Engineering of a plant-produced virus-like particle to improve the display of the Plasmodium falciparum Pfs25 antigen and transmission-blocking activity of the vaccine candidate

Malaria kills around 409,000 people a year, mostly children under the age of five. Malaria transmission-blocking vaccines work to reduce malaria prevalence in a community and have the potential to be part of a multifaceted approach required to eliminate the parasites causing the disease. Pfs25 is a...

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Bibliographic Details
Published in:Vaccine 2023-01, Vol.41 (4), p.938-944
Main Authors: Tottey, Stephen, Shoji, Yoko, Mark Jones, R., Musiychuk, Konstantin, Chichester, Jessica A., Miura, Kazutoyo, Zhou, Luwen, Lee, Shwu-Maan, Plieskatt, Jordan, Wu, Yimin, Long, Carole A., Streatfield, Stephen J., Yusibov, Vidadi
Format: Article
Language:English
Subjects:
Amino acids
Animals
Antibodies
Antibodies, Protozoan
Antigens
Antigens, Protozoan
Chromatography
Disease transmission
Malaria
Malaria - prevention & control
Malaria Vaccines - genetics
Malaria, Falciparum - prevention & control
Mice
Mosquitoes
Mutation
Parasites
Pfs25
Plant-based vaccine
Plasmodium falciparum
Proteins
Protozoan Proteins
Reengineering
Transmission-blocking vaccine
Vaccines
Vector-borne diseases
Virus-like particle
Virus-like particles
Viruses
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Summary:Malaria kills around 409,000 people a year, mostly children under the age of five. Malaria transmission-blocking vaccines work to reduce malaria prevalence in a community and have the potential to be part of a multifaceted approach required to eliminate the parasites causing the disease. Pfs25 is a leading malaria transmission-blocking antigen and has been successfully produced in a plant expression system as both a subunit vaccine and as a virus-like particle. This study demonstrates an improved version of the virus-like particle antigen display molecule by eliminating known protease sites from the prior A85 variant. This re-engineered molecule, termed B29, displays three times the number of Pfs25 antigens per virus-like particle compared to the original Pfs25 virus-like particle. An improved purification scheme was also developed, resulting in a substantially higher yield and improved purity. The molecule was evaluated in a mouse model and found to induce improved transmission-blocking activity at lower doses and longer durations than the original molecule.
ISSN:0264-410X
1873-2518
DOI:10.1016/j.vaccine.2022.12.048