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. 2019 Jan 16;294(10):3783–3793. doi: 10.1074/jbc.RA118.005072

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© 2019 Takaya et al.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 7. — Schematic of chaperone-mediated mechanism of substrate stabilization and switching in SPI2-T3SS. A, SsaH (H) interacts with SsaG (G), and the SsaG–SsaH complex interacts with SsaE (E) for stabilization. The SsaE–SsaH–SsaG complex interacts with the export apparatus through SsaE, leading to initiation of the secretion of SsaG and SsaI (I). B, SseB (B) in the cytosol also interacts with SsaE for stabilization. Secretion of SseB is prevented during SsaG and SsaI secretion. C, SsaP (P) promotes substrate switching (switch) upon completion of SsaG and SsaI polymerization. D, the SsaE–SseB complex associates with the export apparatus to guide the secretion of SseB, SseC (C), and SseD (D). E, following assembly of the translocation pore (C/D) in the phagosomal membrane, effectors (e) are translocated upon sensing neutral pH of the host cytosol environment. IM, inner membrane; OM, outer membrane.