Literature DB >> 22545799

Surface organelles assembled by secretion systems of Gram-negative bacteria: diversity in structure and function.

David G Thanassi1, James B Bliska, Peter J Christie.   

Abstract

Gram-negative bacteria express a wide variety of organelles on their cell surface. These surface structures may be the end products of secretion systems, such as the hair-like fibers assembled by the chaperone/usher (CU) and type IV pilus pathways, which generally function in adhesion to surfaces and bacterial-bacterial and bacterial-host interactions. Alternatively, the surface organelles may be integral components of the secretion machinery itself, such as the needle complex and pilus extensions formed by the type III and type IV secretion systems, which function in the delivery of bacterial effectors inside host cells. Bacterial surface structures perform functions critical for pathogenesis and have evolved to withstand forces exerted by the external environment and cope with defenses mounted by the host immune system. Given their essential roles in pathogenesis and exposed nature, bacterial surface structures also make attractive targets for therapeutic intervention. This review will describe the structure and function of surface organelles assembled by four different Gram-negative bacterial secretion systems: the CU pathway, the type IV pilus pathway, and the type III and type IV secretion systems.
© 2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.

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Year:  2012        PMID: 22545799      PMCID: PMC3421059          DOI: 10.1111/j.1574-6976.2012.00342.x

Source DB:  PubMed          Journal:  FEMS Microbiol Rev        ISSN: 0168-6445            Impact factor:   16.408


  348 in total

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Authors:  Wendy E Thomas; Elena Trintchina; Manu Forero; Viola Vogel; Evgeni V Sokurenko
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2.  Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution.

Authors:  Richard F Collins; Stephan A Frye; Ashraf Kitmitto; Robert C Ford; Tone Tønjum; Jeremy P Derrick
Journal:  J Biol Chem       Date:  2004-07-14       Impact factor: 5.157

3.  Type 1 fimbrial adhesin FimH elicits an immune response that enhances cell adhesion of Escherichia coli.

Authors:  Veronika Tchesnokova; Pavel Aprikian; Dagmara Kisiela; Sarah Gowey; Natalia Korotkova; Wendy Thomas; Evgeni Sokurenko
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4.  Type IV pili of pathogenic Neisseriae elicit cortical plaque formation in epithelial cells.

Authors:  A J Merz; C A Enns; M So
Journal:  Mol Microbiol       Date:  1999-06       Impact factor: 3.501

Review 5.  Protein-translocating outer membrane porins of Gram-negative bacteria.

Authors:  Ming Ren Yen; Christopher R Peabody; Salar M Partovi; Yufeng Zhai; Yi Hsiung Tseng; Milton H Saier
Journal:  Biochim Biophys Acta       Date:  2002-05-03

6.  Agrobacterium tumefaciens VirB6 protein participates in formation of VirB7 and VirB9 complexes required for type IV secretion.

Authors:  Simon J Jakubowski; Vidhya Krishnamoorthy; Peter J Christie
Journal:  J Bacteriol       Date:  2003-05       Impact factor: 3.490

7.  Function of the usher N-terminus in catalysing pilus assembly.

Authors:  Nadine S Henderson; Tony W Ng; Iehab Talukder; David G Thanassi
Journal:  Mol Microbiol       Date:  2010-12-22       Impact factor: 3.501

8.  The structure of F-pili.

Authors:  Ying A Wang; Xiong Yu; Philip M Silverman; Robin L Harris; Edward H Egelman
Journal:  J Mol Biol       Date:  2008-10-25       Impact factor: 5.469

Review 9.  The structural biology of type IV secretion systems.

Authors:  Rémi Fronzes; Peter J Christie; Gabriel Waksman
Journal:  Nat Rev Microbiol       Date:  2009-10       Impact factor: 60.633

10.  Initiation of assembly and association of the structural elements of a bacterial pilus depend on two specialized tip proteins.

Authors:  F Jacob-Dubuisson; J Heuser; K Dodson; S Normark; S Hultgren
Journal:  EMBO J       Date:  1993-03       Impact factor: 11.598

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  58 in total

Review 1.  Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria.

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Journal:  Microbiol Spectr       Date:  2015-10

Review 2.  Type IV pili in Gram-positive bacteria.

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Journal:  Microbiol Mol Biol Rev       Date:  2013-09       Impact factor: 11.056

3.  The Escherichia coli P and Type 1 Pilus Assembly Chaperones PapD and FimC Are Monomeric in Solution.

Authors:  Samema Sarowar; Olivia J Hu; Glenn T Werneburg; David G Thanassi; Huilin Li
Journal:  J Bacteriol       Date:  2016-08-11       Impact factor: 3.490

Review 4.  A comprehensive guide to pilus biogenesis in Gram-negative bacteria.

Authors:  Manuela K Hospenthal; Tiago R D Costa; Gabriel Waksman
Journal:  Nat Rev Microbiol       Date:  2017-05-12       Impact factor: 60.633

5.  In vitro reconstitution of sortase-catalyzed pilus polymerization reveals structural elements involved in pilin cross-linking.

Authors:  Chungyu Chang; Brendan R Amer; Jerzy Osipiuk; Scott A McConnell; I-Hsiu Huang; Van Hsieh; Janine Fu; Hong H Nguyen; John Muroski; Erika Flores; Rachel R Ogorzalek Loo; Joseph A Loo; John A Putkey; Andrzej Joachimiak; Asis Das; Robert T Clubb; Hung Ton-That
Journal:  Proc Natl Acad Sci U S A       Date:  2018-05-29       Impact factor: 11.205

6.  DNA substrate-induced activation of the Agrobacterium VirB/VirD4 type IV secretion system.

Authors:  Eric Cascales; Krishnamohan Atmakuri; Mayukh K Sarkar; Peter J Christie
Journal:  J Bacteriol       Date:  2013-04-05       Impact factor: 3.490

Review 7.  Endocytosis of viruses and bacteria.

Authors:  Pascale Cossart; Ari Helenius
Journal:  Cold Spring Harb Perspect Biol       Date:  2014-08-01       Impact factor: 10.005

8.  Biological Diversity and Evolution of Type IV Secretion Systems.

Authors:  Peter J Christie; Laura Gomez Valero; Carmen Buchrieser
Journal:  Curr Top Microbiol Immunol       Date:  2017       Impact factor: 4.291

Review 9.  Pili Assembled by the Chaperone/Usher Pathway in Escherichia coli and Salmonella.

Authors:  Glenn T Werneburg; David G Thanassi
Journal:  EcoSal Plus       Date:  2018-03

10.  Bacteriocin protein BacL1 of Enterococcus faecalis is a peptidoglycan D-isoglutamyl-L-lysine endopeptidase.

Authors:  Jun Kurushima; Ikue Hayashi; Motoyuki Sugai; Haruyoshi Tomita
Journal:  J Biol Chem       Date:  2013-11-14       Impact factor: 5.157

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