HIGH-LEVEL EXPRESSION, PURIFICATION AND CHARACTERIZATION OF A RECOMBINANTPLASMODIUM VIVAX APICAL MEMBRANE ANTIGEN 1: IMPLICATION FOR VIVAX MALARIA VACCINE DEVELOPMENT

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SALAVATIFAR MARYAM; ZAKERI SEDIGHEH; HAYATI ROODBARI NASIM; DINPARAST DJADID NAVID

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Paper Information

Journal: Cell Journal (Yakhteh) Year:2015 | Volume:17 | Issue:3 (67) Page(s): 520-531

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Title

HIGH-LEVEL EXPRESSION, PURIFICATION AND CHARACTERIZATION OF A RECOMBINANTPLASMODIUM VIVAX APICAL MEMBRANE ANTIGEN 1: IMPLICATION FOR VIVAX MALARIA VACCINE DEVELOPMENT

Author(s)

SALAVATIFAR MARYAM | ZAKERI SEDIGHEH | HAYATI ROODBARI NASIM | DINPARAST DJADID NAVID | Issue Writer Certificate

Keywords

MALARIA

PLASMODIUM VIVAX

APICAL MEMBRANE ANTIGEN-1

VACCINE

Abstract

Objective: The APICAL MEMBRANE ANTIGEN-1 (AMA-1) is considered as a promising candidate for development of a MALARIA VACCINE againstPlasmodium parasites. The correct conformation of this protein appears to be necessary for the stimulation of parasite-inhibitory responses, and these responses, in turn, seem to be antibody-mediated. Therefore, in the present investigation, we expressed thePlasmodium vivax AMA-1 (PvAMA-1) ectodomain inEscherichia coli (E. coli), purified it using standard procedures and characterized it to determine its biological activities for it to be used as a potential target for developing a protective and safe vivax MALARIA VACCINE.Materials and Methods: In this experimental investigation, the ectodomain of PvAMA-1 antigen (GenBank accession no. JX624741) was expressed in theE. coli M15-pQE30 expression system and purified with immobilized-metal affinity chromatography.The correct conformation of the recombinant protein was evaluated by Western blotting and indirect immunofluorescence antibody (IFA) test. In addition, the immunogenic properties of PvAMA-1 were evaluated in BALB/c mice with the purified protein emulsified in Freund’s adjuvant.Results: In the present study, the PvAMA-1 ectodomain was expressed at a high-level (65 mg/L) using a bacterial system. Reduced and non-reduced sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS-PAGE) as well as Western blot analysis confirmed the appropriate conformation and folding of PvAMA-1. The evaluation of immunogenic properties of PvAMA-1 showed that both T helper-1 and 2 cells (Th1 and Th2) responses were present in mice after three immunizations and persisted up to one year after the first immunization. Moreover, the antibodies raised against the recombinant PvAMA-1 in injected mice could recognize the native protein localized on P. vivaxparasites.Conclusion: We demonstrate that our recombinant protein had proper conformation and folding. Also, there were common epitopes in the recombinant forms corresponding to native proteins. These results; therefore, indicate that the expressed PvAMA-1 has the potential to be used as a vivax MALARIA VACCINE.

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APA: Copy

SALAVATIFAR, MARYAM, ZAKERI, SEDIGHEH, HAYATI ROODBARI, NASIM, & DINPARAST DJADID, NAVID. (2015). HIGH-LEVEL EXPRESSION, PURIFICATION AND CHARACTERIZATION OF A RECOMBINANTPLASMODIUM VIVAX APICAL MEMBRANE ANTIGEN 1: IMPLICATION FOR VIVAX MALARIA VACCINE DEVELOPMENT. CELL JOURNAL (YAKHTEH), 17(3 (67)), 520-531. SID. https://sid.ir/paper/670998/en

Vancouver: Copy

SALAVATIFAR MARYAM, ZAKERI SEDIGHEH, HAYATI ROODBARI NASIM, DINPARAST DJADID NAVID. HIGH-LEVEL EXPRESSION, PURIFICATION AND CHARACTERIZATION OF A RECOMBINANTPLASMODIUM VIVAX APICAL MEMBRANE ANTIGEN 1: IMPLICATION FOR VIVAX MALARIA VACCINE DEVELOPMENT. CELL JOURNAL (YAKHTEH)[Internet]. 2015;17(3 (67)):520-531. Available from: https://sid.ir/paper/670998/en

IEEE: Copy

MARYAM SALAVATIFAR, SEDIGHEH ZAKERI, NASIM HAYATI ROODBARI, and NAVID DINPARAST DJADID, “HIGH-LEVEL EXPRESSION, PURIFICATION AND CHARACTERIZATION OF A RECOMBINANTPLASMODIUM VIVAX APICAL MEMBRANE ANTIGEN 1: IMPLICATION FOR VIVAX MALARIA VACCINE DEVELOPMENT,” CELL JOURNAL (YAKHTEH), vol. 17, no. 3 (67), pp. 520–531, 2015, [Online]. Available: https://sid.ir/paper/670998/en

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