The dominant targets of host immune response to malaria are repeat elements, which are short stretches of amino acids repeated within Plasmodium falciparum proteins, and these are associated with short-lived and exposure-dependent antibody responses.

Plasmodium falciparum aminopeptidase PfA-M17 is essential to parasite survival and plays a role in hemoglobin digestion, providing a rationale for further development of inhibitors against this enzyme.

Plasmodium falciparum kelch13 mutations that cause artemisinin resistant malaria in Southeast Asia show markedly different patterns of evolutionary selection in Africa.

Controlled human malaria infection model allows the study of gametocyte biology and dynamics providing novel insights and tools in malaria transmission and elimination efforts.

The de novo selection of a mutation responsible for Plasmodium falciparum in vitro artemisinin resistance is confirmed in Guyana, making artemisinin combination therapies vulnerable to complete resistance in this region.

Multi-omic analyses reveal that the chromatin-associated microrchidia protein, MORC (PF3D7_1468100), at the blood stage of the human malaria parasite, Plasmodium falciparum, interacts with a range of nuclear proteins.

Parasite variants associated with severe malaria do not have an intrinsic growth or survival advantage in vivo, which indicates that a change in host environment is required for their selection.

An enhanced bioinformatic pipeline to quantify Plasmodium falciparum core gene and polymorphic var gene expression revealed changes occurring during early culture adaptation of parasites from naturally infected individuals.

Ribosome profiling has bridged the knowledge gap between transcription and translation during malaria blood stage development and provided a comprehensive gene expression resource for this parasite.

The molecular mechanism behind how emetine inhibits the ribosome of the human malaria parasite, along with structural details of the complex formed, is revealed at high resolution using cryo-electron microscopy.