Marjetka Podobnik

TL;DR: Early steps in NLP cytolysin action that determine plant clade-specific toxin selectivity are unveiled, and it is revealed that NLPs form complexes with terminal monomeric hexose moieties of GIPCs that result in conformational changes within the toxin.

TL;DR: Mutagenic analysis and atomic force microscopy imaging suggest a mechanism for pore assembly for lysenin, which is relevant to the understanding of pore formation by other aerolysin-like pore-forming toxins, which often represent crucial virulence factors in bacteria.

TL;DR: This work reports that the assembly of LLO pores is rapid and efficient irrespective of pH, and indicates significant plasticity of large β-barrel pores, controlled by environmental cues like pH.

TL;DR: The near-atomic structure of PVY’s flexuous virions is determined, revealing a previously unknown lumenal interplay between extended carboxyl-terminal regions of the coat protein units and viral RNA.

TL;DR: This work highlights the advantages and possibilities that this approach offers and shows how it can advance understanding of the pore-forming mechanism and pore properties for one of the most important families of natural toxins, the cholesterol-dependent cytolysins.