Michael E. D'Angelo

TL;DR: In this article, the X-ray crystal structure of perforin pore formation was determined using a cryo-electron microscopy reconstruction, which revealed remarkable flexibility in the mechanism of action and provided new insights into how related immune defence molecules such as complement proteins assemble into pores.

TL;DR: It is concluded that CatH can act as an additional proGrB convertase and that other protease/s must also possess convertase activity, which indicates a great deal of functional redundancy in GrB maturation, which would prevent pathogen-mediated immune suppression by via convertase inhibition.

TL;DR: Comparisons of these many-to-one homologs of human perforin show that they mainly arose from lineage-specific gene duplications in multiple taxa, suggesting acquisition of new roles or different modes of regulation.

TL;DR: It is demonstrated that perforin preferentially delivers cationic molecules while anionic and neutral cargoes are delivered inefficiently, the first report of charge-based discrimination by the perfor in pore.

TL;DR: A pre-pore locked SLO mutant binds reversibly to lipid, suggesting that the partially complete wtSLO forms observed by AFM are anchored to the membrane, and shows the signature of SLO in QCM-D changes when pore formation is inhibited, and that bound and inserted SLO forms can be distinguished.