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. 2019 Jul 11;10:1402. doi: 10.3389/fmicb.2019.01402

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Copyright © 2019 Yang, Xue, Tian, Hutchins, Yang and He.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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A schematic diagram showing the TriP-PdeR interaction resulting in enhanced PDE activity of PdeR in the presence of PdeK in Xanthomonas oryzae pv. Oryzae. PdeR functions as a PDE for c-di-GMP hydrolysis and forms a TCS with PdeK. TriP specifically interacts with the EAL domain of PdeR via the REC domain. The TriP-PdeR interaction significantly enhances PdeR's PDE ability for degradation of c-di-GMP into pGpG, thereby promoting EPS production and bacterial virulence in a c-di-GMP-dependent manner.