The strain-transcendent receptor CD55 plays a distinct functional role relative to other known receptors for Plasmodium falciparum invasion of human erythrocytes, indicating it may present a vulnerable target for intervention.

Interaction of P. falciparum with the erythrocyte activates a phosphorylation cascade altering the viscoelastic properties of this area of the host membrane conditioning it for successful invasion.

A numerical model of malaria parasite adhesion to an erythrocyte shows that the original egg-like shape of merozoites is more robust than other shapes in negotiating various physiological conditions during the alignment process upon erythrocyte invasion.

A systemic proteome of the pellicle organelle inner membrane complex (IMC) provides new insight for the intraerythrocytic proliferation of malaria parasite and identifies the palmitoyl-acyl-transferase DHHC2 as a key enzyme regulating the localization of IMC proteins through palmitoylation.

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 bond-based adhesion model is a key step toward a realistic description of RBC-parasite interaction, which allows the investigation of more realistic scenarios and is relevant for other biological systems.

The structure of the promising malaria blood-stage vaccine candidate antigen PfCyRPA and the characterization of a protective epitope are facilitating research on its essential role in parasite invasion, and will guide future epitope-focused vaccine design.

Genetic analysis identifies an enzyme of the malaria parasite that is required to seal its host red blood cell membrane upon invasion, a key requirement of this important intracellular pathogen.

The rhoptry protein RhopH3 is crucial for the invasion and growth of the malaria parasite and disruption of it provides insight into the binding of the parasite to the host red blood cell and into the formation of new import pathways.

Gene knockdowns reveal that the conserved RhopH protein complex functions in both host cell invasion and channel-mediated nutrient uptake in malaria.