Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Pore-forming proteins insert from solution into membranes to create lesions, undergoing a structural rearrangement often accompanied by oligomerization. Lysenin, a pore-forming toxin from the earthworm Eisenia fetida, specifically interacts with sphingomyelin (SM) and may confer innate immunity against parasites by attacking their membranes to form pores. SM has important roles in cell membranes and lysenin is a popular SM-labeling reagent. The structure of lysenin suggests common ancestry with other pore-forming proteins from a diverse set of eukaryotes and prokaryotes. The complex with SM shows the mode of its recognition by a protein in which both the phosphocholine headgroup and one acyl tail are specifically bound. Lipid interaction studies and assays using viable target cells confirm the functional reliance of lysenin on this form of SM recognition.

Original publication

DOI

10.1016/j.str.2012.06.011

Type

Journal article

Journal

Structure

Publication Date

05/09/2012

Volume

20

Pages

1498 - 1507

Keywords

Amino Acid Sequence, Animals, Binding Sites, Cell Membrane, Cell Membrane Permeability, Crystallography, X-Ray, Evolution, Molecular, Humans, Jurkat Cells, Models, Molecular, Molecular Sequence Data, Oligochaeta, Phosphorylcholine, Pore Forming Cytotoxic Proteins, Protein Binding, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Secondary, Sphingomyelins, Toxins, Biological