Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/201101
Type: Artigo de periódico
Title: Peptides Derived From Phage Display Libraries As Potential Neutralizers Of Shiga Toxin-induced Cytotoxicity In Vitro And In Vivo.
Author: Bernedo-Navarro, R A
Miyachiro, M M
da Silva, M J
Reis, C F
Conceição, R A
Gatti, M S V
Yano, T
Abstract: To use the phage display technique to develop peptides with the capability to neutralize the cytotoxicity induced by Stx1 and Stx2 toxins produced by Shiga toxin-producing Escherichia coli (STEC). The phage display technique permitted the development of three peptides, named PC7-12, P12-26 and PC7-30, which bind to the globotriaosylceramide (Gb3) receptor for Shiga toxins produced by STEC. Moreover, these peptides were capable of competing efficiently with the Shiga toxins for binding to Gb3. The peptides described herein partially inhibited the Stx-induced cytotoxicity of cell-free filtrates of STEC O157 : H7 and purified Stx toxins in Vero cells. The inhibition of lethality induced by Stx toxins in mice indicated that peptide PC7-30 inhibited the lethality caused by Stx1 (2LD50) in mice. The phage display technique permitted the development of peptides that inhibited the cytotoxicity induced by Stx toxins in vitro. Peptide PC7-30 inhibited the lethality of Stx1 in vivo; this molecule would be a promising candidate for the development of therapeutic agents for STEC-related diseases in humans. The selection of Gb3, the common receptor for Stx1 and Stx2, may contribute to the development of efficient neutralizers for both toxins, and our approach would be an interesting alternative for the development of therapeutic molecules for the treatment of diseases caused by STEC strains.
Subject: Animals
Cercopithecus Aethiops
Humans
Mice
Peptide Library
Peptides
Shiga Toxin 1
Shiga Toxin 2
Shiga-toxigenic Escherichia Coli
Trihexosylceramides
Vero Cells
Ehec (enterohaemorrhagic E. coli)
Bacteriophages
Intestinal Microbiology
Peptides
Toxins
Rights: fechado
Identifier DOI: 10.1111/jam.12451
Address: http://www.ncbi.nlm.nih.gov/pubmed/24447276
Date Issue: 2014
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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