Coat protein of Chinese wheat mosaic virus upregulates and interacts with cytosolic glyceraldehyde-3-phosphate dehydrogenase, a negative regulator of plant autophagy, to promote virus infection

Erbo Niu, Chaozheng Ye, Wanying Zhao, Hideki Kondo, Yunfeng Wu, Jianping Chen, Andika Ida Bagus, Liying Sun

Research output: Contribution to journalArticlepeer-review

Abstract

Autophagy is an intracellular degradation mechanism involved in antiviral defense, but the strategies employed by plant viruses to counteract autophagy-related defense remain unknown for the majority of the viruses. Herein, we describe how the Chinese wheat mosaic virus (CWMV, genus Furovirus) interferes with autophagy and enhances its infection in Nicotiana benthamiana. Yeast two-hybrid screening and in vivo/in vitro assays revealed that the 19 kDa coat protein (CP19K) of CWMV interacts with cytosolic glyceraldehyde-3-phosphate dehydrogenases (GAPCs), negative regulators of autophagy, which bind autophagy-related protein 3 (ATG3), a key factor in autophagy. CP19K also directly interacts with ATG3, possibly leading to the formation of a CP19K–GAPC–ATG3 complex. CP19K–GAPC interaction appeared to intensify CP19K–ATG3 binding. Moreover, CP19K expression upregulated GAPC gene transcripts and reduced autophagic activities. Accordingly, the silencing of GAPC genes in transgenic N. benthamiana reduced CWMV accumulation, whereas CP19K overexpression enhanced it. Overall, our results suggest that CWMV CP19K interferes with autophagy through the promotion and utilization of the GAPC role as a negative regulator of autophagy.

Original languageEnglish
Pages (from-to)1631-1645
Number of pages15
JournalJournal of Integrative Plant Biology
Volume64
Issue number8
DOIs
Publication statusPublished - Aug 2022

Keywords

  • antiviral defense
  • autophagy
  • plant virus
  • protein interaction
  • viral coat protein

ASJC Scopus subject areas

  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Plant Science

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