Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794-5215, USA.
Sci Signal. 2011 Oct 18;4(195):ra69. doi: 10.1126/scisignal.2002124.
The SCF (Skp1-Cul1-F-box protein) ubiquitin ligase complex plays a pivotal role in various biological processes, including host-pathogen interactions. Many pathogens exploit the host SCF machinery to promote efficient infection by translocating pathogen-encoded F-box proteins into the host cell. How pathogens ensure sufficient amounts of the F-box effectors in the host cell despite the intrinsically unstable nature of F-box proteins, however, remains unclear. We found that the Agrobacterium F-box protein VirF, an important virulence factor, undergoes rapid degradation through the host proteasome pathway. This destabilization of VirF was counteracted by VirD5, another bacterial effector that physically associated with VirF. These observations reveal a previously unknown counterdefense strategy used by pathogens against potential host antimicrobial responses.
SCF(Skp1-Cul1-F-box 蛋白)泛素连接酶复合物在各种生物过程中发挥着关键作用,包括宿主-病原体相互作用。许多病原体利用宿主 SCF 机制,通过将病原体编码的 F-box 蛋白易位到宿主细胞中,来促进有效的感染。然而,尽管 F-box 蛋白本质上不稳定,但病原体如何确保宿主细胞中有足够数量的 F-box 效应物仍然不清楚。我们发现,根癌农杆菌 F-box 蛋白 VirF,一种重要的毒力因子,通过宿主蛋白酶体途径迅速降解。这种 VirF 的不稳定性被另一种细菌效应物 VirD5 抵消,VirD5 与 VirF 物理结合。这些观察结果揭示了一种以前未知的病原体对抗潜在宿主抗菌反应的反防御策略。