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High Yield Purification of Plasmodium falciparum Merozoites For Use in Opsonizing Antibody Assays
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High Yield Purification of Plasmodium falciparum Merozoites For Use in Opsonizing Antibody Assays

Published on: July 17, 2014

Characterization of a protective Escherichia coli-expressed Plasmodium falciparum merozoite surface protein 3

Chiawei W Tsai1, Peter F Duggan, Albert J Jin

  • 1Malaria Vaccine Development Branch, National Institute of Allergy and Infectious Disease, National Institutes of Health, Rockville, MD 20852, United States.

Molecular and Biochemical Parasitology
|December 17, 2008
PubMed

Insights

Developing a scalable malaria vaccine candidate, recombinant Plasmodium falciparum merozoite surface protein 3 (MSP3) expressed in E. coli induced protective antibodies in monkeys against virulent malaria challenge.

Area of Science:

  • Malariology
  • Vaccine Development
  • Protein Expression and Characterization

Background:

  • Recombinant yeast-expressed Plasmodium falciparum merozoite surface protein 3 (MSP3) showed protection in monkeys but was not suitable for human trials due to production limitations.
  • A scalable production method for MSP3 is crucial for developing a viable malaria vaccine.

Purpose of the Study:

  • To express and purify a near-full-length MSP3 protein in Escherichia coli (EcMSP3) for potential use in malaria vaccines.
  • To characterize the structure of EcMSP3 and evaluate its immunogenicity and efficacy in a non-human primate model.

Main Methods:

  • Near-full-length MSP3 was expressed and purified from Escherichia coli.
  • EcMSP3 structure was analyzed using analytical size-exclusion HPLC, multi-angle light scatter, quasi-elastic light scatter detection, velocity sedimentation, and atomic force microscopy.
  • Aotus nancymai monkeys were vaccinated with EcMSP3 in Freund's adjuvant and challenged with the FVO strain of P. falciparum.

Main Results:

  • Purified EcMSP3 formed non-globular dimers with asymmetric structures, beaded domains, and flexible loops.
  • Vaccination with EcMSP3 induced antibodies recognizing native MSP3 on parasitized erythrocytes.
  • Monkeys vaccinated with EcMSP3 showed delayed time to treatment and reduced peak parasitemia during challenge infection.

Conclusions:

  • EcMSP3, produced scalably in E. coli, mimics the native MSP3 structure and induces a protective immune response.
  • EcMSP3 is a promising candidate for inclusion in a multi-component malaria vaccine.
  • This study provides a foundation for further development of an E. coli-expressed MSP3-based malaria vaccine.

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