Disulfide bonds in the ectodomain of anthrax toxin receptor 2 are required for the receptor-bound protective-antigen pore to function

Cell-surface receptors play essential roles in anthrax toxin action by providing the toxin with a high-affinity anchor and self-assembly site on the plasma membrane, mediating the toxin entry into cells through endocytosis, and shifting the pH threshold for prepore-to-pore conversion of anthrax toxi...

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Veröffentlicht in:	PloS one 2010-05, Vol.5 (5), p.e10553-e10553
Hauptverfasser:	Sun, Jianjun, Collier, R John
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analysis Animals Anthrax Antigens Antigens, Bacterial - chemistry Antigens, Bacterial - metabolism Bacterial Toxins - chemistry Bacterial Toxins - metabolism Binding sites Cell Membrane - drug effects Cell Membrane - metabolism Cell surface Chemical bonds CHO Cells Conformation Cricetinae Cricetulus Disulfide bonds Disulfides - metabolism E coli Endocytosis Escherichia coli - metabolism Hydrogen-Ion Concentration - drug effects Immunoglobulins Infectious Diseases/Bacterial Infections Kinases Liposomes Microbiology/Cellular Microbiology and Pathogenesis Microbiology/Immunity to Infections Molecular Sequence Data Oxidation-Reduction - drug effects pH effects Pore formation Potassium - metabolism Protective antigen Protein Binding - drug effects Protein Structure, Quaternary Protein Structure, Tertiary Protein Transport - drug effects Receptor mechanisms Receptors Receptors, Peptide - chemistry Receptors, Peptide - metabolism Recombinant Proteins - isolation & purification Reducing Agents - pharmacology Reduction Self-assembly Sodium Dodecyl Sulfate - pharmacology Toxins Translocation Von Willebrand factor
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