ArticleProtein science : a publication of the Protein Society2013
Babesia divergens and Neospora caninum apical membrane antigen 1 structures reveal selectivity and plasticity in apicomplexan parasite host cell invasion.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 36 citations in OpenAlex.
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- Immunization of Cattle With Recombinant Structural Ectodomains I and II ofFrontiers in veterinary science · 2022Article
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- Complete Molecular and Immunoprotective Characterization ofFrontiers in 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
- Genetic characterization and molecular survey of Babesia bovis, Babesia bigemina and Babesia ovata in cattle, dairy cattle and yaks in China.Parasites & vectors · 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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- An Extended Surface Loop on Toxoplasma gondii Apical Membrane Antigen 1 (AMA1) Governs Ligand Binding Selectivity.PloS one · 2015Article
- Crystal structure of Plasmodium knowlesi apical membrane antigen 1 and its complex with an invasion-inhibitory monoclonal antibody.PloS one · 2015Article
- Molecular insights into the interaction between Plasmodium falciparum apical membrane antigen 1 and an invasion-inhibitory peptide.PloS one · 2014Article
- Toxoplasma gondii sporozoites invade host cells using two novel paralogues of RON2 and AMA1.PloS one · 2013Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Host cell invasion by the obligate intracellular apicomplexan parasites, including Plasmodium (malaria) and Toxoplasma (toxoplasmosis), requires a step-wise mechanism unique among known host-pathogen interactions. A key step is the formation of the moving junction (MJ) complex, a circumferential constriction between the apical tip of the parasite and the host cell membrane that traverses in a posterior direction to enclose the parasite in a protective vacuole essential for intracellular survival. The leading model of MJ assembly proposes that Rhoptry Neck Protein 2 (RON2) is secreted into the host cell and integrated into the membrane where it serves as the receptor for apical membrane antigen 1 (AMA1) on the parasite surface. We have previously demonstrated that the AMA1-RON2 interaction is an effective target for inhibiting apicomplexan invasion. To better understand the AMA1-dependant molecular recognition events that promote invasion, including the significant AMA1-RON2 interaction, we present the structural characterization of AMA1 from the apicomplexan parasites Babesia divergens (BdAMA1) and Neospora caninum (NcAMA1) by X-ray crystallography. These studies offer intriguing structural insight into the RON2-binding surface groove in the AMA1 apical domain, which shows clear evidence for receptor-ligand co-evolution, and the hyper variability of the membrane proximal domain, which in Plasmodium is responsible for direct binding to erythrocytes. By incorporating the structural analysis of BdAMA1 and NcAMA1 with existing AMA1 structures and complexes we were able to define conserved pockets in the AMA1 apical groove that could be targeted for the design of broadly reactive therapeutics.
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