Research ExplorerPublicationsStructural and Functional Characterization of the Bacterial ...

Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus

Standard

Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus. / Dietsche, Tobias; Tesfazgi Mebrhatu, Mehari; Brunner, Matthias J; Abrusci, Patrizia; Franz-Wachtel, Mirita; Schärfe, Charlotta; Zilkenat, Susann; Grin, Iwan; Galán, Jorge E; Kohlbacher, Oliver; Lea, Susan; Macek, Boris; Marlovits, Thomas C; Robinson, Carol V; Wagner, Samuel.

In: PLOS PATHOG, Vol. 12, No. 12, 12.2016, p. e1006071.

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

Harvard

Dietsche, T, Tesfazgi Mebrhatu, M, Brunner, MJ, Abrusci, P, Franz-Wachtel, M, Schärfe, C, Zilkenat, S, Grin, I, Galán, JE, Kohlbacher, O, Lea, S, Macek, B, Marlovits, TC, Robinson, CV & Wagner, S 2016, 'Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus', PLOS PATHOG, vol. 12, no. 12, pp. e1006071. https://doi.org/10.1371/journal.ppat.1006071

APA

Dietsche, T., Tesfazgi Mebrhatu, M., Brunner, M. J., Abrusci, P., Franz-Wachtel, M., Schärfe, C., Zilkenat, S., Grin, I., Galán, J. E., Kohlbacher, O., Lea, S., Macek, B., Marlovits, T. C., Robinson, C. V., & Wagner, S. (2016). Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus. PLOS PATHOG, 12(12), e1006071. https://doi.org/10.1371/journal.ppat.1006071

Vancouver

Dietsche T, Tesfazgi Mebrhatu M, Brunner MJ, Abrusci P, Franz-Wachtel M, Schärfe C et al. Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus. PLOS PATHOG. 2016 Dec;12(12):e1006071. https://doi.org/10.1371/journal.ppat.1006071

Bibtex

@article{c190bff9815243afa8845af0ee93464c,
title = "Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus",
abstract = "Bacterial type III protein secretion systems inject effector proteins into eukaryotic host cells in order to promote survival and colonization of Gram-negative pathogens and symbionts. Secretion across the bacterial cell envelope and injection into host cells is facilitated by a so-called injectisome. Its small hydrophobic export apparatus components SpaP and SpaR were shown to nucleate assembly of the needle complex and to form the central {"}cup{"} substructure of a Salmonella Typhimurium secretion system. However, the in vivo placement of these components in the needle complex and their function during the secretion process remained poorly defined. Here we present evidence that a SpaP pentamer forms a 15 {\AA} wide pore and provide a detailed map of SpaP interactions with the export apparatus components SpaQ, SpaR, and SpaS. We further refine the current view of export apparatus assembly, consolidate transmembrane topology models for SpaP and SpaR, and present intimate interactions of the periplasmic domains of SpaP and SpaR with the inner rod protein PrgJ, indicating how export apparatus and needle filament are connected to create a continuous conduit for substrate translocation.",
keywords = "Journal Article",
author = "Tobias Dietsche and {Tesfazgi Mebrhatu}, Mehari and Brunner, {Matthias J} and Patrizia Abrusci and Mirita Franz-Wachtel and Charlotta Sch{\"a}rfe and Susann Zilkenat and Iwan Grin and Gal{\'a}n, {Jorge E} and Oliver Kohlbacher and Susan Lea and Boris Macek and Marlovits, {Thomas C} and Robinson, {Carol V} and Samuel Wagner",
year = "2016",
month = dec,
doi = "10.1371/journal.ppat.1006071",
language = "English",
volume = "12",
pages = "e1006071",
journal = "PLOS PATHOG",
issn = "1553-7366",
publisher = "Public Library of Science",
number = "12",

}

RIS

TY - JOUR

T1 - Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus

AU - Dietsche, Tobias

AU - Tesfazgi Mebrhatu, Mehari

AU - Brunner, Matthias J

AU - Abrusci, Patrizia

AU - Franz-Wachtel, Mirita

AU - Schärfe, Charlotta

AU - Zilkenat, Susann

AU - Grin, Iwan

AU - Galán, Jorge E

AU - Kohlbacher, Oliver

AU - Lea, Susan

AU - Macek, Boris

AU - Marlovits, Thomas C

AU - Robinson, Carol V

AU - Wagner, Samuel

PY - 2016/12

Y1 - 2016/12

N2 - Bacterial type III protein secretion systems inject effector proteins into eukaryotic host cells in order to promote survival and colonization of Gram-negative pathogens and symbionts. Secretion across the bacterial cell envelope and injection into host cells is facilitated by a so-called injectisome. Its small hydrophobic export apparatus components SpaP and SpaR were shown to nucleate assembly of the needle complex and to form the central "cup" substructure of a Salmonella Typhimurium secretion system. However, the in vivo placement of these components in the needle complex and their function during the secretion process remained poorly defined. Here we present evidence that a SpaP pentamer forms a 15 Å wide pore and provide a detailed map of SpaP interactions with the export apparatus components SpaQ, SpaR, and SpaS. We further refine the current view of export apparatus assembly, consolidate transmembrane topology models for SpaP and SpaR, and present intimate interactions of the periplasmic domains of SpaP and SpaR with the inner rod protein PrgJ, indicating how export apparatus and needle filament are connected to create a continuous conduit for substrate translocation.

AB - Bacterial type III protein secretion systems inject effector proteins into eukaryotic host cells in order to promote survival and colonization of Gram-negative pathogens and symbionts. Secretion across the bacterial cell envelope and injection into host cells is facilitated by a so-called injectisome. Its small hydrophobic export apparatus components SpaP and SpaR were shown to nucleate assembly of the needle complex and to form the central "cup" substructure of a Salmonella Typhimurium secretion system. However, the in vivo placement of these components in the needle complex and their function during the secretion process remained poorly defined. Here we present evidence that a SpaP pentamer forms a 15 Å wide pore and provide a detailed map of SpaP interactions with the export apparatus components SpaQ, SpaR, and SpaS. We further refine the current view of export apparatus assembly, consolidate transmembrane topology models for SpaP and SpaR, and present intimate interactions of the periplasmic domains of SpaP and SpaR with the inner rod protein PrgJ, indicating how export apparatus and needle filament are connected to create a continuous conduit for substrate translocation.

KW - Journal Article

U2 - 10.1371/journal.ppat.1006071

DO - 10.1371/journal.ppat.1006071

M3 - SCORING: Journal article

C2 - 27977800

VL - 12

SP - e1006071

JO - PLOS PATHOG

JF - PLOS PATHOG

SN - 1553-7366

IS - 12

ER -