The Rice RBRL Protein: The Hub of a Triple Antivirus Network

Jing Liu; Sheng Wang; Wishwajith Kandegama; Xin Xie; Xiangyang Li

doi:10.1016/j.eng.2026.02.032

Engineering ›› :202602032 DOI: 10.1016/j.eng.2026.02.032

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The Rice RBRL Protein: The Hub of a Triple Antivirus Network

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Abstract

Upon virus entry into rice cells, facilitated by insect vectors, the viral CP is recognized and bound by the RING-type ubiquitin ligase RBRL, which subsequently activates its E3 ubiquitin ligase activity. This activation results in the ubiquitination and subsequent degradation of NINJA3, a known inhibitor of the jasmonic acid (JA) signaling pathway. Degradation of NINJA3 alleviates the inhibitor’s repression of the JA signaling pathway, facilitating pathway activation, which leads to the upregulation of genes responsible for JA biosynthesis and the expression of downstream antiviral factors, including AGO18. This mechanism also inhibits viral replication through enhanced RNA interference, ultimately enabling rice plants to mount a robust antiviral defense.

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Jing Liu, Sheng Wang, Wishwajith Kandegama, Xin Xie, Xiangyang Li. The Rice RBRL Protein: The Hub of a Triple Antivirus Network. Engineering 202602032 DOI:10.1016/j.eng.2026.02.032

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