Discovery of an archetypal protein transport system in bacterial outer membranes

Joel Selkrig, Khedidja Mosbahi, Chaille T Webb, Matthew J Belousoff, Andrew J Perry, Timothy J Wells, Faye C Morris, Denisse L Leyton, Makrina Totsika, Minh-Duy Phan, Nemin Celik, Michelle Kelly, Clare Oates, Elizabeth L Hartland, Roy M Robins-Browne, Sri H Ramarathinam, Anthony W Purcell, Mark A Schembri, Richard A Strugnell, Ian R HendersonDaniel Walker, Trevor J Lithgow

Research output: Contribution to journalArticleResearchpeer-review

122 Citations (Scopus)

Abstract

Bacteria have mechanisms to export proteins for diverse purposes, including colonization of hosts and pathogenesis. A small number of archetypal bacterial secretion machines have been found in several groups of bacteria and mediate a fundamentally distinct secretion process. Perhaps erroneously, proteins called autotransporters have long been thought to be one of these protein secretion systems. Mounting evidence suggests that autotransporters might be substrates to be secreted, not an autonomous transporter system. We have discovered a new translocation and assembly module (TAM) that promotes efficient secretion of autotransporters in proteobacteria. Functional analysis of the TAM in Citrobacter rodentium, Salmonella enterica and Escherichia coli showed that it consists of an Omp85-family protein, TamA, in the outer membrane and TamB in the inner membrane of diverse bacterial species. The discovery of the TAM provides a new target for the development of therapies to inhibit colonization by bacterial pathogens.
Original languageEnglish
Pages (from-to)506 - 510
Number of pages5
JournalNature Structural and Molecular Biology
Volume19
Issue number5 (S 1)
DOIs
Publication statusPublished - 2012

Cite this

Selkrig, Joel ; Mosbahi, Khedidja ; Webb, Chaille T ; Belousoff, Matthew J ; Perry, Andrew J ; Wells, Timothy J ; Morris, Faye C ; Leyton, Denisse L ; Totsika, Makrina ; Phan, Minh-Duy ; Celik, Nemin ; Kelly, Michelle ; Oates, Clare ; Hartland, Elizabeth L ; Robins-Browne, Roy M ; Ramarathinam, Sri H ; Purcell, Anthony W ; Schembri, Mark A ; Strugnell, Richard A ; Henderson, Ian R ; Walker, Daniel ; Lithgow, Trevor J. / Discovery of an archetypal protein transport system in bacterial outer membranes. In: Nature Structural and Molecular Biology. 2012 ; Vol. 19, No. 5 (S 1). pp. 506 - 510.
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title = "Discovery of an archetypal protein transport system in bacterial outer membranes",
abstract = "Bacteria have mechanisms to export proteins for diverse purposes, including colonization of hosts and pathogenesis. A small number of archetypal bacterial secretion machines have been found in several groups of bacteria and mediate a fundamentally distinct secretion process. Perhaps erroneously, proteins called autotransporters have long been thought to be one of these protein secretion systems. Mounting evidence suggests that autotransporters might be substrates to be secreted, not an autonomous transporter system. We have discovered a new translocation and assembly module (TAM) that promotes efficient secretion of autotransporters in proteobacteria. Functional analysis of the TAM in Citrobacter rodentium, Salmonella enterica and Escherichia coli showed that it consists of an Omp85-family protein, TamA, in the outer membrane and TamB in the inner membrane of diverse bacterial species. The discovery of the TAM provides a new target for the development of therapies to inhibit colonization by bacterial pathogens.",
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doi = "10.1038/nsmb.2261",
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Selkrig, J, Mosbahi, K, Webb, CT, Belousoff, MJ, Perry, AJ, Wells, TJ, Morris, FC, Leyton, DL, Totsika, M, Phan, M-D, Celik, N, Kelly, M, Oates, C, Hartland, EL, Robins-Browne, RM, Ramarathinam, SH, Purcell, AW, Schembri, MA, Strugnell, RA, Henderson, IR, Walker, D & Lithgow, TJ 2012, 'Discovery of an archetypal protein transport system in bacterial outer membranes', Nature Structural and Molecular Biology, vol. 19, no. 5 (S 1), pp. 506 - 510. https://doi.org/10.1038/nsmb.2261

Discovery of an archetypal protein transport system in bacterial outer membranes. / Selkrig, Joel; Mosbahi, Khedidja; Webb, Chaille T; Belousoff, Matthew J; Perry, Andrew J; Wells, Timothy J; Morris, Faye C; Leyton, Denisse L; Totsika, Makrina; Phan, Minh-Duy; Celik, Nemin; Kelly, Michelle; Oates, Clare; Hartland, Elizabeth L; Robins-Browne, Roy M; Ramarathinam, Sri H; Purcell, Anthony W; Schembri, Mark A; Strugnell, Richard A; Henderson, Ian R; Walker, Daniel; Lithgow, Trevor J.

In: Nature Structural and Molecular Biology, Vol. 19, No. 5 (S 1), 2012, p. 506 - 510.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Selkrig, Joel

AU - Mosbahi, Khedidja

AU - Webb, Chaille T

AU - Belousoff, Matthew J

AU - Perry, Andrew J

AU - Wells, Timothy J

AU - Morris, Faye C

AU - Leyton, Denisse L

AU - Totsika, Makrina

AU - Phan, Minh-Duy

AU - Celik, Nemin

AU - Kelly, Michelle

AU - Oates, Clare

AU - Hartland, Elizabeth L

AU - Robins-Browne, Roy M

AU - Ramarathinam, Sri H

AU - Purcell, Anthony W

AU - Schembri, Mark A

AU - Strugnell, Richard A

AU - Henderson, Ian R

AU - Walker, Daniel

AU - Lithgow, Trevor J

PY - 2012

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AB - Bacteria have mechanisms to export proteins for diverse purposes, including colonization of hosts and pathogenesis. A small number of archetypal bacterial secretion machines have been found in several groups of bacteria and mediate a fundamentally distinct secretion process. Perhaps erroneously, proteins called autotransporters have long been thought to be one of these protein secretion systems. Mounting evidence suggests that autotransporters might be substrates to be secreted, not an autonomous transporter system. We have discovered a new translocation and assembly module (TAM) that promotes efficient secretion of autotransporters in proteobacteria. Functional analysis of the TAM in Citrobacter rodentium, Salmonella enterica and Escherichia coli showed that it consists of an Omp85-family protein, TamA, in the outer membrane and TamB in the inner membrane of diverse bacterial species. The discovery of the TAM provides a new target for the development of therapies to inhibit colonization by bacterial pathogens.

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U2 - 10.1038/nsmb.2261

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SP - 506

EP - 510

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JF - Nature Structural Biology

SN - 1545-9993

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ER -