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 first non-invasive technique to assess the action of brain clearance mechanisms, driven by the perivascular inflow of cerebrospinal fluid, has been developed using magnetic resonance imaging.
p27Kip1 directly controls invadopodia turnover by promoting the interaction of PAK1 with Cortactin, which induces Cortactin phosphorylation, invadopodia disassembly and facilitates invasion through extracellular matrix.
An aspartyl protease is essential for the lytic cycle of Toxoplasma gondii and is involved in the maturation of proteins critical for invasion and egress, and it can be targeted selectively with an ethylamine scaffold based peptidomimetic inhibitor.
The crystal structures of the key vaccine candidate CyRPA alone and in complex with antibody Fab fragment was solved and this will be important information for designing a vaccine.
Plasmodium falciparum invasion protein EBA-175, once shed from the parasite surface post invasion, facilitates RBC clustering and enhances parasite growth while simultaneously enabling parasite immune evasion of host neutralizing antibodies.
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.