August 18th, 2014
Biotech company ExpreS2ion® Biotechnologies announced the publication of the article: ‘Structure of malariainvasion protein RH5 with erythrocyte basigin and blocking antibodies’ in the high impact scientific journal Nature, with teams at the University of Oxford.
The scientists have been working together since the University of Oxford took a license to ExpreS2ions’ Drosophila Schneider-2 cell-based protein production technology platform – ExpreS2.
The RH5 protein is essential for the invasion of human erythrocytes by the parasite that causes the most deadly form of malaria, Plasmodium falciparum. This is an essential stage in the life cycle of the parasite and a target for development of therapeutics to prevent the disease. The data now published reveals the structure of RH5 and shows how it interacts with its binding partner, basigin, from the human erythrocyte. It also demonstrates how antibodies can be used to prevent RH5 from binding to basigin. These findings will allow the development of improved vaccines to prevent malaria.
Dr Wian de Jongh, ExpreS2ion’s CSO, and one of the authors of the Nature paper commented: “We are thrilled that our work with this challenging-to-produce malaria protein is contributing to the advancement of this promising vaccine antigen. The collaboration with the teams at the Jenner Institute and the Department of Biochemistry at the University of Oxford is providing relevant scientific advances to malaria research. This publication in a high impact scientific journal is a recognition of the relevance of the ExpreS2 platform in advancing malaria and vaccine research through enabling the production of difficult and complex proteins, in a GMP-compatible system.”
Dr Simon Draper, Associate Professor at the Jenner Institute and Group Leader for the Blood-Stage Malaria Vaccine Programme commented: “These new data on the structure of the RH5 protein will greatly expedite our ability to develop a highly effective vaccine against this important and critical target within the blood-stage malaria parasite. We can now begin to understand how human antibodies neutralise red blood cell invasion by the malaria parasite and use this information to design improved versions of the vaccine that focus the immune response on the most susceptible regions of the RH5 protein. Our collaboration with ExpreS2ion, and access to the ExpreS2 platform at the Jenner Institute in Oxford, has greatly expanded our capabilities to develop new clinically-relevant protein vaccines against difficult pathogens, such as malaria. We are looking forward to working further with ExpreS2ion Biotechnologies as we progress this important new RH5 malaria target into early-phase clinical trials at Oxford.”
Professor Matthew Higgins’ team at the Department of Biochemistry study interactions between the malaria-causing parasites and their human ligands. He commented: “The RH5 protein from the malaria parasite proved to be very difficult to express in large quantities and we were delighted when ExpreS2ion showed that they could produce enough for the heavy requirements of structural biology. ExpreS2ion were extremely helpful as we transferred the S2 cell system to the lab’ and their system was absolutely necessary for us to solve the RH5:basigin structure.”