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A new study sheds light on how the malaria parasite can evade the body's defences whilst retaining the ability to interact with and thrive in its host.

The structure of a complex of the CIDR domain of a PfEMP1 variant (yellow) bound to EPCR (blue). A phenylalanine of the CIDR domain, at the centre of the interface, is shown as pink sticks.
The structure of a complex of the CIDR domain of a PfEMP1 variant (yellow) bound to EPCR (blue). A phenylalanine of the CIDR domain, at the centre of the interface, is shown as pink sticks.

Clinton Lau in Matt Higgins' group, working with groups in Denmark and Tanzania, has characterised a family of variant proteins in the malarial parasite Plasmodium falciparum, believed to be responsible for severe childhood malaria.

By identifying conserved features of the protein family that are required to make the infection so deadly, the group can begin to design therapeutics that might prevent this form of malaria.

Many human infective parasites express surface protein families that are highly variable, avoiding immune detection, but that also have exquisitely conserved molecular features enabling them to maintain the necessary interaction with their host targets.

Read more (Department of Biochemistry website)