BamA and BamD Are Essential for the Secretion of Trimeric Autotransporter Adhesins
The BAM complex in Escherichia coli is composed of five proteins, BamA-E. BamA and BamD are essential for cell viability and are required for the assembly of β-barrel outer membrane proteins. Consequently, BamA and BamD are indispensable for secretion via the classical autotransporter pathway (Type...
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Frontiers Media S.A.
2021-02-01
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Series: | Frontiers in Microbiology |
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Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2021.628879/full |
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author | Jessica L. Rooke Jessica L. Rooke Christopher Icke Christopher Icke Timothy J. Wells Timothy J. Wells Amanda E. Rossiter Douglas F. Browning Faye C. Morris Jack C. Leo Jack C. Leo Monika S. Schütz Ingo B. Autenrieth Adam F. Cunningham Dirk Linke Ian R. Henderson Ian R. Henderson |
author_facet | Jessica L. Rooke Jessica L. Rooke Christopher Icke Christopher Icke Timothy J. Wells Timothy J. Wells Amanda E. Rossiter Douglas F. Browning Faye C. Morris Jack C. Leo Jack C. Leo Monika S. Schütz Ingo B. Autenrieth Adam F. Cunningham Dirk Linke Ian R. Henderson Ian R. Henderson |
author_sort | Jessica L. Rooke |
collection | DOAJ |
description | The BAM complex in Escherichia coli is composed of five proteins, BamA-E. BamA and BamD are essential for cell viability and are required for the assembly of β-barrel outer membrane proteins. Consequently, BamA and BamD are indispensable for secretion via the classical autotransporter pathway (Type 5a secretion). In contrast, BamB, BamC, and BamE are not required for the biogenesis of classical autotransporters. Recently, we demonstrated that TamA, a homologue of BamA, and its partner protein TamB, were required for efficient secretion of proteins via the classical autotransporter pathway. The trimeric autotransporters are a subset of the Type 5-secreted proteins. Unlike the classical autotransporters, they are composed of three identical polypeptide chains which must be assembled together to allow secretion of their cognate passenger domains. In contrast to the classical autotransporters, the role of the Bam and Tam complex components in the biogenesis of the trimeric autotransporters has not been investigated fully. Here, using the Salmonella enterica trimeric autotransporter SadA and the structurally similar YadA protein of Yersinia spp., we identify the importance of BamA and BamD in the biogenesis of the trimeric autotransporters and reveal that BamB, BamC, BamE, TamA and TamB are not required for secretion of functional passenger domain on the cell surface.ImportanceThe secretion of trimeric autotransporters (TAA’s) has yet to be fully understood. Here we show that efficient secretion of TAAs requires the BamA and D proteins, but does not require BamB, C or E. In contrast to classical autotransporter secretion, neither trimeric autotransporter tested required TamA or B proteins to be functionally secreted. |
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language | English |
last_indexed | 2024-12-19T06:39:36Z |
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spelling | doaj.art-fd9ef170f5574032b9cbbacb3621a6cb2022-12-21T20:32:07ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2021-02-011210.3389/fmicb.2021.628879628879BamA and BamD Are Essential for the Secretion of Trimeric Autotransporter AdhesinsJessica L. Rooke0Jessica L. Rooke1Christopher Icke2Christopher Icke3Timothy J. Wells4Timothy J. Wells5Amanda E. Rossiter6Douglas F. Browning7Faye C. Morris8Jack C. Leo9Jack C. Leo10Monika S. Schütz11Ingo B. Autenrieth12Adam F. Cunningham13Dirk Linke14Ian R. Henderson15Ian R. Henderson16Institute for Molecular Bioscience, University of Queensland, St Lucia, QLD, AustraliaInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United KingdomInstitute for Molecular Bioscience, University of Queensland, St Lucia, QLD, AustraliaInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United KingdomInstitute for Molecular Bioscience, University of Queensland, St Lucia, QLD, AustraliaThe