Publication Date:
2011-07-23
Description:
Apicomplexan parasites such as Toxoplasma gondii and Plasmodium species actively invade host cells through a moving junction (MJ) complex assembled at the parasite-host cell interface. MJ assembly is initiated by injection of parasite rhoptry neck proteins (RONs) into the host cell, where RON2 spans the membrane and functions as a receptor for apical membrane antigen 1 (AMA1) on the parasite. We have determined the structure of TgAMA1 complexed with a RON2 peptide at 1.95 angstrom resolution. A stepwise assembly mechanism results in an extensive buried surface area, enabling the MJ complex to resist the mechanical forces encountered during host cell invasion. Besides providing insights into host cell invasion by apicomplexan parasites, the structure offers a basis for designing therapeutics targeting these global pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tonkin, Michelle L -- Roques, Magali -- Lamarque, Mauld H -- Pugniere, Martine -- Douguet, Dominique -- Crawford, Joanna -- Lebrun, Maryse -- Boulanger, Martin J -- MOP82915/Canadian Institutes of Health Research/Canada -- New York, N.Y. -- Science. 2011 Jul 22;333(6041):463-7. doi: 10.1126/science.1204988.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21778402" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Amino Acid Substitution
;
Antibodies, Monoclonal/immunology
;
Antibodies, Protozoan/immunology
;
Antigens, Protozoan/*chemistry/genetics/immunology/*metabolism
;
*Host-Parasite Interactions
;
Hydrophobic and Hydrophilic Interactions
;
Membrane Proteins/chemistry/immunology/metabolism
;
Models, Molecular
;
Molecular Sequence Data
;
Mutagenesis
;
Peptide Fragments/chemistry/metabolism
;
Plasmodium falciparum/chemistry/metabolism/pathogenicity
;
Protein Binding
;
Protein Conformation
;
Protein Interaction Domains and Motifs
;
Protein Structure, Secondary
;
Protozoan Proteins/*chemistry/immunology/*metabolism
;
Toxoplasma/chemistry/*metabolism/*pathogenicity/ultrastructure
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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