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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

Online
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1437-4315
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Volume 393, Issue 8

Issues

Structural determinants of the eosinophil cationic protein antimicrobial activity

Ester Boix
  • Corresponding author
  • Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, E-08193 Cerdanyola del Vallès, Spain
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  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Vivian A. Salazar
  • Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, E-08193 Cerdanyola del Vallès, Spain
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Marc Torrent
  • Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, E-08193 Cerdanyola del Vallès, Spain
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ David Pulido
  • Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, E-08193 Cerdanyola del Vallès, Spain
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ M. Victòria Nogués
  • Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, E-08193 Cerdanyola del Vallès, Spain
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Mohammed Moussaoui
  • Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, E-08193 Cerdanyola del Vallès, Spain
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar

Abstract

Antimicrobial RNases are small cationic proteins belonging to the vertebrate RNase A superfamily and endowed with a wide range of antipathogen activities. Vertebrate RNases, while sharing the active site architecture, are found to display a variety of noncatalytical biological properties, providing an excellent example of multitask proteins. The antibacterial activity of distant related RNases suggested that the family evolved from an ancestral host-defence function. The review provides a structural insight into antimicrobial RNases, taking as a reference the human RNase 3, also named eosinophil cationic protein (ECP). A particular high binding affinity against bacterial wall structures mediates the protein action. In particular, the interaction with the lipopolysaccharides at the Gram-negative outer membrane correlates with the protein antimicrobial and specific cell agglutinating activity. Although a direct mechanical action at the bacteria wall seems to be sufficient to trigger bacterial death, a potential intracellular target cannot be discarded. Indeed, the cationic clusters at the protein surface may serve both to interact with nucleic acids and cell surface heterosaccharides. Sequence determinants for ECP activity were screened by prediction tools, proteolysis and peptide synthesis. Docking results are complementing the structural analysis to delineate the protein anchoring sites for anionic targets of biological significance.

This article offers supplementary material which is provided at the end of the article.

Keywords: bactericidal; glycosaminoglycans; host defence; innate immunity; nucleotides; RNase

About the article

Ester Boix

Ester Boix graduated in Biological Sciences in 1986 at the Universitat de Barcelona and in 1994 obtained her PhD in Biochemistry at the Universitat Autònoma de Barcelona (UAB). During a first postdoctoral stage at the National Institutes of Health, Bethesda, that she enrolled on cytotoxic RNases and following that she enrolled in the Structural Biology Group at the University of Bath. In 2001 she moved to the Biochemistry and Molecular Biology Dpt., UAB, first as a lecturer, then as a “Ramón y Cajal” research fellow and since 2004 as an Associate Professor. Her current research project focuses on the antipathogen mechanism of action of human RNases involved in host defense.

Vivian A. Salazar

Vivian Salazar obtained her BSc in Bacteriology from Pontificia Universidad Javeriana (Colombia) in 2002, and MSc in Biological Sciences at Andes University (Colombia) in 2008. She then moved to Universitat Autònoma de Barcelona where she obtained her MSc in Biochemistry, Molecular Biology and Biomedicine in 2011. Currently she is a PhD student working on the structure–function characterization of human ribonucleases.

Marc Torrent

Marc Torrent obtained his PhD in Biochemistry at the Universitat Autònoma de Barcelona in 2009. From 2009 to 2011, he worked as a postdoctoral fellow at the Universitat Pompeu Fabra and currently he is a Career Development Fellow at the Laboratory of Molecular Biology at Cambridge, UK. His main research interests include the study of the structural activity relationships on antimicrobial proteins and peptides and how evolution has shaped their sequence to develop and improve their antimicrobial activity.

David Pulido

David Pulido graduated in Microbiology at the Universitat Autònoma de Barcelona (UAB) in 2009. One year later he obtained a MSc in Biochemistry and Molecular Biology at the same university. Currently he is a PhD student. His work in the Biochemistry department of UAB is centered on the study of human RNases structure, their antimicrobial mechanism of action and role in the host immune system.

M. Victòria Nogués

M. Victòria Nogués (1954, Barcelona, Spain) graduated in Biological Sciences and obtained her PhD in Biological Sciences in 1982 at Universitat Autònoma de Barcelona (Spain). Presently she is Full Professor at the Department of Biochemistry and Molecular Biology at the Faculty of Biosciences of the Universitat Autònoma de Barcelona. Her main scientific interests have been focused in the field of the proteins of the ribonuclease A family. Her contributions include kinetics and structural studies directed to analyze catalytic mechanism and the contribution of non-catalytic binding sites in the cleavage of polymeric substrates and the structural bases and mechanisms associated to the biological functions of ribonucleases, especially the cytotoxicity directed to bacteria and eukaryotic cells.

