Lysenin is a pore-forming toxin derived from coelomic fluid of the earthworm Eisenia foetida. The model of lysenin-induced hemolysis includes the specific binding of lysenin to sphingomyelin, oligomerization of the pore proteins, and pore formation. Although the mechanism of lysenin-induced hemolysis is unique, its precise mechanism of action and its inhibitors are poorly understood. In the present study, we screened for inhibitors of lysenin-induced hemolysis by using an optimized screening system and found a methanolic extract of Dalbergia latifolia leaves to be a potential candidate. After isolation and identification, all-E-lutein was identified as the hemolysis inhibitor with an effective dose of 0.025-2.5 ng/mL without any toxicity. The inhibition by all-E-lutein is likely to occur during the receptor binding and/or pore-forming protein oligomerization.
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http://dx.doi.org/10.1055/s-0031-1298538 | DOI Listing |
Membranes (Basel)
May 2021
Biomolecular Sciences Graduate Program, Boise State University, Boise, ID 83725, USA.
The need for alternatives to antibiotics in the fight against infectious diseases has inspired scientists to focus on antivirulence factors instead of the microorganisms themselves. In this respect, prior work indicates that tiny, enclosed bilayer lipid membranes (liposomes) have the potential to compete with cellular targets for toxin binding, hence preventing their biological attack and aiding with their clearance. The effectiveness of liposomes as decoy targets depends on their availability in the host and how rapidly they are cleared from the circulation.
View Article and Find Full Text PDFToxins (Basel)
August 2013
Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Kanagawa 223-8522, Japan.
Lysenin is a pore-forming toxin from the coelomic fluid of earthworm Eisenia foetida. This protein specifically binds to sphingomyelin and induces erythrocyte lysis. Lysenin consists of 297 amino acids with a molecular weight of 41 kDa.
View Article and Find Full Text PDFPlanta Med
June 2012
Faculty of Science and Technology, Keio University, Kanagawa, Japan.
Lysenin is a pore-forming toxin derived from coelomic fluid of the earthworm Eisenia foetida. The model of lysenin-induced hemolysis includes the specific binding of lysenin to sphingomyelin, oligomerization of the pore proteins, and pore formation. Although the mechanism of lysenin-induced hemolysis is unique, its precise mechanism of action and its inhibitors are poorly understood.
View Article and Find Full Text PDFBiochemistry
February 2007
Lipid Biology Laboratory, RIKEN (Institute of Physical and Chemical Research) Discovery Research Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.
Lysenin is a pore-forming toxin that specifically binds sphingomyelin (SM). The binding of the toxin to the membrane is accompanied by the oligomerization of the protein, leading to pore formation. The interaction of lysenin with SM is affected by the presence of other lipids found in the plasma membrane.
View Article and Find Full Text PDFJ Biol Chem
June 2003
Supra-Biomolecular System Research Group, RIKEN (Institute of Physical and Chemical Research) Frontier Research System, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.
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.
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