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PLoS One. 2014 Nov 17;9(11):e110810. doi: 10.1371/journal.pone.0110810. eCollection 2014.

A disordered region in the EvpP protein from the type VI secretion system of Edwardsiella tarda is essential for EvpC binding.

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Department of Biological Sciences, 14 Science Drive 4, National University of Singapore, Singapore, Singapore 117543.
Department of Biology, Faculty of Natural and Applied Sciences, Trinity Western University, Langley, British Columbia, Canada V2Y 1Y1; State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China 200237.


The type VI secretion system (T6SS) of pathogenic bacteria plays important roles in both virulence and inter-bacterial competitions. The effectors of T6SS are presumed to be transported either by attaching to the tip protein or by interacting with HcpI (haemolysin corregulated protein 1). In Edwardsiella tarda PPD130/91, the T6SS secreted protein EvpP (E. tarda virulent protein P) is found to be essential for virulence and directly interacts with EvpC (Hcp-like), suggesting that it could be a potential effector. Using limited protease digestion, nuclear magnetic resonance heteronuclear Nuclear Overhauser Effects, and hydrogen-deuterium exchange mass spectrometry, we confirmed that the dimeric EvpP (40 kDa) contains a substantial proportion (40%) of disordered regions but still maintains an ordered and folded core domain. We show that an N-terminal, 10-kDa, protease-resistant fragment in EvpP connects to a shorter, 4-kDa protease-resistant fragment through a highly flexible region, which is followed by another disordered region at the C-terminus. Within this C-terminal disordered region, residues Pro143 to Ile168 are essential for its interaction with EvpC. Unlike the highly unfolded T3SS effector, which has a lower molecular weight and is maintained in an unfolded conformation with a dedicated chaperone, the T6SS effector seems to be relatively larger, folded but partially disordered and uses HcpI as a chaperone.

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