University of Queensland Diamantina Institute, The University of Queensland, Brisbane, QLD, AustraliaInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United KingdomInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United KingdomInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United KingdomDepartment of Biosciences, Nottingham Trent University, Nottingham, United KingdomDepartment of Biosciences, University of Oslo, Oslo, NorwayInstitut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum Tübingen, Tübingen, GermanyInstitut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum Tübingen, Tübingen, GermanyInstitute of Immunology and Immunotherapy, University of Birmingham, Birmingham, United KingdomDepartment of Biosciences, University of Oslo, Oslo, NorwayInstitute for Molecular Bioscience, University of Queensland, St Lucia, QLD, AustraliaInstitute of Microbiology and Infection, University of Birmingham, Birmingham, United KingdomThe BAM complex in Escherichia coli is composed of five proteins, BamA-E. BamA and BamD are essential for cell viability and are required for the assembly of β-barrel outer membrane proteins. Consequently, BamA and BamD are indispensable for secretion via the classical autotransporter pathway (Type 5a secretion). In contrast, BamB, BamC, and BamE are not required for the biogenesis of classical autotransporters. Recently, we demonstrated that TamA, a homologue of BamA, and its partner protein TamB, were required for efficient secretion of proteins via the classical autotransporter pathway. The trimeric autotransporters are a subset of the Type 5-secreted proteins. Unlike the classical autotransporters, they are composed of three identical polypeptide chains which must be assembled together to allow secretion of their cognate passenger domains. In contrast to the classical autotransporters, the role of the Bam and Tam complex components in the biogenesis of the trimeric autotransporters has not been investigated fully. Here, using the Salmonella enterica trimeric autotransporter SadA and the structurally similar YadA protein of Yersinia spp., we identify the importance of BamA and BamD in the biogenesis of the trimeric autotransporters and reveal that BamB, BamC, BamE, TamA and TamB are not required for secretion of functional passenger domain on the cell surface.ImportanceThe secretion of trimeric autotransporters (TAA’s) has yet to be fully understood. Here we show that efficient secretion of TAAs requires the BamA and D proteins, but does not require BamB, C or E. In contrast to classical autotransporter secretion, neither trimeric autotransporter tested required TamA or B proteins to be functionally secreted.https://www.frontiersin.org/articles/10.3389/fmicb.2021.628879/fullautotransportertrimeric autotransporter adhesinBam complexouter membrane assemblyprotein secretion |
spellingShingle | Jessica L. Rooke Jessica L. Rooke Christopher Icke Christopher Icke Timothy J. Wells Timothy J. Wells Amanda E. Rossiter Douglas F. Browning Faye C. Morris Jack C. Leo Jack C. Leo Monika S. Schütz Ingo B. Autenrieth Adam F. Cunningham Dirk Linke Ian R. Henderson Ian R. Henderson BamA and BamD Are Essential for the Secretion of Trimeric Autotransporter Adhesins Frontiers in Microbiology autotransporter trimeric autotransporter adhesin Bam complex outer membrane assembly protein secretion |
title | BamA and BamD Are Essential for the Secretion of Trimeric Autotransporter Adhesins |
title_full | BamA and BamD Are Essential for the Secretion of Trimeric Autotransporter Adhesins |
title_fullStr | BamA and BamD Are Essential for the Secretion of Trimeric Autotransporter Adhesins |
title_full_unstemmed | BamA and BamD Are Essential for the Secretion of Trimeric Autotransporter Adhesins |
title_short | BamA and BamD Are Essential for the Secretion of Trimeric Autotransporter Adhesins |
title_sort | bama and bamd are essential for the secretion of trimeric autotransporter adhesins |
topic | autotransporter trimeric autotransporter adhesin Bam complex outer membrane assembly protein secretion |
url | https://www.frontiersin.org/articles/10.3389/fmicb.2021.628879/full |
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