Literature DB >> 15694855

Actin-based motility of intracellular pathogens.

Edith Gouin1, Matthew D Welch, Pascale Cossart.   

Abstract

The actin cytoskeleton is harnessed by several pathogenic bacteria that are capable of entering into non-phagocytic cells, the so-called 'invasive bacteria'. Among them, a few also exploit the host actin cytoskeleton to move intra- and inter-cellularly. Our knowledge of the basic mechanisms underlying actin-based motility has dramatically increased and the list of bacteria that are able to move in this way is also increasing including not only Listeria, Shigella and Rickettsia species but also Mycobacterium marinum and Burkholderia pseudomallei. In all cases the central player is the Arp2/3 complex. Vaccinia virus moves intracellularly on microtubules and just after budding, triggers actin polymerization and the formation of protrusions similar to that of adherent enteropathogenic Escherichia coli, that involve the Arp2/3 complex and facilitate its inter-cellular spread.

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Year:  2005        PMID: 15694855     DOI: 10.1016/j.mib.2004.12.013

Source DB:  PubMed          Journal:  Curr Opin Microbiol        ISSN: 1369-5274            Impact factor:   7.934


  138 in total

1.  Rickettsia Sca2 is a bacterial formin-like mediator of actin-based motility.

Authors:  Cat M Haglund; Julie E Choe; Colleen T Skau; David R Kovar; Matthew D Welch
Journal:  Nat Cell Biol       Date:  2010-10-24       Impact factor: 28.824

Review 2.  The emerging functions of septins in metazoans.

Authors:  Juha Saarikangas; Yves Barral
Journal:  EMBO Rep       Date:  2011-10-28       Impact factor: 8.807

3.  Actin filament curvature biases branching direction.

Authors:  Viviana I Risca; Evan B Wang; Ovijit Chaudhuri; Jia Jun Chia; Phillip L Geissler; Daniel A Fletcher
Journal:  Proc Natl Acad Sci U S A       Date:  2012-01-30       Impact factor: 11.205

4.  Intracellular trafficking of plasmids during transfection is mediated by microtubules.

Authors:  Erin E Vaughan; David A Dean
Journal:  Mol Ther       Date:  2005-11-21       Impact factor: 11.454

5.  Arp2/3 complex-deficient mouse fibroblasts are viable and have normal leading-edge actin structure and function.

Authors:  Alessia Di Nardo; Gregor Cicchetti; Hervé Falet; John H Hartwig; Thomas P Stossel; David J Kwiatkowski
Journal:  Proc Natl Acad Sci U S A       Date:  2005-10-27       Impact factor: 11.205

6.  New frontiers in immunology. Workshop on the road ahead: future directions in fundamental and clinical immunology.

Authors:  Bruce Beutler; Jean-Laurent Casanova
Journal:  EMBO Rep       Date:  2005-07       Impact factor: 8.807

7.  Enteropathogenic Escherichia coli, Shigella flexneri, and Listeria monocytogenes recruit a junctional protein, zonula occludens-1, to actin tails and pedestals.

Authors:  Miyuki Hanajima-Ozawa; Takeshi Matsuzawa; Aya Fukui; Shigeki Kamitani; Hiroe Ohnishi; Akio Abe; Yasuhiko Horiguchi; Masami Miyake
Journal:  Infect Immun       Date:  2006-11-21       Impact factor: 3.441

8.  Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex.

Authors:  Alexander E Kelly; Heather Kranitz; Volker Dötsch; R Dyche Mullins
Journal:  J Biol Chem       Date:  2005-12-23       Impact factor: 5.157

9.  Chlamydial TARP is a bacterial nucleator of actin.

Authors:  Travis J Jewett; Elizabeth R Fischer; David J Mead; Ted Hackstadt
Journal:  Proc Natl Acad Sci U S A       Date:  2006-10-06       Impact factor: 11.205

10.  Internalization of large double-membrane intercellular vesicles by a clathrin-dependent endocytic process.

Authors:  Michelle Piehl; Corinna Lehmann; Anna Gumpert; Jean-Pierre Denizot; Dominique Segretain; Matthias M Falk
Journal:  Mol Biol Cell       Date:  2006-11-15       Impact factor: 4.138

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