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Insights into the Antimicrobial Mechanism of Action of Human RNase6 : Structural Determinants for Bacterial Cell Agglutination and Membrane Permeation
Pulido Gomez, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Arranz Trullén, Javier (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Prats, Guillem, 1942- (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Velázquez, Diego (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Torrent Burgas, Marc (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Moussaoui, Mohammed (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)
Boix i Borràs, Esther (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular)

Date: 2016
Abstract: Human Ribonuclease 6 is a secreted protein belonging to the ribonuclease A (RNaseA) superfamily, a vertebrate specific family suggested to arise with an ancestral host defense role. Tissue distribution analysis revealed its expression in innate cell types, showing abundance in monocytes and neutrophils. Recent evidence of induction of the protein expression by bacterial infection suggested an antipathogen function in vivo. In our laboratory, the antimicrobial properties of the protein have been evaluated against Gram-negative and Gram-positive species and its mechanism of action was characterized using a membrane model. Interestingly, our results indicate that RNase6, as previously reported for RNase3, is able to specifically agglutinate Gram-negative bacteria as a main trait of its antimicrobial activity. Moreover, a side by side comparative analysis with the RN6(1–45) derived peptide highlights that the antimicrobial activity is mostly retained at the protein N-terminus. Further work by site directed mutagenesis and structural analysis has identified two residues involved in the protein antimicrobial action (Trp1 and Ile13) that are essential for the cell agglutination properties. This is the first structure-functional characterization of RNase6 antimicrobial properties, supporting its contribution to the infection focus clearance.
Rights: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. Creative Commons
Language: Anglès.
Document: article ; recerca ; publishedVersion
Subject: RNases ; Host defence ; Antimicrobial peptides ; Cell agglutination ; Infectious diseases
Published in: International Journal of Molecular Sciences, Vol. 17 Núm. 4 (april 2016) , ISSN 1422-0067

DOI: 10.3390/ijms17040552
PMID: 27089320


19 p, 3.6 MB

The record appears in these collections:
Articles > Research articles
Articles > Published articles

 Record created 2016-11-11, last modified 2019-02-04



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