Document Detail

Concerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondii.
MedLine Citation:
PMID:  20949068     Owner:  NLM     Status:  MEDLINE    
The invasive forms of apicomplexan parasites share a conserved form of gliding motility that powers parasite migration across biological barriers, host cell invasion and egress from infected cells. Previous studies have established that the duration and direction of gliding motility are determined by actin polymerization; however, regulators of actin dynamics in apicomplexans remain poorly characterized. In the absence of a complete ARP2/3 complex, the formin homology 2 domain containing proteins and the accessory protein profilin are presumed to orchestrate actin polymerization during host cell invasion. Here, we have undertaken the biochemical and functional characterization of two Toxoplasma gondii formins and established that they act in concert as actin nucleators during invasion. The importance of TgFRM1 for parasite motility has been assessed by conditional gene disruption. The contribution of each formin individually and jointly was revealed by an approach based upon the expression of dominant mutants with modified FH2 domains impaired in actin binding but still able to dimerize with their respective endogenous formin. These mutated FH2 domains were fused to the ligand-controlled destabilization domain (DD-FKBP) to achieve conditional expression. This strategy proved unique in identifying the non-redundant and critical roles of both formins in invasion. These findings provide new insights into how controlled actin polymerization drives the directional movement required for productive penetration of parasites into host cells.
Wassim Daher; Fabienne Plattner; Marie-France Carlier; Dominique Soldati-Favre
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-10-07
Journal Detail:
Title:  PLoS pathogens     Volume:  6     ISSN:  1553-7374     ISO Abbreviation:  PLoS Pathog.     Publication Date:  2010  
Date Detail:
Created Date:  2010-10-15     Completed Date:  2011-03-07     Revised Date:  2013-07-03    
Medline Journal Info:
Nlm Unique ID:  101238921     Medline TA:  PLoS Pathog     Country:  United States    
Other Details:
Languages:  eng     Pagination:  e1001132     Citation Subset:  IM    
Department of Microbiology and Molecular Medicine, CMU, University of Geneva, Geneva, Switzerland.
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MeSH Terms
Actins / metabolism
Amino Acid Motifs / physiology
Amino Acid Sequence
Fetal Proteins / chemistry,  genetics,  metabolism,  physiology
Host-Parasite Interactions / physiology*
Microfilament Proteins / chemistry,  genetics,  metabolism,  physiology*
Microscopy, Video
Models, Biological
Molecular Sequence Data
Movement / physiology*
Mutant Proteins / metabolism,  physiology
Nuclear Proteins / chemistry,  genetics,  metabolism,  physiology
Protein Multimerization / genetics
Protein Structure, Tertiary / genetics
Tissue Distribution
Toxoplasma / genetics*,  metabolism,  physiology*,  ultrastructure
Grant Support
//Howard Hughes Medical Institute
Reg. No./Substance:
0/Actins; 0/Fetal Proteins; 0/Microfilament Proteins; 0/Mutant Proteins; 0/Nuclear Proteins; 147336-47-8/formin 1

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