Literature DB >> 15866036

Trimeric autotransporters: a distinct subfamily of autotransporter proteins.

Shane E Cotter1, Neeraj K Surana, Joseph W St Geme.   

Abstract

Autotransporter proteins are a large family of gram-negative bacterial extracellular proteins. These proteins have a characteristic arrangement of functional domains, including an N-terminal signal peptide, an internal passenger domain, and a C-terminal translocator domain. Recent studies have identified a novel subfamily of autotransporters, defined by a short trimeric C-terminal translocator domain and known as trimeric autotransporters. In this article, we review our current knowledge of the structural and functional characteristics of trimeric autotransporters, highlighting the distinctions between this subfamily and conventional autotransporters. We speculate that trimeric autotransporters evolved to enable high-affinity multivalent adhesive interactions with host surfaces and circulating host molecules to take place.

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Year:  2005        PMID: 15866036     DOI: 10.1016/j.tim.2005.03.004

Source DB:  PubMed          Journal:  Trends Microbiol        ISSN: 0966-842X            Impact factor:   17.079


  101 in total

1.  The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportation.

Authors:  Kornelia M Mikula; Jack C Leo; Andrzej Łyskowski; Sylwia Kedracka-Krok; Artur Pirog; Adrian Goldman
Journal:  J Bacteriol       Date:  2011-12-09       Impact factor: 3.490

2.  Mapping of the Neisseria meningitidis NadA cell-binding site: relevance of predicted {alpha}-helices in the NH2-terminal and dimeric coiled-coil regions.

Authors:  Regina Tavano; Barbara Capecchi; Paolo Montanari; Susanna Franzoso; Oriano Marin; Maryta Sztukowska; Paola Cecchini; Daniela Segat; Maria Scarselli; Beatrice Aricò; Emanuele Papini
Journal:  J Bacteriol       Date:  2010-10-22       Impact factor: 3.490

3.  Molecular characterization of the EhaG and UpaG trimeric autotransporter proteins from pathogenic Escherichia coli.

Authors:  Makrina Totsika; Timothy J Wells; Christophe Beloin; Jaione Valle; Luke P Allsopp; Nathan P King; Jean-Marc Ghigo; Mark A Schembri
Journal:  Appl Environ Microbiol       Date:  2012-01-27       Impact factor: 4.792

Review 4.  Protein-translocating trimeric autotransporters of gram-negative bacteria.

Authors:  David S H Kim; Yi Chao; Milton H Saier
Journal:  J Bacteriol       Date:  2006-08       Impact factor: 3.490

5.  Trimeric autotransporters require trimerization of the passenger domain for stability and adhesive activity.

Authors:  Shane E Cotter; Neeraj K Surana; Susan Grass; Joseph W St Geme
Journal:  J Bacteriol       Date:  2006-08       Impact factor: 3.490

6.  Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter.

Authors:  Guoyu Meng; Neeraj K Surana; Joseph W St Geme; Gabriel Waksman
Journal:  EMBO J       Date:  2006-05-11       Impact factor: 11.598

7.  The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation.

Authors:  Nancy Rutherford; Marie-Eve Charbonneau; Frédéric Berthiaume; Jean-Michel Betton; Michael Mourez
Journal:  J Bacteriol       Date:  2006-06       Impact factor: 3.490

8.  The Haemophilus cryptic genospecies Cha adhesin has at least two variants that differ in host cell binding, bacterial aggregation, and biofilm formation properties.

Authors:  Jessica R McCann; Amanda J Sheets; Susan Grass; Joseph W St Geme
Journal:  J Bacteriol       Date:  2014-02-28       Impact factor: 3.490

9.  Autotransporter structure reveals intra-barrel cleavage followed by conformational changes.

Authors:  Travis J Barnard; Nathalie Dautin; Petra Lukacik; Harris D Bernstein; Susan K Buchanan
Journal:  Nat Struct Mol Biol       Date:  2007-11-11       Impact factor: 15.369

10.  Trimeric autotransporter DsrA is a major mediator of fibrinogen binding in Haemophilus ducreyi.

Authors:  William G Fusco; Christopher Elkins; Isabelle Leduc
Journal:  Infect Immun       Date:  2013-09-16       Impact factor: 3.441

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