Production of the 42-kDa fragment of Plasmodium falciparum merozoite surface protein 1, a leading malaria vaccine antigen, in Arabidopsis thaliana seeds

Lau, On Sun, Ng, Danny W.-K., Chan, Wendy W. L., Chang, Sandra P. and Sun, Samuel S. M. (2010) Production of the 42-kDa fragment of Plasmodium falciparum merozoite surface protein 1, a leading malaria vaccine antigen, in Arabidopsis thaliana seeds. Plant Biotechnology Journal, 8 9: 994-1004. doi:10.1111/j.1467-7652.2010.00526.x


Author Lau, On Sun
Ng, Danny W.-K.
Chan, Wendy W. L.
Chang, Sandra P.
Sun, Samuel S. M.
Title Production of the 42-kDa fragment of Plasmodium falciparum merozoite surface protein 1, a leading malaria vaccine antigen, in Arabidopsis thaliana seeds
Formatted title
Production of the 42-kDa fragment of Plasmodium falciparum merozoite surface protein 1, a leading malaria vaccine antigen, in Arabidopsis thaliana seeds
Journal name Plant Biotechnology Journal   Check publisher's open access policy
ISSN 1467-7644
1467-7652
Publication date 2010
Sub-type Article (original research)
DOI 10.1111/j.1467-7652.2010.00526.x
Open Access Status DOI
Volume 8
Issue 9
Start page 994
End page 1004
Total pages 11
Place of publication Oxford, United Kingdom
Publisher Wiley-Blackwell
Abstract Malaria is widely associated with poverty, and a low-cost vaccine against malaria is highly desirable for implementing comprehensive vaccination programmes in developing countries. Production of malaria antigens in plants is a promising approach, but its development has been hindered by poor expression of the antigens in plant cells. In the present study, we targeted plant seeds as a low-cost vaccine production platform and successfully expressed the Plasmodium falciparum 42-kDa fragment of merozoite surface protein 1 (MSP1 42), a leading malaria vaccine candidate, at a high level in transgenic Arabidopsis seeds. We overcame hurdles of transcript and protein instabilities of MSP1 42 in plants by synthesizing a plant-optimized MSP1 42 cDNA and either targeting the recombinant protein to protein storage vacuoles or fusing it with a stable plant storage protein. An exceptional improvement in MSP1 42 expression, from an undetectable level to 5% of total extractable protein, was achieved with these combined strategies. Importantly, the plant-derived MSP1 42 maintains its natural antigenicity and can be recognized by immune sera from malaria-infected patients. Our results provide a strong basis for the development of a plant-based, low-cost malaria vaccine. © 2010 The Authors. Plant Biotechnology Journal
Keyword Malaria vaccine
Plasmodium falciparum
Seed bioreactor
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Biological Sciences Publications
 
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