One-step design of a stable variant of the malaria invasion protein RH5 for use as a vaccine immunogen.

ABSTRACT: Many promising vaccine candidates from pathogenic viruses, bacteria, and parasites are unstable and cannot be produced cheaply for clinical use. For instance, Plasmodium falciparum reticulocyte-binding protein homolog 5 (PfRH5) is essential for erythrocyte invasion, is highly conserved among field isolates, and elicits antibodies that neutralize in vitro and protect in an animal model, making it a leading malaria vaccine candidate. However, functional RH5 is only expressible in eukaryotic systems and exhibits moderate temperature tolerance, limiting its usefulness in hot and low-income countries where malaria prevails. Current approaches to immunogen stabilization involve iterative application of rational or semirational design, random mutagenesis, and biochemical characterization. Typical

SUBMITTER: Campeotto I 

PROVIDER: S-EPMC5293100 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature