Determinants of pH-Dependent Modulation of Translocation in Dermonecrotic G-Protein-Deamidating ToxinsReportar como inadecuado




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Department of Microbiology, School of Molecular and Cell Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA





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Abstract Cytotoxic necrotizing factors from E. coli CNF1, CNF2 and Yersinia CNFy share N-terminal sequence similarity with Pasteurella multocida toxin PMT. This common N-terminal region harbors the receptor-binding and translocation domains that mediate uptake and delivery of the C-terminal catalytic cargo domains into the host cytosol. Subtle variations in the N-terminal ~500 amino acids of CNFs and PMT could allow for selective recognition of cellular receptors and thus, selective target cell specificity. Through studies with cellular inhibitors, we have identified an additional novel function for this region in modulating responses of these toxin proteins to changes in pH during intoxication and delivery of the catalytic cargo domain into the cytosol. View Full-Text

Keywords: cytotoxic necrotizing factor; Pasteurella multocida toxin; dermonecrotic toxin; endosomal acidification; intoxication; drug-delivery; toxin-based therapeutics cytotoxic necrotizing factor; Pasteurella multocida toxin; dermonecrotic toxin; endosomal acidification; intoxication; drug-delivery; toxin-based therapeutics





Autor: Tana L. Repella, Mengfei Ho and Brenda A. Wilson *

Fuente: http://mdpi.com/



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