期刊
MOLECULAR PLANT-MICROBE INTERACTIONS
卷 25, 期 12, 页码 1562-1573出版社
AMER PHYTOPATHOLOGICAL SOC
DOI: 10.1094/MPMI-04-12-0091-R
关键词
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资金
- SUNY
- National Science Foundation (NSF) [DBI-0218166]
- Kwanjeong Educational Foundation
- United States Department of Agriculture Initiative for Future Agriculture, Food Systems Award [2001-52100-113347]
- National Research Foundation of Korea (NRF)
- Ministry of Education, Science and Technology [NRF 2011-0014507]
Potyvirus resistance in Capsicum spp. has been attributed to amino acid substitutions at the pvr1 locus that cause conformational shifts in eukaryotic translation initiation factor eIF4E. The viral genome-linked protein (VPg) sequence was isolated and compared from three Tobacco etch virus (TEV) strains, highly aphid-transmissible (HAT), Mex21, and N, which differentially infect Capsicum genotypes encoding Pvr1(+), pyr1, and pvr1(2). Viral chimeras were synthesized using the TEV-HAT genome, replacing HAT VPg with Mex21 or N VPg. TEV HAT did not infect pepper plants homozygous for either the pvr1 or pvr1(2) allele. However, the novel chimeric TEV strains, TEV-HAT(Mex21-VPg) and TEV-HAT(N-VPg), infected pyr1 and pvr1(2) pepper plants, respectively, demonstrating that VPg is the virulence determinant in this pathosystem. Three-dimensional structural models predicted interaction between VPg and the susceptible eIF4E genotype in every case, while resistant genotypes were never predicted to interact. To determine whether there is a correlation between physical interaction of VPg with eIF4E and infectivity, the effects of amino acid variation within VPg were assessed. Interaction between pvr1(2) eIF4E and N VPg was detected in planta, implying that the six amino acid differences in N VPg relative to HAT VPg are responsible for restoring the physical interaction and infectivity.
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