ArticleThe Journal of biological chemistry2010
Structural characterization of apical membrane antigen 1 (AMA1) from Toxoplasma gondii.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Functionality of Toxoplasma gondii antibodies in a population of Beninese pregnant women exposed to malaria.Scientific reports · 2025Article
- Studies on experimental animals immunized with different antigenic vaccine combinations of Neospora caninum of cattle origin.Parasites & vectors · 2025Article
- Potent AMA1-specific human monoclonal antibody against Plasmodium vivax Pre-erythrocytic and Blood Stages.Nature communications · 2024Article
- Structure guided mimicry of an essential P. falciparum receptor-ligand complex enhances cross neutralizing antibodies.Nature communications · 2023Article
- Structure guided mimicry of an essential P. falciparum receptor-ligand complex enhances cross neutralizing antibodies.Research square · 2023Article
- Mining the Proteome ofAnimals : an open access journal from MDPI · 2022Review
- Retrospective study of toxoplasmosis prevalence in pregnant women in Benin and its relation with malaria.PloS one · 2022Article
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- Article
- Proteomic and transcriptomic analyses of early and late-chronic Toxoplasma gondii infection shows novel and stage specific transcripts.BMC genomics · 2019Article
- Efficient invasion by Toxoplasma depends on the subversion of host protein networks.Nature microbiology · 2017Article
- Multilevel Precision-Based Rational Design of Chemical Inhibitors Targeting the Hydrophobic Cleft of Toxoplasma gondii Apical Membrane Antigen 1 (AMA1).Genomics & informatics · 2016Article
- Dissecting the interface between apicomplexan parasite and host cell: Insights from a divergent AMA-RON2 pair.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Stability of the Plasmodium falciparum AMA1-RON2 Complex Is Governed by the Domain II (DII) Loop.PloS one · 2016Article
- Global Analysis of Palmitoylated Proteins in Toxoplasma gondii.Cell host & microbe · 2015Article
- Expression, Purification, and Biological Characterization of Babesia microti Apical Membrane Antigen 1.Infection and immunity · 2015Article
- The apicomplexan glideosome and adhesins - Structures and function.Journal of structural biology · 2015Review
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- Protective immunity induced by peptides of AMA1, RON2 and RON4 containing T-and B-cell epitopes via an intranasal route against toxoplasmosis in mice.Parasites & vectors · 2015Article
- An Extended Surface Loop on Toxoplasma gondii Apical Membrane Antigen 1 (AMA1) Governs Ligand Binding Selectivity.PloS one · 2015Article
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Authors and funding
4 authors.
Funding
Abstract
Apical membrane antigen 1 (AMA1) is an essential component of the moving junction complex used by Apicomplexan parasites to invade host cells. We report the 2.0 A resolution x-ray crystal structure of the full ectodomain (domains I, II, and III) of AMA1 from the pervasive protozoan parasite Toxoplasma gondii. The structure of T. gondii AMA1 (TgAMA1) is the most complete of any AMA1 structure to date, with more than 97.5% of the ectodomain unambiguously modeled. Comparative sequence analysis reveals discrete segments of divergence in TgAMA1 that map to areas of established functional importance in AMA1 from Plasmodium vivax (PvAMA1) and Plasmodium falciparum (PfAMA1). Inspection of the TgAMA1 structure reveals a network of apical surface loops, reorganized in both size and chemistry relative to PvAMA1/PfAMA1, that appear to serve as structural filters restricting access to a central hydrophobic groove. The terminal portion of this groove is formed by an extended loop from DII that is 14 residues shorter in TgAMA1. A pair of tryptophan residues (Trp(353) and Trp(354)) anchor the DII loop in the hydrophobic groove and frame a conserved tyrosine (Tyr(230)), forming a contiguous surface that may be critical for moving junction assembly. The minimalist DIII structure folds into a cystine knot that probably stabilizes and orients the bulk of the ectodmain without providing excess surface area to which invasion-inhibitory antibodies can be generated. The detailed structural characterization of TgAMA1 provides valuable insight into the mechanism of host cell invasion by T. gondii.
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