Oligomerization and pore formation of a sphingomyelin-specific toxin, lysenin - PubMed (original) (raw)
. 2003 Jun 20;278(25):22762-70.
doi: 10.1074/jbc.M213209200. Epub 2003 Apr 3.
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- PMID: 12676961
- DOI: 10.1074/jbc.M213209200
Free article
Oligomerization and pore formation of a sphingomyelin-specific toxin, lysenin
Akiko Yamaji-Hasegawa et al. J Biol Chem. 2003.
Free article
Abstract
Lysenin is a novel protein derived from coelomic fluid of the earthworm Eisenia foetida, which specifically recognizes sphingomyelin and induces cytolysis. The mechanism underlying lysenin-induced cell lysis has not been clarified. In this report we studied the interaction of lysenin with red blood cells as well as artificial liposomes. Our results showed that lysenin bound membranes and assembled to SDS-resistant oligomers in a sphingomyelin-dependent manner, leading to the formation of pores with a hydrodynamic diameter of approximately 3 nm. Antibody scanning analysis suggested that the C-terminal region of lysenin was exposed, whereas the N-terminal was hidden in the isolated oligomer complex. Differential scanning calorimetry revealed that lysenin interacted with both hydrophilic head group and hydrophobic hydrocarbon tails of sphingomyelin. Oligomerization but not binding was affected by the amide-linked fatty acid composition of sphingomyelin, suggesting the role of membrane fluidity in the oligomerization step.
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