When I first encountered the paper by Weiner et al. in 2011 (1), I was struck not just by the data, but by the questions it raised. Their use of focused ion beam scanning electron microscopy (FIB-SEM) to generate high-resolution 3D reconstructions of nuclear pore organization across the intraerythrocytic cycle of Plasmodium falciparum offered a tantalizing glimpse into the nuclear envelope (NE) of a parasite that replicates unlike any model eukaryote (2). The idea that this structure—a defining feature of eukaryotic cells—could remain intact throughout mitosis, while still accommodating spindle formation, organelle inheritance, and gene regulation, challenged my assumptions about cell division.

Researchers at the Francis Crick Institute have shown that the Cryptosporidium parasite exports a protein into infected intestinal cells, altering the gut environment and enabling the parasite to surv...

Blood-stage Plasmodium falciparum parasites rely on a non-photosynthetic plastid, the apicoplast, for survival, making it an attractive target for antimalarial intervention. Like the mitochondrion, th...

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Nearly 150 years ago, scientists began to imagine how information might flow through the brain based on the shapes of neurons they had seen under the microscopes of the time. With today’s imaging tech...

Single-celled apicomplexan parasites have to grow, replicate, and divide all of the organelles of a eukaryotic cell all while being a tiny fraction of the size of most other eukaryotes. For example, a...

Cryptosporidium is a common intestinal infection of vertebrates and a significant threat to public health. Within the epithelial layer of the intestine, the parasite invades and replicates. Infected cells are readily detected under the microscope by the presence of elongated microvilli, particularly around the vacuole where the parasite resides. Here, we identify a family of Cryptosporidium virulence factors that are exported into the host cell during infection and localise to the microvilli. We examine the trafficking and function of the most highly expressed family member, MVP1, which appears to control the elongation of microvilli through engagement of host EBP50 and CDC42. Remarkably, this mechanism closely mirrors that of an enteropathogenic Escherichia coli virulence factor, MAP, which is also known to drive host microvilli elongation during infection. This highlights a unique instance where eukaryotic and prokaryotic virulence factors have convergently evolved to modulate host actin structures through a similar mechanism. ### Competing Interest Statement The authors have declared no competing interest.

Functional characterization of PfFBXO1, utilizing cell biology, genetics, and biochemistry, demonstrates essential roles for this protein in formation of the inner membrane complex in asexual merozoit...