in a resistant host and impeded essential eIF4E functions in yeast. However, the ability of eIF4E to bind a cap analogue or to fully interact with eIF4G appeared unlinked to LMV infection. In addition to providing a functional mutational map of a plant eIF4E, this suggests that the role of eIF4E in the LMV cycle might be distinct from its physiological function in cellular mRNA translation.


* Corresponding author. Mailing address: UMR 1090 GDPP INRA Université Bordeaux 2, BP-81, F-33883 Villenave d'Ornon Cedex, France. Phone: 33.557.122.378. Fax: 33.557.122.384. E-mail: german{at}bordeaux.inra.fr

{triangledown} Published ahead of print on 14 May 2008.


Journal of Virology, August 2008, p. 7601-7612, Vol. 82, No. 15
0022-538X/08/$08.00+0     doi:10.1128/JVI.00209-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.







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