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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Structure of Rhoptry Neck Protein 2 is essential for the interaction in vitro with Apical Membrane Antigen 1 in Plasmodium vivax

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Author(s):
Salgado-Mejias, Perla [1, 2] ; Alves, Flavio L. [3] ; Francoso, Katia S. [1] ; Riske, Karin A. [3] ; Silva, Emerson R. [3] ; Miranda, Antonio [3] ; Soares, Irene S. [1]
Total Authors: 7
Affiliation:
[1] Univ Sao Paulo, Sch Pharmaceut Sci, Dept Clin & Toxicol Anal, Sao Paulo, SP - Brazil
[2] Univ La Frontera, Fac Engn & Sci, Dept Chem Sci & Nat Resources, Temuco - Chile
[3] Univ Fed Sao Paulo, Dept Biofis, Sao Paulo, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Malaria Journal; v. 18, JAN 25 2019.
Web of Science Citations: 1
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=23.912.078mol/L) and ITC (K=3x10(5) mol/L) studies conclusively showed an interaction between the cyclic peptide based on PvRON2 and PvAMA1-His(6). In contrast, the linear peptide and recombinant PvRON2 (GST fusion protein) did not show an interaction with PvAMA1. However, the interaction among recombinant proteins PvRON2.2 and PvAMA1-His(6) was possible to show by far western blot.Conclusions The 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. (AU)

FAPESP's process: 12/13032-5 - Generation and analysis of the immunogenicity of recombinant proteins based on the different allelic forms of the circumsporozoite antigen of Plasmodium vivax aiming at the development of a universal vaccine against malaria
Grantee:Irene da Silva Soares
Support type: Research Projects - Thematic Grants
FAPESP's process: 12/17060-3 - Functional and immunological characterization of Plasmodium vivax RON2 protein
Grantee:Irene da Silva Soares
Support type: Regular Research Grants