Scientists at the Institut Pasteur and McMaster University have discovered that the evolution of a gene in the bacterium that causes bubonic plague, Yersinia pestis, may have prolonged the duration of...

Influenza viruses replicate and transcribe their genome in the context of a conserved ribonucleoprotein (RNP) complex. By integrating cryo–electron microscopy single-particle analysis and cryo–electro...

Toxoplasma gondii evolved two ISWI remodellers, TgSNF2h and TgSNF2L. TgSNF2h forms a complex that insulates active genes, regulates MORC-driven sexual commitment and ensures precise gene expression, s...

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.

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Author summary Malaria caused by Plasmodium falciparum infections remains a major human threat in endemic countries. Its proliferation within the host relies on the iteration of red blood cell invasio...

Iron-sulfur proteins require specialized assembly pathways and play vital roles in cellular functions. This study shows that the plastid-derived protein HCF101 functions in the cytosolic Fe-S assembly...

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