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Int. J. Mol. Sci. 2016, 17(4), 552; doi:10.3390/ijms17040552

Insights into the Antimicrobial Mechanism of Action of Human RNase6: Structural Determinants for Bacterial Cell Agglutination and Membrane Permeation

Department of Biochemistry and Molecular Biology, Faculty of Biosciences, Universitat Autònoma de Barcelona, E-08193 Cerdanyola del Vallès, Spain
These authors contributed equally to this work.
Present address: Department of Life Sciences, Imperial College London, South Kensington Campus London, SW7 2AZ London, UK
§
Present address: Microbiology Department, Hospital del Valle Hebron, 08035 Barcelona, Spain
*
Authors to whom correspondence should be addressed.
Academic Editor: Constantinos Stathopoulos
Received: 31 January 2016 / Revised: 18 March 2016 / Accepted: 5 April 2016 / Published: 13 April 2016
(This article belongs to the Special Issue Antimicrobial RNases in Host Defense)
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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. View Full-Text
Keywords: RNases; host defence; antimicrobial peptides; cell agglutination; infectious diseases RNases; host defence; antimicrobial peptides; cell agglutination; infectious diseases
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MDPI and ACS Style

Pulido, D.; Arranz-Trullén, J.; Prats-Ejarque, G.; Velázquez, D.; Torrent, M.; Moussaoui, M.; Boix, E. Insights into the Antimicrobial Mechanism of Action of Human RNase6: Structural Determinants for Bacterial Cell Agglutination and Membrane Permeation. Int. J. Mol. Sci. 2016, 17, 552.

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