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The type 3 secretion system requires actin polymerization to open translocon pores
Many bacterial pathogens require a type 3 secretion system (T3SS) to establish a niche. Host contact activates bacterial T3SS assembly of a translocon pore in the host plasma membrane. Following pore formation, the T3SS docks onto the translocon pore. Docking establishes a continuous passage that en...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8454972/ https://www.ncbi.nlm.nih.gov/pubmed/34499700 http://dx.doi.org/10.1371/journal.ppat.1009932 |
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author | Russo, Brian C. Duncan-Lowey, Jeffrey K. Chen, Poyin Goldberg, Marcia B. |
author_facet | Russo, Brian C. Duncan-Lowey, Jeffrey K. Chen, Poyin Goldberg, Marcia B. |
author_sort | Russo, Brian C. |
collection | PubMed |
description | Many bacterial pathogens require a type 3 secretion system (T3SS) to establish a niche. Host contact activates bacterial T3SS assembly of a translocon pore in the host plasma membrane. Following pore formation, the T3SS docks onto the translocon pore. Docking establishes a continuous passage that enables the translocation of virulence proteins, effectors, into the host cytosol. Here we investigate the contribution of actin polymerization to T3SS-mediated translocation. Using the T3SS model organism Shigella flexneri, we show that actin polymerization is required for assembling the translocon pore in an open conformation, thereby enabling effector translocation. Opening of the pore channel is associated with a conformational change to the pore, which is dependent upon actin polymerization and a coiled-coil domain in the pore protein IpaC. Analysis of an IpaC mutant that is defective in ruffle formation shows that actin polymerization-dependent pore opening is distinct from the previously described actin polymerization-dependent ruffles that are required for bacterial internalization. Moreover, actin polymerization is not required for other pore functions, including docking or pore protein insertion into the plasma membrane. Thus, activation of the T3SS is a multilayered process in which host signals are sensed by the translocon pore leading to the activation of effector translocation. |
format | Online Article Text |
id | pubmed-8454972 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-84549722021-09-22 The type 3 secretion system requires actin polymerization to open translocon pores Russo, Brian C. Duncan-Lowey, Jeffrey K. Chen, Poyin Goldberg, Marcia B. PLoS Pathog Research Article Many bacterial pathogens require a type 3 secretion system (T3SS) to establish a niche. Host contact activates bacterial T3SS assembly of a translocon pore in the host plasma membrane. Following pore formation, the T3SS docks onto the translocon pore. Docking establishes a continuous passage that enables the translocation of virulence proteins, effectors, into the host cytosol. Here we investigate the contribution of actin polymerization to T3SS-mediated translocation. Using the T3SS model organism Shigella flexneri, we show that actin polymerization is required for assembling the translocon pore in an open conformation, thereby enabling effector translocation. Opening of the pore channel is associated with a conformational change to the pore, which is dependent upon actin polymerization and a coiled-coil domain in the pore protein IpaC. Analysis of an IpaC mutant that is defective in ruffle formation shows that actin polymerization-dependent pore opening is distinct from the previously described actin polymerization-dependent ruffles that are required for bacterial internalization. Moreover, actin polymerization is not required for other pore functions, including docking or pore protein insertion into the plasma membrane. Thus, activation of the T3SS is a multilayered process in which host signals are sensed by the translocon pore leading to the activation of effector translocation. Public Library of Science 2021-09-09 /pmc/articles/PMC8454972/ /pubmed/34499700 http://dx.doi.org/10.1371/journal.ppat.1009932 Text en © 2021 Russo et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Russo, Brian C. Duncan-Lowey, Jeffrey K. Chen, Poyin Goldberg, Marcia B. The type 3 secretion system requires actin polymerization to open translocon pores |
title | The type 3 secretion system requires actin polymerization to open translocon pores |
title_full | The type 3 secretion system requires actin polymerization to open translocon pores |
title_fullStr | The type 3 secretion system requires actin polymerization to open translocon pores |
title_full_unstemmed | The type 3 secretion system requires actin polymerization to open translocon pores |
title_short | The type 3 secretion system requires actin polymerization to open translocon pores |
title_sort | type 3 secretion system requires actin polymerization to open translocon pores |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8454972/ https://www.ncbi.nlm.nih.gov/pubmed/34499700 http://dx.doi.org/10.1371/journal.ppat.1009932 |
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