Vibrio parahaemolyticus prey targeting requires autoproteolysis-triggered dimerization of the type VI secretion system effector RhsP
Le Tang, Shuqi Dong, Nadia Rasheed, Hao Wu, Ningkun Zhou, Huadong Li, Meilin Wang, Jun Zheng, Jun He, William Chong Hang Chao
Abstract
) can bind to VgrG2 via a VgrG2-interacting region (VIR). Our electron microscopy (EM) analysis reveals that the VIR is encapsulated inside the Rhs β barrel structure and that autoproteolysis triggers a dramatic conformational change of the VIR. This alternative VIR conformation promotes RhsP dimerization, which significantly contributes to T6SS2-mediated prey targeting by V. parahaemolyticus.
Topics & Concepts
Type VI secretion systemVibrio parahaemolyticusEffectorSecretionBiologyMicrobiologyCell biologyBiofilmVirulenceBacteriaBiochemistryGeneticsGeneVibrio bacteria research studiesEscherichia coli research studiesAntibiotic Resistance in Bacteria