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Structural basis for subversion of host cell actin cytoskeleton during Salmonella infection

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Structural basis for subversion of host cell actin cytoskeleton during Salmonella infection. / Yuan, Biao; Scholz, Jonas; Wald, Jiri; Thuenauer, Roland; Hennell James, Rory; Ellenberg, Irina; Windhorst, Sabine; Faix, Jan; Marlovits, Thomas C.

In: SCI ADV, Vol. 9, No. 49, 08.12.2023, p. eadj5777.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Yuan, B, Scholz, J, Wald, J, Thuenauer, R, Hennell James, R, Ellenberg, I, Windhorst, S, Faix, J & Marlovits, TC 2023, 'Structural basis for subversion of host cell actin cytoskeleton during Salmonella infection', SCI ADV, vol. 9, no. 49, pp. eadj5777. https://doi.org/10.1126/sciadv.adj5777

APA

Yuan, B., Scholz, J., Wald, J., Thuenauer, R., Hennell James, R., Ellenberg, I., Windhorst, S., Faix, J., & Marlovits, T. C. (2023). Structural basis for subversion of host cell actin cytoskeleton during Salmonella infection. SCI ADV, 9(49), eadj5777. https://doi.org/10.1126/sciadv.adj5777

Vancouver

Yuan B, Scholz J, Wald J, Thuenauer R, Hennell James R, Ellenberg I et al. Structural basis for subversion of host cell actin cytoskeleton during Salmonella infection. SCI ADV. 2023 Dec 8;9(49):eadj5777. https://doi.org/10.1126/sciadv.adj5777

Bibtex

@article{3d2a43e8e7b34823be185fc62444890e,
title = "Structural basis for subversion of host cell actin cytoskeleton during Salmonella infection",
abstract = "Secreted bacterial type III secretion system (T3SS) proteins are essential for successful infection by many human pathogens. Both T3SS translocator SipC and effector SipA are critical for Salmonella infection by subversion of the host cell cytoskeleton, but the precise molecular interplay between them remains unknown. Here, using cryo-electron microscopy, we show that SipA binds along the F-actin grooves with a unique binding pattern. SipA stabilizes F-actin through charged interface residues and appears to prevent inorganic phosphate release through closure of the {"}back door{"} of adenosine 5'-triphosphate pocket. We also show that SipC enhances the binding of SipA to F-actin, thus demonstrating that a sequential presence of T3SS proteins in host cells is associated with a sequence of infection events-starting with actin nucleation, filament growth, and stabilization. Together, our data explain the coordinated interplay of a precisely tuned and highly effective mechanism during Salmonella infection and provide a blueprint for interfering with Salmonella effectors acting on actin.",
keywords = "Humans, Actins/metabolism, Cryoelectron Microscopy, Bacterial Proteins/metabolism, Actin Cytoskeleton/metabolism, Salmonella Infections",
author = "Biao Yuan and Jonas Scholz and Jiri Wald and Roland Thuenauer and {Hennell James}, Rory and Irina Ellenberg and Sabine Windhorst and Jan Faix and Marlovits, {Thomas C}",
year = "2023",
month = dec,
day = "8",
doi = "10.1126/sciadv.adj5777",
language = "English",
volume = "9",
pages = "eadj5777",
journal = "SCI ADV",
issn = "2375-2548",
publisher = "American Association for the Advancement of Science",
number = "49",

}

RIS

TY - JOUR

T1 - Structural basis for subversion of host cell actin cytoskeleton during Salmonella infection

AU - Yuan, Biao

AU - Scholz, Jonas

AU - Wald, Jiri

AU - Thuenauer, Roland

AU - Hennell James, Rory

AU - Ellenberg, Irina

AU - Windhorst, Sabine

AU - Faix, Jan

AU - Marlovits, Thomas C

PY - 2023/12/8

Y1 - 2023/12/8

N2 - Secreted bacterial type III secretion system (T3SS) proteins are essential for successful infection by many human pathogens. Both T3SS translocator SipC and effector SipA are critical for Salmonella infection by subversion of the host cell cytoskeleton, but the precise molecular interplay between them remains unknown. Here, using cryo-electron microscopy, we show that SipA binds along the F-actin grooves with a unique binding pattern. SipA stabilizes F-actin through charged interface residues and appears to prevent inorganic phosphate release through closure of the "back door" of adenosine 5'-triphosphate pocket. We also show that SipC enhances the binding of SipA to F-actin, thus demonstrating that a sequential presence of T3SS proteins in host cells is associated with a sequence of infection events-starting with actin nucleation, filament growth, and stabilization. Together, our data explain the coordinated interplay of a precisely tuned and highly effective mechanism during Salmonella infection and provide a blueprint for interfering with Salmonella effectors acting on actin.

AB - Secreted bacterial type III secretion system (T3SS) proteins are essential for successful infection by many human pathogens. Both T3SS translocator SipC and effector SipA are critical for Salmonella infection by subversion of the host cell cytoskeleton, but the precise molecular interplay between them remains unknown. Here, using cryo-electron microscopy, we show that SipA binds along the F-actin grooves with a unique binding pattern. SipA stabilizes F-actin through charged interface residues and appears to prevent inorganic phosphate release through closure of the "back door" of adenosine 5'-triphosphate pocket. We also show that SipC enhances the binding of SipA to F-actin, thus demonstrating that a sequential presence of T3SS proteins in host cells is associated with a sequence of infection events-starting with actin nucleation, filament growth, and stabilization. Together, our data explain the coordinated interplay of a precisely tuned and highly effective mechanism during Salmonella infection and provide a blueprint for interfering with Salmonella effectors acting on actin.

KW - Humans

KW - Actins/metabolism

KW - Cryoelectron Microscopy

KW - Bacterial Proteins/metabolism

KW - Actin Cytoskeleton/metabolism

KW - Salmonella Infections

U2 - 10.1126/sciadv.adj5777

DO - 10.1126/sciadv.adj5777

M3 - SCORING: Journal article

C2 - 38064550

VL - 9

SP - eadj5777

JO - SCI ADV

JF - SCI ADV

SN - 2375-2548

IS - 49

ER -