Document Detail


Entrapment of intracytosolic bacteria by septin cage-like structures.
MedLine Citation:
PMID:  21075354     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Actin-based motility is used by various pathogens for dissemination within and between cells. Yet host factors restricting this process have not been identified. Septins are GTP-binding proteins that assemble as filaments and are essential for cell division. However, their role during interphase has remained elusive. Here, we report that septin assemblies are recruited to different bacteria that polymerize actin. We observed that intracytosolic Shigella either become compartmentalized in septin cage-like structures or form actin tails. Inactivation of septin caging increases the number of Shigella with actin tails and enhances cell-to-cell spread. TNF-α, a host cytokine produced upon Shigella infection, stimulates septin caging and restricts actin tail formation and cell-to-cell spread. Finally, we show that septin cages entrap bacteria targeted to autophagy. Together, these results reveal an unsuspected mechanism of host defense that restricts dissemination of invasive pathogens.
Authors:
Serge Mostowy; Matteo Bonazzi; Mélanie Anne Hamon; To Nam Tham; Adeline Mallet; Mickaël Lelek; Edith Gouin; Caroline Demangel; Roland Brosch; Christophe Zimmer; Anna Sartori; Makoto Kinoshita; Marc Lecuit; Pascale Cossart
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cell host & microbe     Volume:  8     ISSN:  1934-6069     ISO Abbreviation:  Cell Host Microbe     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-11-15     Completed Date:  2011-03-01     Revised Date:  2014-02-20    
Medline Journal Info:
Nlm Unique ID:  101302316     Medline TA:  Cell Host Microbe     Country:  United States    
Other Details:
Languages:  eng     Pagination:  433-44     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier Inc. All rights reserved.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism
Caco-2 Cells / immunology,  microbiology,  ultrastructure
Cervix Uteri / cytology,  microbiology*
Colon / cytology,  microbiology*
Cytosol / microbiology*
Female
HeLa Cells / immunology,  microbiology,  ultrastructure
Host-Pathogen Interactions*
Humans
Septins / metabolism*
Shigella flexneri / metabolism,  pathogenicity*
Tumor Necrosis Factor-alpha / metabolism
Grant Support
ID/Acronym/Agency:
233348//European Research Council; //Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/Actins; 0/Tumor Necrosis Factor-alpha; EC 3.6.1.-/Septins
Comments/Corrections
Comment In:
Cell Host Microbe. 2010 Nov 18;8(5):391-3   [PMID:  21075349 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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