Membrane Perforation by the Pore-Forming Toxin Pneumolysin
نویسندگان
چکیده
منابع مشابه
Two Structural Transitions in Membrane Pore Formation by Pneumolysin, the Pore-Forming Toxin of Streptococcus pneumoniae
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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The bacterial toxin pneumolysin is released as a soluble monomer that kills target cells by assembling into large oligomeric rings and forming pores in cholesterol-containing membranes. Using cryo-EM and image processing, we have determined the structures of membrane-surface bound (prepore) and inserted-pore oligomer forms, providing a direct observation of the conformational transition into th...
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Introduction: Chemotherapy has been restricted due to the high-dose side effects. In the present study, acceleration of the chemotherapeutic drug (5FU) entrance into MCF-7 cells has been explored by using a recombinant form of Fragaceatoxin C (FraC) pore-forming toxin. Methods: In this experimental study, the gene for FraC toxin was order from a commercial source and was sub-cloned into pET28a...
متن کاملThe pore-forming toxin proaerolysin is activated by furin.
Aerolysin is secreted as an inactive dimeric precursor by the bacterium Aeromonas hydrophila. Proteolytic cleavage within a mobile loop near the C terminus of the protoxin is required for oligomerization and channel formation. This loop contains the sequence KVRRAR432, which should be recognized by mammalian proprotein convertases such as furin, PACE4, and PC5/6A. Here we show that these three ...
متن کاملStructural analysis of the protein/lipid complexes associated with pore formation by the bacterial toxin pneumolysin.
Pneumolysin, a major virulence factor of the human pathogen Streptococcus pneumoniae, is a soluble protein that disrupts cholesterol-containing membranes of cells by forming ring-shaped oligomers. Magic angle spinning and wideline static (31)P NMR have been used in combination with freeze-fracture electron microscopy to investigate the effect of pneumolysin on fully hydrated model membranes con...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2020
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2019.11.1397