Document Detail


Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites.
MedLine Citation:
PMID:  12718875     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Host cell invasion by apicomplexan parasites requires coordinated interactions between cell surface adhesins and the parasite cytoskeleton. We have identified a complex of parasite proteins, including the actin binding protein aldolase, which specifically interacts with the C-terminal domains of several parasite adhesins belonging to the thrombospondin-related anonymous protein (TRAP) family. Binding of aldolase to the adhesin was disrupted by mutation of a critical tryptophan in the C domain, a residue that was previously shown to be essential for parasite motility. Our findings reveal a potential role for aldolase in connecting TRAP family adhesins with the cytoskeleton, and provide a model linking adhesion with motility in apicomplexan parasites.
Authors:
Travis J Jewett; L David Sibley
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular cell     Volume:  11     ISSN:  1097-2765     ISO Abbreviation:  Mol. Cell     Publication Date:  2003 Apr 
Date Detail:
Created Date:  2003-04-29     Completed Date:  2003-06-18     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  9802571     Medline TA:  Mol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  885-94     Citation Subset:  IM    
Affiliation:
Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, Missouri 63110, USA.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AY250663
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MeSH Terms
Descriptor/Qualifier:
Animals
Apicomplexa / enzymology*,  pathogenicity,  ultrastructure
Cell Adhesion / genetics*
Cell Membrane / genetics,  metabolism*
Cell Movement / genetics
Cells, Cultured
Fructose-Bisphosphate Aldolase / genetics,  metabolism*
Host-Parasite Interactions / genetics,  physiology*
Humans
Male
Membrane Proteins / genetics,  metabolism
Microfilaments / genetics,  metabolism*
Molecular Sequence Data
Mutation / genetics
Plasmodium / enzymology,  pathogenicity,  ultrastructure
Protein Structure, Tertiary / genetics
Protozoan Infections / enzymology*,  physiopathology
Protozoan Proteins / genetics,  metabolism*
Sequence Homology, Amino Acid
Toxoplasma / enzymology,  pathogenicity,  ultrastructure
Tryptophan / genetics
Grant Support
ID/Acronym/Agency:
AI 34036/AI/NIAID NIH HHS; AI017172/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/MIC2 protein, Toxoplasma gondii; 0/Membrane Proteins; 0/Protozoan Proteins; 120300-02-9/thrombospondin-related adhesive protein, protozoan; 73-22-3/Tryptophan; EC 4.1.2.13/Fructose-Bisphosphate Aldolase

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


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