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...

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Autores principales: Brian C Russo, Jeffrey K Duncan-Lowey, Poyin Chen, Marcia B Goldberg
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Publicado: Public Library of Science (PLoS) 2021
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Acceso en línea:https://doaj.org/article/af4cef629e8b44c59266d04ecf09c18c
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spelling oai:doaj.org-article:af4cef629e8b44c59266d04ecf09c18c2021-12-02T20:00:12ZThe type 3 secretion system requires actin polymerization to open translocon pores.1553-73661553-737410.1371/journal.ppat.1009932https://doaj.org/article/af4cef629e8b44c59266d04ecf09c18c2021-09-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.1009932https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Many 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.Brian C RussoJeffrey K Duncan-LoweyPoyin ChenMarcia B GoldbergPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 17, Iss 9, p e1009932 (2021)
institution DOAJ
collection DOAJ
language EN
topic Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
spellingShingle Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
Brian C Russo
Jeffrey K Duncan-Lowey
Poyin Chen
Marcia B Goldberg
The type 3 secretion system requires actin polymerization to open translocon pores.
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 article
author Brian C Russo
Jeffrey K Duncan-Lowey
Poyin Chen
Marcia B Goldberg
author_facet Brian C Russo
Jeffrey K Duncan-Lowey
Poyin Chen
Marcia B Goldberg
author_sort Brian C Russo
title 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_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_sort type 3 secretion system requires actin polymerization to open translocon pores.
publisher Public Library of Science (PLoS)
publishDate 2021
url https://doaj.org/article/af4cef629e8b44c59266d04ecf09c18c
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