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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 被引量:10

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摘要 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 k Da coat protein(CP19 K)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.CP19 K also directly interacts with ATG3,possibly leading to the formation of a CP19 K–GAPC–ATG3 complex.CP19 K–GAPC interaction appeared to intensify CP19 K–ATG3 binding.Moreover,CP19 K expression upregulated GAPC gene transcripts and reduced autophagic activities.Accordingly,the silencing of GAPC genes in transgenic N.benthamiana reduced CWMV accumulation,whereas CP19 K overexpression enhanced it.Overall,our results suggest that CWMV CP19 K interferes with autophagy through the promotion and utilization of the GAPC role as a negative regulator of autophagy.
出处 《Journal of Integrative Plant Biology》 SCIE CAS CSCD 2022年第8期1631-1645,共15页 植物学报(英文版)
基金 supported in part by the National Natural Science Foundation of China(32170163) the Basic Scientific Research Foundation,Ministry of education of China(Z109021801)to Liying Sun The program of introducing Talents of Innovative Discipline to Universities(project 111)(B18042)and(2016KW-069)to Liying Sun。
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