Ribonucleases as a host-defense family: Evidence of evolutionary conserved antimicrobial activity at the N-terminus.

Vertebrate secreted ribonucleases (RNases) are small proteins that play important roles in RNA metabolism, angiogenesis or host defense.
In the present study we describe the antimicrobial properties of the N-terminal domain of the human canonical RNases (hcRNases) and show that its 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 presented here show that, for all antimicrobial hcRNases, (i) activity is retained at the N-terminus; (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 defense 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.

Source: BJ Cell - August 20, 2013 Category: Biochemistry Authors: M Torrent, D Pulido, J Valle, M Nogués, D Andreu, E Boix Tags: BJ Cell Source Type: research