Ribonucleases as a host-defence family: Evidence of evolutionarily conserved antimicrobial activity at the N-terminus

Marc Torrent, David Pulido, Javier Valle, M. Victòria Nogués, David Andreu, Ester Boix

Research output: Contribution to journalArticleResearchpeer-review

31 Citations (Scopus)

Abstract

Vertebrate secreted RNases (ribonucleases) are small proteins that play important roles in RNA metabolism, angiogenesis or host defence. In the present study we describe the antimicrobial properties of the N-terminal domain of the hcRNases (human canonical RNases) and show that their antimicrobial activity is well conserved among their lineage. Furthermore, all domains display a similar antimicrobial mechanism, characterized by bacteria agglutination followed by membrane permeabilization. The results of the present study show that, for all antimicrobial hcRNases, (i) activity is retained at the N-terminus and (ii) the antimicrobial mechanism is conserved. Moreover, using computational analysis we show that antimicrobial propensity may be conserved at the N-terminus for all vertebrate RNases, thereby suggesting that a defence mechanism could be a primary function in vertebrate RNases and that the N-terminus was selected to ensure this property. In a broader context, from the overall comparison of the peptides' physicochemical and biological properties, general correlation rules could be drawn to assist in the structure-based development of antimicrobial agents. © 2013 Biochemical Society.
Original languageEnglish
Pages (from-to)99-108
JournalBiochemical Journal
Volume456
DOIs
Publication statusPublished - 15 Nov 2013

Keywords

  • Antimicrobial peptide
  • Drug discovery
  • Evolution
  • Innate immunity
  • Ribonuclease

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