Mohammed Moussaoui

Mohammed Moussaoui received his PhD in Biochemistry and Molecular Biology in 1998 at the Universitat Autònoma de Barcelona (UAB), Spain. Since 1999, he works at the Biochemistry and Molecular Biology Department (UAB) as a Researcher and Lecturer. His main research interests are in the catalytic and antipathogen mechanism of ribonucleases.


Corresponding author


Received: 2012-03-20

Accepted: 2012-04-17

Published in Print: 2012-08-01


Citation Information: , Volume 393, Issue 8, Pages 801–815, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2012-0160.

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[1]
Guillem Prats-Ejarque, Jose A. Blanco, Vivian A. Salazar, Victòria M. Nogués, Mohammed Moussaoui, and Ester Boix
Biochimica et Biophysica Acta (BBA) - General Subjects, 2018
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David Pulido, Marc Torrent, David Andreu, M. Victoria Nogués, and Ester Boix
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David Pulido, Guillem Prats-Ejarque, Clara Villalba, Marcel Albacar, Juan J. González-López, Marc Torrent, Mohammed Moussaoui, and Ester Boix
Antimicrobial Agents and Chemotherapy, 2016, Volume 60, Number 10, Page 6313
[4]
Lu Lu, Jiarui Li, Mohammed Moussaoui, and Ester Boix
Frontiers in Immunology, 2018, Volume 9
[5]
David Pulido, Guillem Prats-Ejarque, Clara Villalba, Marcel Albacar, Mohammed Moussaoui, David Andreu, Rudolf Volkmer, Marc Torrent, and Ester Boix
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[6]
Chitra Narayanan, David N. Bernard, Khushboo Bafna, Donald Gagné, Chakra S. Chennubhotla, Nicolas Doucet, and Pratul K. Agarwal
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[8]
Javier Arranz-Trullén, Lu Lu, David Pulido, Sanjib Bhakta, and Ester Boix
Frontiers in Immunology, 2017, Volume 8
[9]
K. Ravi Acharya and Steven J. Ackerman
Journal of Biological Chemistry, 2014, Volume 289, Number 25, Page 17406
[10]
Jumin Xie, Zhen Chen, Xueyan Zhang, Honghe Chen, and Wuxiang Guan
Scientific Reports, 2017, Volume 7, Page 45207
[11]
Nicolò Baranzini, Edoardo Pedrini, Rossana Girardello, Gianluca Tettamanti, Magda de Eguileor, Roberto Taramelli, Francesco Acquati, and Annalisa Grimaldi
Cell and Tissue Research, 2017, Volume 368, Number 2, Page 337
[12]
Marc Torrent, David Pulido, M. Victòria Nogués, Ester Boix, and H. Steven Seifert
PLoS Pathogens, 2012, Volume 8, Number 11, Page e1003005
[13]
David Pulido, Maria Flor Garcia-Mayoral, Mohammed Moussaoui, Diego Velázquez, Marc Torrent, Marta Bruix, and Ester Boix
The FEBS Journal, 2016, Volume 283, Number 22, Page 4176
[14]
Patrick Koczera, Lukas Martin, Gernot Marx, and Tobias Schuerholz
International Journal of Molecular Sciences, 2016, Volume 17, Number 8, Page 1278
[15]
Vivian A. Salazar, Javier Arranz-Trullén, Susanna Navarro, Jose A. Blanco, Daniel Sánchez, Mohammed Moussaoui, and Ester Boix
MicrobiologyOpen, 2016, Volume 5, Number 5, Page 830
[16]
David Pulido, Javier Arranz-Trullén, Guillem Prats-Ejarque, Diego Velázquez, Marc Torrent, Mohammed Moussaoui, and Ester Boix
International Journal of Molecular Sciences, 2016, Volume 17, Number 4, Page 552
[17]
M. Flor García-Mayoral, Ángeles Canales, Dolores Díaz, Javier López-Prados, Mohammed Moussaoui, José L. de Paz, Jesús Angulo, Pedro M. Nieto, Jesús Jiménez-Barbero, Ester Boix, and Marta Bruix
ACS Chemical Biology, 2013, Volume 8, Number 1, Page 144
[18]
Vivian A. Salazar, Jenny Rubin, Mohammed Moussaoui, David Pulido, Maria Victòria Nogués, Per Venge, and Ester Boix
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[19]
Guangshun Wang
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[20]
Avinash Padhi, Mitali Sengupta, Srabasti Sengupta, Klaus H. Roehm, and Avinash Sonawane
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[21]
Marc Torrent, David Pulido, Javier Valle, M. Victòria Nogués, David Andreu, and Ester Boix
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[22]
David Pulido, Mohammed Moussaoui, M. Victòria Nogués, Marc Torrent, and Ester Boix
FEBS Journal, 2013, Volume 280, Number 22, Page 5841
[23]
Ester Boix, Jose A. Blanco, M. Victòria Nogués, and Mohammed Moussaoui
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