Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition.

Journal article

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 wi...

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Authors: De Colibus, L; Sonnen, A; Morris, K; Siebert, C; Abrusci, P

• Publication status: Published
• Journal: Structure (London, England : 1993)
• Volume: 20
• Issue: 9
• Pages: 1498-1507
• Publication date: 2012-09-01
• DOI: 10.1016/j.str.2012.06.011
• EISSN: 1878-4186
• ISSN: 0969-2126
• Language: English
• Keywords: Amino Acid Sequence; Molecular Sequence Data; Sphingomyelins; Models, Molecular; Phosphorylcholine; Cell Membrane; Protein Multimerization; Humans; Crystallography, X-Ray; Protein Binding; Protein Structure, Secondary; Jurkat Cells; Protein Structure, Quaternary; Cell Membrane Permeability; Evolution, Molecular; Pore Forming Cytotoxic Proteins; Animals; Oligochaeta; Toxins, Biological; Binding Sites