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Structure of a pathogenic type 3 secretion system in action

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Structure of a pathogenic type 3 secretion system in action. / Radics, Julia; Königsmaier, Lisa; Marlovits, Thomas C.

In: NAT STRUCT MOL BIOL, Vol. 21, No. 1, 01.01.2014, p. 82-7.

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

Harvard

Radics, J, Königsmaier, L & Marlovits, TC 2014, 'Structure of a pathogenic type 3 secretion system in action', NAT STRUCT MOL BIOL, vol. 21, no. 1, pp. 82-7. https://doi.org/10.1038/nsmb.2722

APA

Radics, J., Königsmaier, L., & Marlovits, T. C. (2014). Structure of a pathogenic type 3 secretion system in action. NAT STRUCT MOL BIOL, 21(1), 82-7. https://doi.org/10.1038/nsmb.2722

Vancouver

Radics J, Königsmaier L, Marlovits TC. Structure of a pathogenic type 3 secretion system in action. NAT STRUCT MOL BIOL. 2014 Jan 1;21(1):82-7. https://doi.org/10.1038/nsmb.2722

Bibtex

@article{bc5deedc1bbb44e59ebf54c8d607a49b,
title = "Structure of a pathogenic type 3 secretion system in action",
abstract = "Type 3 secretion systems use 3.5-megadalton syringe-like, membrane-embedded 'injectisomes', each containing an ~800-{\AA}-long needle complex to connect intracellular compartments of infectious bacteria and hosts. Here we identify requirements for substrate association with, transport through and exit from the injectisome of Salmonella enterica serovar Typhimurium. This guided the design of substrates that become trapped within the secretion path and enabled visualization of injectisomes in action in situ. We used cryo-EM to define the secretion path, providing a structural explanation as to why effector proteins must be unfolded during transport. Furthermore, trapping of a heterologous substrate in the needle prevents secretion of natural bacterial effectors. Together, the data reveal the path of protein secretion across multiple membranes and show that mechanisms rejecting unacceptable substrates can be undermined, and transport of bacterial effectors across an already assembled type 3 secretion system can be inhibited.",
keywords = "Bacterial Proteins, Protein Conformation, Protein Transport, Salmonella enterica",
author = "Julia Radics and Lisa K{\"o}nigsmaier and Marlovits, {Thomas C}",
year = "2014",
month = jan,
day = "1",
doi = "10.1038/nsmb.2722",
language = "English",
volume = "21",
pages = "82--7",
journal = "NAT STRUCT MOL BIOL",
issn = "1545-9993",
publisher = "NATURE PUBLISHING GROUP",
number = "1",

}

RIS

TY - JOUR

T1 - Structure of a pathogenic type 3 secretion system in action

AU - Radics, Julia

AU - Königsmaier, Lisa

AU - Marlovits, Thomas C

PY - 2014/1/1

Y1 - 2014/1/1

N2 - Type 3 secretion systems use 3.5-megadalton syringe-like, membrane-embedded 'injectisomes', each containing an ~800-Å-long needle complex to connect intracellular compartments of infectious bacteria and hosts. Here we identify requirements for substrate association with, transport through and exit from the injectisome of Salmonella enterica serovar Typhimurium. This guided the design of substrates that become trapped within the secretion path and enabled visualization of injectisomes in action in situ. We used cryo-EM to define the secretion path, providing a structural explanation as to why effector proteins must be unfolded during transport. Furthermore, trapping of a heterologous substrate in the needle prevents secretion of natural bacterial effectors. Together, the data reveal the path of protein secretion across multiple membranes and show that mechanisms rejecting unacceptable substrates can be undermined, and transport of bacterial effectors across an already assembled type 3 secretion system can be inhibited.

AB - Type 3 secretion systems use 3.5-megadalton syringe-like, membrane-embedded 'injectisomes', each containing an ~800-Å-long needle complex to connect intracellular compartments of infectious bacteria and hosts. Here we identify requirements for substrate association with, transport through and exit from the injectisome of Salmonella enterica serovar Typhimurium. This guided the design of substrates that become trapped within the secretion path and enabled visualization of injectisomes in action in situ. We used cryo-EM to define the secretion path, providing a structural explanation as to why effector proteins must be unfolded during transport. Furthermore, trapping of a heterologous substrate in the needle prevents secretion of natural bacterial effectors. Together, the data reveal the path of protein secretion across multiple membranes and show that mechanisms rejecting unacceptable substrates can be undermined, and transport of bacterial effectors across an already assembled type 3 secretion system can be inhibited.

KW - Bacterial Proteins

KW - Protein Conformation

KW - Protein Transport

KW - Salmonella enterica

U2 - 10.1038/nsmb.2722

DO - 10.1038/nsmb.2722

M3 - SCORING: Journal article

C2 - 24317488

VL - 21

SP - 82

EP - 87

JO - NAT STRUCT MOL BIOL

JF - NAT STRUCT MOL BIOL

SN - 1545-9993

IS - 1

ER -