Organisms from all kingdoms produce pore-forming proteins, with the best-characterized
being of bacterial origin. The last decade of research has revealed that the channels formed …

Posttranslational modification is an evolutionarily conserved mechanism for regulating
protein activity, binding affinity, and stability. Compared with established posttranslational …

Immunotoxins (ITs) are protein-based drugs that compose of targeting and cytotoxic
moieties. After binding the IT to the specific cell-surface antigen, the IT internalises into the …

The most potent toxins secreted by pathogenic bacteria contain enzymatic moieties that
must reach the cytosol of target cells to exert their full toxicity. Toxins such as anthrax …

The translocation (T)-domain plays a key role in the action of diphtheria toxin and is
responsible for transferring the catalytic domain across the endosomal membrane into the …

Tetanus and botulinum neurotoxins are di‐chain proteins that cause paralysis by inhibiting
neuroexocytosis. These neurotoxins enter into nerve terminals via endocytosis inside …

Fluorescence spectroscopy provides numerous methodological tools for structural and
functional studies of biological macromolecules and their complexes. All fluorescence …

Abstract pH-induced conformational switching is essential for functioning of diphtheria toxin,
which undergoes a membrane insertion/translocation transition triggered by endosomal …

Fluorescence techniques have become powerful and widely used tools for studies of
biochemical and biophysical processes occurring in biological membranes. Various …

Protonation of key histidine residues has been long implicated in the acid-mediated cellular
action of the diphtheria toxin translocation (T-) domain, responsible for the delivery of the …