ArticleMalaria journal2019
Structure of Rhoptry Neck Protein 2 is essential for the interaction in vitro with Apical Membrane Antigen 1 in Plasmodium vivax.
Article in Malaria journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- Chemical Protein Engineering: Backbone Cyclization Rescues Folding of a 183-Residue Truncated Domain of Malaria Parasite Protein PfAMA1.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- The global transcriptome ofMicrobiology spectrum · 2023Article
- Efficient refolding and functional characterization ofBiochemistry and biophysics reports · 2021Article
- Antibodies Against theFrontiers in cellular and infection microbiology · 2021Article
- New highly antigenic linear B cell epitope peptides from PvAMA-1 as potential vaccine candidates.PloS one · 2021Article
- RON2, a novel gene inParasitology · 2019Article
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Authors and funding
7 authors.
Funding
Abstract
backgroundIn several Apicomplexa, the formation of moving junctions (MJs) at the interface between the external membranes of the invading parasite and the host cell is essential for the process of parasite invasion. In Plasmodium falciparum and Toxoplasma gondii, the MJ is composed of the Apical Membrane Antigen 1 (AMA1) and Rhoptry Neck Proteins (RONs) complex; specifically, AMA1 interacts with RON2 during host cell invasion.
methodsRecombinant proteins based on Plasmodium vivax RON2 (A2033-P2100) and its synthetic peptide fragments, one cyclic and one linear, based on PvRON2 (D2035-T2074) were generated and used to evaluate the interaction with P. vivax AMA1 (PvAMA1) by the far western blot, surface plasmon resonance (SPR), and isothermal titration microcalorimetry (ITC) methods. The structural studies of peptides were performed by circular dichroism, and the structural analysis of the complex of PvAMA1 with peptides based on PvRON2 (D2035-T2074) was conducted with small-angle X-ray scattering (SAXS).
resultsSurface plasmon resonance (KD = 23.91 ± 2.078 μmol/L) and ITC (K = 3 × 10
conclusionsThe results show that the PvRON2 structure, particularly the S-S bond between C2051 and C2063, is determinant for the existence of the interaction between PvAMA1 and PvRON2.
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