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Toxins 2013, 5(6), 1167-1179; doi:10.3390/toxins5061167

Determinants of pH-Dependent Modulation of Translocation in Dermonecrotic G-Protein-Deamidating Toxins

Department of Microbiology, School of Molecular and Cell Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA
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Received: 17 May 2013 / Revised: 28 May 2013 / Accepted: 4 June 2013 / Published: 14 June 2013
(This article belongs to the Special Issue Novel Properties of Well-Characterized Toxins)
View Full-Text   |   Download PDF [647 KB, 19 June 2013; original version 14 June 2013]   |  

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
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Repella, T.L.; Ho, M.; Wilson, B.A. Determinants of pH-Dependent Modulation of Translocation in Dermonecrotic G-Protein-Deamidating Toxins. Toxins 2013, 5, 1167-1179.

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