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REVIEW article

Front. Drug Discov.
Sec. Anti-Infective Agents
Volume 4 - 2024 | doi: 10.3389/fddsv.2024.1458057

Cathelicidins -a rich seam of antimicrobial peptides waiting for exploitation

Provisionally accepted
Alessandro Tossi Alessandro Tossi 1*Marco Gerdol Marco Gerdol 1Andrea Caporale Andrea Caporale 2,3Sabrina Pacor Sabrina Pacor 1Mario Mardirossian Mario Mardirossian 1Marco Scocchi Marco Scocchi 1Dennis M. Prickett Dennis M. Prickett 1Giorgio Manzini Giorgio Manzini 1Renato Gennaro Renato Gennaro 1
  • 1 Department of Life Sciences, University of Trieste, Trieste, Friuli-Venezia Giulia, Italy
  • 2 Institute of Crystallography, National Research Council (CNR), Bari, Italy
  • 3 University of Naples Federico II, Naples, Campania, Italy

The final, formatted version of the article will be published soon.

    Cathelicidins are a ubiquitous family of host defence antimicrobial peptides in vertebrate animals.Unlike other antimicrobial peptide families, it is defined by a large and relatively well conserved proregion rather than by the mature bioactive peptides themselves, which are highly diverse and conform to at least five different structural types, resulting in distinct modes of action. Cathelicidinderived host defence peptides have a pleiotropic role in immunity, displaying both a direct antimicrobial activity and the ability to boost other host responses to infection and injury. The presence of a relatively well conserved proregion attached to a vast repertoire of structurally and functionally diverse peptides allows mining the increasing number of vertebrate genomes for lead sequences to potentially useful new anti-infective and/or immunomodulatory agents. This should increase the number of cathelicidin-based peptides entering clinical trials, which has been limited to date, despite considerable efforts in the last two decades.

    Keywords: Cathelicidin, CRAMP, LL-37, PrAMP, host defence peptide, antimicrobial peptide, innate immunity, AMP, antimicrobial peptide, CLD, cathelin-like domain, DFU, diabetic foot ulcers, hCAP18, human 18kDa cathelicidin antimicrobial protein, HDP, host defence peptide, LPS, lipopolysaccharide, LTA, lipoteichoic acid, VDRE, vitamin D response element

    Received: 01 Jul 2024; Accepted: 09 Aug 2024.

    Copyright: © 2024 Tossi, Gerdol, Caporale, Pacor, Mardirossian, Scocchi, Prickett, Manzini and Gennaro. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Alessandro Tossi, Department of Life Sciences, University of Trieste, Trieste, 34127, Friuli-Venezia Giulia, Italy

    Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.