| Host cell entry by apicomplexa parasites requires actin polymerization in the host cell. | |
| | |
MedLine Citation:
|
PMID: 19286135 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Apicomplexa are obligate intracellular parasites that actively invade host cells using their membrane-associated, actin-myosin motor. The current view is that host cell invasion by Apicomplexa requires the formation of a parasite-host cell junction, which has been termed the moving junction, but does not require the active participation of host actin. Using Toxoplasma gondii tachyzoites and Plasmodium berghei sporozoites, we show that host actin participates in parasite entry. Parasites induce the formation of a ring-shaped F-actin structure in the host cell at the parasite-cell junction, which remains stable during parasite entry. The Arp2/3 complex, an actin-nucleating factor, is recruited at the ring structure and is important for parasite entry. We propose that Apicomplexa invasion of host cells requires not only the parasite motor but also de novo polymerization of host actin at the entry site for anchoring the junction on which the parasite pulls to penetrate the host cell. |
| | |
Authors:
|
Virginie Gonzalez; Audrey Combe; Violaine David; Nicholas A Malmquist; Violaine Delorme; Carole Leroy; Samantha Blazquez; Robert Ménard; Isabelle Tardieux |
Related Documents
:
|
18232735 - The evolution of quorum sensing in bacterial biofilms. 20872885 - An adaptable two-color flow cytometric assay to quantitate the invasion of erythrocytes... 1568565 - Adherence and internalization of helicobacter pylori by hep-2 cells. 16835795 - Moss-associated methylobacteria as phytosymbionts: an experimental study. 7296775 - Efficiency of isolation of revertible 6-thioguanine resistant clones is dependent on th... 18667025 - Establishment and characterization of a cell line (igsk-3) secreting human chorionic go... |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: Cell host & microbe Volume: 5 ISSN: 1934-6069 ISO Abbreviation: Cell Host Microbe Publication Date: 2009 Mar |
Date Detail:
|
Created Date: 2009-03-16 Completed Date: 2009-05-04 Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 101302316 Medline TA: Cell Host Microbe Country: United States |
Other Details:
|
Languages: eng Pagination: 259-72 Citation Subset: IM |
Affiliation:
|
Institut Cochin, Université Paris Descartes, CNRS (UMR 8104), Paris, France. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Actin-Related Protein 2-3 Complex
/
analysis Actins / metabolism* Animals Cell Line Cytoplasm / chemistry Host-Parasite Interactions* Humans Plasmodium berghei / physiology* Protein Multimerization* Toxoplasma / physiology* |
| Grant Support | |
ID/Acronym/Agency:
|
//Howard Hughes Medical Institute |
| Chemical | |
Reg. No./Substance:
|
0/Actin-Related Protein 2-3 Complex; 0/Actins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: IRSp53 Links the Enterohemorrhagic E. coli Effectors Tir and EspF(U) for Actin Pedestal Formation.
Next Document: Two Mosquito LRR Proteins Function as Complement Control Factors in the TEP1-Mediated Killing of Pla...