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Plant Cell Advance Online Publication
Published on September 21, 2007; 10.1105/tpc.107.050997

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Received February 9, 2007
Returned for revision July 30, 2007
Accepted August 28, 2007

Functional Dissection of Naturally Occurring Amino Acid Substitutions in eIF4E That Confers Recessive Potyvirus Resistance in Plants

Inhwa Yeam 1, Jason R. Cavatorta 1, Daniel R. Ripoll 2, Byoung-Cheorl Kang 3, and Molly M. Jahn 4*

1 Department of Plant Breeding and Genetics, College of Agriculture and Life Sciences, Cornell University, Ithaca, New York 14853
2 Computational Biology Service Unit, Life Sciences Core Laboratories Center, Cornell University, Ithaca, New York 14853
3 Department of Plant Breeding and Genetics, College of Agriculture and Life Sciences, Cornell University, Ithaca, New York 14853; Department of Plant Science, College of Agriculture and Life Sciences, Seoul National University, Seoul 151-742, Republic of Korea
4 Department of Plant Breeding and Genetics, College of Agriculture and Life Sciences, Cornell University, Ithaca, New York 14853; College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin 53706

* To whom correspondence should be addressed. E-mail: mjahn{at}cals.wisc.edu.

Naturally existing variation in the eukaryotic translation initiation factor 4E (eIF4E) homolog encoded at the pvr1 locus in Capsicum results in recessively inherited resistance against several potyviruses. Previously reported data indicate that the physical interaction between Capsicum-eIF4E and the viral genome-linked protein (VPg) is required for the viral infection in the Capsicum-Tobacco etch virus (TEV) pathosystem. In this study, the potential structural role(s) of natural variation in the eIF4E protein encoded by recessive resistance alleles and their biological consequences have been assessed. Using high-resolution three-dimensional structural models based on the available crystallographic structures of eIF4E, we show that the amino acid substitution G107R, found in many recessive plant virus resistance genes encoding eIF4E, is predicted to result in a substantial modification in the protein binding pocket. The G107R change was shown to not only be responsible for the interruption of VPg binding in planta but also for the loss of cap binding ability in vitro, the principal function of eIF4E in the host. Overexpression of the Capsicum-eIF4E protein containing the G107R amino acid substitution in Solanum lycopersicum indicated that this polymorphism alone is sufficient for the acquisition of resistance against several TEV strains.




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