Details

Autor(en) / Beteiligte

• Zhou, Ling‐Xi
• Tian, Yan‐Ping
• Ren, Li‐Li
• Yan, Zhi‐Yong
• Jiang, Jun
• Shi, Qing‐Hua
• Geng, Chao
• Li, Xiang‐Dong

Titel

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

Ist Teil von

• Molecular plant pathology, 2024-01, Vol.25 (1), p.n/a

Ort / Verlag

Oxford: John Wiley & Sons, Inc

Erscheinungsjahr

2024

Quelle

Wiley-Blackwell Journals

Beschreibungen/Notizen

• 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 conferred resistance against papaya ringspot virus‐watermelon strain and zucchini yellow mosaic virus, and the equivalent mutation D55G in tobacco eIF4E conferred resistance to potato virus Y. Therefore, our finding provides a potential precise target for breeding plants resistant to multiple potyviruses. The amino acid substitution D71G in the cap‐binding pocket of watermelon eIF4E and its equivalent substitution D55G in tobacco eIF4E confers resistance to multiple potyviruses by disrupting the interaction between eIF4E and VPg.