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. 2015 Oct 5;370(1679):20150021. doi: 10.1098/rstb.2015.0021

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© 2015 The Authors.

Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.

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Figure 1. — T6SS mode of action. Assembly of T6SS in an extended ‘ready to fire’ conformation starts by the assembly of a membrane complex composed of TssJLM. Effector domains can be either present on VgrG C-terminus and PAAR C- and N-termini or be preloaded onto VgrG/PAAR spike complex, optionally with an assistance of non-secreted chaperones. VgrG/PAAR/effector complex possibly together with TssEFG and K proteins form the baseplate in a conformation that initiates assembly of tube and sheath. Hexameric rings of Hcp, potentially with bound effectors, assemble to a long rigid tube that serves as a template for the assembly of an extended VipA/VipB sheath. Potential conformational change in the baseplate/membrane complex triggers the sheath contraction, which pushes the Hcp tube with the VgrG/PAAR spike and associated effectors from the cell to an extracellular space or across a target cell membrane. The contracted sheath is specifically recognized by ClpV ATPase, which unfolds the subunits and thus recycles them for a new round of assembly of an extended sheath.