Temporary Membrane Permeabilization via the Pore-Forming Toxin Lysenin
نویسندگان
چکیده
منابع مشابه
Lysenin: a sphingomyelin specific pore-forming toxin.
Sphingomyelin is a major sphingolipid in mammalian cells. Recent results indicate that sphingomyelin is a reservoir of lipid second messengers, ceramide and sphingosine-1-phosphate. Sphingomyelin is also a major component of sphingolipid and cholesterol-rich membrane domains (lipid rafts). Lysenin is a pore-forming toxin that specifically binds sphingomyelin. The binding of lysenin to sphingomy...
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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. We screened for cellular signal transduction inhibitors of low molecular weight from microorganisms and plants. The purpose of the screening was to study the me...
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Clostridium perfringens epsilon toxin (ET) is a potent pore-forming cytotoxin causing fatal enterotoxemia in livestock. ET accumulates in brain and kidney, particularly in the renal distal-collecting ducts. ET binds and oligomerizes in detergent-resistant membranes (DRMs) microdomains and causes cell death. However, the causal linkage between membrane permeabilization and cell death is not clea...
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The human pathogen Streptococcus pneumoniae produces soluble pneumolysin monomers that bind host cell membranes to form ring-shaped, oligomeric pores. We have determined three-dimensional structures of a helical oligomer of pneumolysin and of a membrane-bound ring form by cryo-electron microscopy. Fitting the four domains from the crystal structure of the closely related perfringolysin reveals ...
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Y. Tanaka and M. Yao (Hokkaido Univ.) Pathogenic bacteria express pore-forming toxins (PFTs) to attack host cells. PFTs are expressed as soluble monomeric proteins, which assemble to prepore oligomer on the target cells. After forming prepore, conformational change occurs, and then the pore is formed. Although the crystal structures of monomer and pore have been determined, the detailed mechani...
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ژورنال
عنوان ژورنال: Toxins
سال: 2020
ISSN: 2072-6651
DOI: 10.3390/toxins12050343