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銆€銆€銆愯嫳鏂囨憳瑕併€�

 

銆€銆€Many virus genomes encode proteases that facilitate infection. The molecular mechanism of plant recognition of viral proteases is largely unexplored. Using the system ofVigna unguiculataand cowpea mosaic virus 锛圕PMV锛夛紝 we identified a cowpea lipid transfer protein 锛圠TP1锛� which interacts with CPMV-encoded 24KPro, a cysteine protease, but not with the enzymatically inactive mutant 24KPro锛圕166A锛夈€� Biochemical assays showed that LTP1 inhibited 24KPro proteolytic cleavage of the coat protein precursor LCP-sCP. Transient overexpression of LTP1 in cowpea reduced CPMV infection, whereas RNAi-mediatedLTP1silencing increased CPMV accumulation in cowpea. LTP1 is mainly localized in the apoplast of uninfected plant cells, and after CPMV infection, most of the LTP1 is relocated to intracellular compartments, including chloroplast. Moreover, in stableLTP1-transgenicN. benthamianaplants,LTP1 repressed SMV NIa protease activity and accumulation of soybean mosaic virus 锛圫MV锛� was significantly reduced. We propose that cowpea LTP1 suppresses CPMV and SMV accumulation by directly inhibiting viral cysteine protease activity.

 

銆€銆€璁烘枃閾炬帴锛� https://www.pnas.org/doi/10.1073/pnas.2403424121