3F0948 Molecular basis of staphylococcal bi-component pore forming toxin(Membrane Proteins,Oral Presentation)
نویسندگان
چکیده
منابع مشابه
Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins.
Pathogenic bacteria secrete pore-forming toxins (PFTs) to attack target cells. PFTs are expressed as water-soluble monomeric proteins, which oligomerize into nonlytic prepore intermediates on the target cell membrane before forming membrane-spanning pores. Despite a wealth of biochemical data, the lack of high-resolution prepore structural information has hampered understanding of the β-barrel ...
متن کاملPore Formation Mechanism of Staphylococcal Pore- forming Toxin
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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Staphylococcal leucocidins and gamma-hemolysins (leucotoxins) are bi-component toxins that form lytic transmembrane pores. Their cytotoxic activities require the synergistic association of a class S component and a class F component, produced as water-soluble monomers that form hetero-oligomeric membrane-associated complexes. Strains that produce the Panton-Valentine leucocidin are clinically a...
متن کاملStaphylococcal Bicomponent Pore-Forming Toxins: Targets for Prophylaxis and Immunotherapy
Staphylococccus aureus represents one of the most challenging human pathogens as well as a common colonizer of human skin and mucosal surfaces. S. aureus causes a wide range of diseases from skin and soft tissue infection (SSTI) to debilitating and life-threatening conditions such as osteomyelitis, endocarditis, and necrotizing pneumonia. The range of diseases reflects the remarkable diversity ...
متن کاملThe molecular basis for antimicrobial activity of pore-forming cyclic peptides.
The mechanism of action of antimicrobial peptides is, to our knowledge, still poorly understood. To probe the biophysical characteristics that confer activity, we present here a molecular-dynamics and biophysical study of a cyclic antimicrobial peptide and its inactive linear analog. In the simulations, the cyclic peptide caused large perturbations in the bilayer and cooperatively opened a diso...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2012
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.52.s66_3