Cited by 9Antimicrobial Peptides and ActivitiesAntimicrobial agents and applicationsInvertebrate Immune Response Mechanisms

Antimicrobial Activity of Cathelicidin-Derived Peptide from the Iberian Mole Talpa occidentalis

Open access
Otazo-Pérez, Andrea, Asensio-Calavia, Patricia, González-Acosta, Sergio, Baca-González, Victoria, López, Manuel R., Morales-delaNuez, Antonio, Pérez de la Lastra, José Manuel·2022·Vaccines

Abstract

The immune systems of all vertebrates contain cathelicidins, a family of antimicrobial peptides. Cathelicidins are a type of innate immune effector that have a number of biological functions, including a well-known direct antibacterial action and immunomodulatory function. In search of new templates for antimicrobial peptide discovery, we have identified and characterized the cathelicidin of the small mammal Talpa occidentalis. We describe the heterogeneity of cathelicidin in the order Eulipotyphla in relation to the Iberian mole and predict its antibacterial activity using bioinformatics tools. In an effort to correlate these findings, we derived the putative active peptide and performed in vitro hemolysis and antimicrobial activity assays, confirming that Iberian mole cathelicidins are antimicrobial. Our results showed that the Iberian mole putative peptide, named To-KL37 (KLFGKVGNLLQKGWQKIKNIGRRIKDFFRNIRPMQEA) has antibacterial and antifungal activity. Understanding the antimicrobial defense of insectivores may help scientists prevent the spread of pathogens to humans. We hope that this study can also provide new, effective antibacterial peptides for future drug development.

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Crossref · 10.3390/vaccines10071105

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  • Cathelicidins and defensins are a family of antimicrobial peptides that show a wide spectrum of antimicrobial activity against bacteria, enveloped viruses, and fungi.

    “Cathelicidins and defensins are a family of antimicrobial peptides that show a wide spectrum of antimicrobial activity against bacteria, enveloped viruses, and fungi [176].”

    From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [176]

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Research works printed but not linked: 1

  1. [13]Souvorov A. Kapustin Y. Kiryutin B. Chetvernin V. Tatusova T. Lipman D. Gnomon–NCBI eukaryotic gene prediction tool Natl. Cent. Biotechnol. Inf. 2010 1 24 Available online: https://www.ncbi.nlm.nih.gov/genome/annotation_euk/gnomon (accessed on 9 May 2022)

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Authors
Otazo-Pérez, A., Asensio-Calavia, P., González-Acosta, S., Baca-González, V., López, M. R., Morales-delaNuez, A., & Pérez de la Lastra, J. M.
Affiliations
  • Biotechnology of Macromolecules Research Group, Instituto de Productos Naturales y Agrobiología (IPNA-CSIC), Avda. Astrofísico Francisco Sánchez, 3, 38206 San Cristóbal de la Laguna, Spain
  • Consejo Superior de Investigaciones Científicas (ES)
Venue
Vaccines
Publisher
MDPI AG
Published
2022-07-10
Volume
10
Issue
7
Pages
1105
ISSN
2076-393X (ISSN-L)
OpenAlex
W4285007986
Cited by
9
References
59
Citations by year
2025: 1 · 2024: 5 · 2022: 2
FWCI
1.25
Type
journal article
Language
en
Open access
Locations
  • Vaccines (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Acceda (Universidad de Las Palmas de Gran Canaria) (submittedVersion)
  • DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Agencia Canaria de Investigación, Innovación y Sociedad de la Información (ACIISI) del Gobierno de Canarias (ProID2020010134, 2019SP43)
  • Fundación Cajacanarias (ProID2020010134, 2019SP43)
Topics
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
  • Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
Keywords
cathelicidin, antimicrobial peptides, Talpa occidentalis, antibacterial activity, antifungal activity, innate immunity, Eulipotyphla, insectivores, hemolysis, peptide design

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