A natural substitution of a conserved amino acid in eIF4E confers resistance against multiple potyviruses.

ABSTRACT: Eukaryotic translation initiation factor 4E (eIF4E), which plays a pivotal role in initiating translation in eukaryotic organisms, is often hijacked by the viral genome-linked protein to facilitate the infection of potyviruses. In this study, we found that the naturally occurring amino acid substitution D71G in eIF4E is widely present in potyvirus-resistant watermelon accessions and disrupts the interaction between watermelon eIF4E and viral genome-linked protein of papaya ringspot virus-watermelon strain, zucchini yellow mosaic virus or watermelon mosaic virus. Multiple sequence alignment and protein modelling showed that the amino acid residue D⁷¹ located in the cap-binding pocket of eIF4E is strictly conserved in many plant species. The mutation D71G in watermelon eIF4E confe

SUBMITTER: Zhou LX 

PROVIDER: S-EPMC10777747 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature