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Integrin-Like Tethering of Motility Complexes at Bacterial Focal Adhesions

81 Pages Posted: 7 Jun 2018 Sneak Peek Status: Review Complete

See all articles by Salim T. Islam

Salim T. Islam

Institut national de la recherche scientifique (INRS) - INRS–Institut Armand-Frappier Research Centre

Akeisha M. Belgrave

Princeton University - Lewis-Sigler Institute for Integrative Genomics; Harrisburg University of Science and Technology - Integrative Sciences Program

Betty Fleuchot

Aix-Marseille University - Laboratoire de Chimie Bactérienne

Nicolas Y. Jolivet

Institut national de la recherche scientifique (INRS) - INRS–Institut Armand-Frappier Research Centre

Laetitia My

Aix-Marseille University - Laboratoire de Chimie Bactérienne

Laura M. Faure

Aix-Marseille University - Laboratoire de Chimie Bactérienne

Gaurav Sharma

University of California, Davis - Department of Microbiology and Molecular Genetics

David J. Lemon

Syracuse University - Department of Biology

Jean-Bernard Fiche

University of Montpellier - Center for Structural Biochemistry (CBS)

Benjamin T. Bratton

Princeton University - Lewis-Sigler Institute for Integrative Genomics

Mitchell Singer

University of California, Davis - Department of Microbiology and Molecular Genetics

Anthony G. Garza

Syracuse University - Department of Biology

Marcelo Nöllmann​

University of Angers - U1054; University of Montpellier - Center for Structural Biochemistry (CBS)

Joshua W. Shaevitz

Princeton University - Lewis-Sigler Institute for Integrative Genomics

Tâm Mignot

Aix-Marseille University - Laboratoire de Chimie Bactérienne

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Abstract

Directed surface motility of metazoan cells and protozoan parasites involves substratum engagement by surface-exposed integrin(-like) adhesins, directionally transported by molecular motors via coupling to the internal cytoskeleton. The predatory deltaproteobacterium Myxococcus xanthus uses a helically-trafficked motor at bacterial focal adhesions to power gliding motility. However, the mechanisms of gliding machinery-substratum coupling and force mechanotransduction between innermembrane motors and substratum are unknown. Herein, we use bead force spectroscopy and TIRF microscopy to characterize CglB as the essential substratum-coupling integrin αI-domain-like adhesin. Protease susceptibility reveals that CglB interacts with a globular-protein-accessorized β-barrel OM display platform, which regulates the cell-surface conformational state and accessibility of the adhesin. Surface retention of CglB is further regulated by a cell-surface metalloprotease, a phenomenon also modulated by the OM display platform. These data depict a complex mechanism for bacterial gliding adhesin secretion, cell-surface anchoring, and processing, with conserved themes between prokaryotic and eukaryotic cell motility.

Suggested Citation

Islam, Salim T. and Belgrave, Akeisha M. and Fleuchot, Betty and Jolivet, Nicolas Y. and My, Laetitia and Faure, Laura M. and Sharma, Gaurav and Lemon, David J. and Fiche, Jean-Bernard and Bratton, Benjamin T. and Singer, Mitchell and Garza, Anthony G. and Nöllmann​, Marcelo and Shaevitz, Joshua W. and Mignot, Tâm, Integrin-Like Tethering of Motility Complexes at Bacterial Focal Adhesions (2018). Available at SSRN: https://ssrn.com/abstract=3188409 or http://dx.doi.org/10.2139/ssrn.3188409
This is a paper under consideration at Cell Press and has not been peer-reviewed.

Salim T. Islam (Contact Author)

Institut national de la recherche scientifique (INRS) - INRS–Institut Armand-Frappier Research Centre ( email )

531, boulevard des Prairies
Laval, Québec H7V 1B7
Canada

Akeisha M. Belgrave

Princeton University - Lewis-Sigler Institute for Integrative Genomics

Carl Icahn Laboratory
Princeton, NJ 08544
United States

Harrisburg University of Science and Technology - Integrative Sciences Program

Harrisburg, PA 17101
United States

Betty Fleuchot

Aix-Marseille University - Laboratoire de Chimie Bactérienne

31 Chemin Joseph Aiguier
Marseille, 13402
France

Nicolas Y. Jolivet

Institut national de la recherche scientifique (INRS) - INRS–Institut Armand-Frappier Research Centre

531, boulevard des Prairies
Laval, Québec H7V 1B7
Canada

Laetitia My

Aix-Marseille University - Laboratoire de Chimie Bactérienne

31 Chemin Joseph Aiguier
Marseille, 13402
France

Laura M. Faure

Aix-Marseille University - Laboratoire de Chimie Bactérienne

31 Chemin Joseph Aiguier
Marseille, 13402
France

Gaurav Sharma

University of California, Davis - Department of Microbiology and Molecular Genetics

One Shields Ave
Davis, CA 95616
United States

David J. Lemon

Syracuse University - Department of Biology

107 College Place
110 Life Sciences Complex
Syracuse, NY 13244
United States

Jean-Bernard Fiche

University of Montpellier - Center for Structural Biochemistry (CBS)

France

Benjamin T. Bratton

Princeton University - Lewis-Sigler Institute for Integrative Genomics

Carl Icahn Laboratory
Princeton, NJ 08544
United States

Mitchell Singer

University of California, Davis - Department of Microbiology and Molecular Genetics

One Shields Ave
Davis, CA 95616
United States

Anthony G. Garza

Syracuse University - Department of Biology

107 College Place
110 Life Sciences Complex
Syracuse, NY 13244
United States

Marcelo Nöllmann​

University of Angers - U1054

France

University of Montpellier - Center for Structural Biochemistry (CBS)

France

Joshua W. Shaevitz

Princeton University - Lewis-Sigler Institute for Integrative Genomics

Carl Icahn Laboratory
Princeton, NJ 08544
United States

Tâm Mignot

Aix-Marseille University - Laboratoire de Chimie Bactérienne ( email )

31 Chemin Joseph Aiguier
Marseille, 13402
France

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