Yujie Liu,Xinyv Li,Chu Gong,Yonghong Cao,Jun Wang,Min Han,Jun-Li Yang
Anthracnose is a plant disease caused by Colletotrichum spp ., known for its widespread infectivity and extreme destructiveness. Colletotrichum gloeosporioides is a representative pathogen of anthracnose in China. Gypenosides GP4 - GP7 , derived from Gynostemma pentaphyllum (Thunb.) Makino, could significantly inhibit the growth of C. gloeosporioides mycelial, with EC 50 values of 96.98, 27.5, 38.48, and 61.59 mg L −1 . The inhibitory effect of these compounds surpassed the commonly used chemical pesticide chlorothalonant and plant-derived pesticide matrine. Among them, the most active compound GP5 also showed a significant inhibitory effect on spore germination and bud tube elongation of C. gloeosporioides . In addition, GP5 could effectively suppress the spread of anthracnose spots in postharvest fruit. Transmission electron microscopy and fluorescence microscopy demonstrated that GP5 primarily exerted its antifungal function by activating cellular autophagy. Additionally, proteomics analysis revealed that GP5 had an antifungal effect against C. gloeosporioides by enhancing cellular autophagy through upregulation of the expression of the autophagy-related protein Atg8. This study presents a novel approach for the control and management of anthracnose in C. gloeosporioides . Consequently, GP5 has the potential to be developed as a plant-derived fungicide for the biological control of anthracnose.
Prevention and control of infection by porcine reproductive and respiratory syndrome virus (PRRSV) remains a challenge, due to our limited understanding of the PRRSV invasion mechanism. Our previous study has shown that PRRSV glycoprotein GP5 interacts with MYH9 C-terminal domain protein (PRA). Here we defined that the first ectodomain of GP5 (GP5-ecto-1) directly interacted with PRA and this interaction triggered PRA and endogenous MYH9 to form filament assembly. More importantly, MYH9 filament assembly was also formed in GP5-ecto-1-transfected MARC-145 cells. Notably, PRRSV infection of MARC-145 cells and porcine alveolar macrophages also induced endogenous MYH9 aggregation and polymerization that were required for subsequent PRRSV internalization. Moreover, overexpression of S100A4, a MYH9-specific disassembly inducer, in MARC-145 cells significantly resulted in diminished MYH9 aggregation and marked inhibition of subsequent virion internalization and infection by both PRRSV-1 and PRRSV-2 isolates. The collective results of this work reveal a novel molecular mechanism employed by MYH9 that helps PRRSV gain entry into permissive cells.
危险品化学品经营许可证（带存储）