Aquiluscidin, a Cathelicidin from Crotalus aquilus, and the Vcn-23 Derivative Peptide, Have Anti-Microbial Activity against Gram-Negative and Gram-Positive Bacteria

Author:

Hernández-Arvizu Edwin Esaú12ORCID,Silis-Moreno Teresa Monserrat1,García-Arredondo José Alejandro3,Rodríguez-Torres Angelina45ORCID,Cervantes-Chávez José Antonio4ORCID,Mosqueda Juan15ORCID

Affiliation:

1. Immunology and Vaccine Research Laboratory, Natural Sciences College, Autonomous University of Queretaro, Queretaro 76230, Mexico

2. Ph.D. Program in Natural Sciences, Natural Sciences College, Autonomous University of Queretaro, Queretaro 76230, Mexico

3. Departamento de Investigación Química y Farmacológica de Productos Naturales, Facultad de Química, Universidad Autónoma de Querétaro, Centro Universitario S/N, Queretaro 76010, Mexico

4. Natural Sciences College, Autonomous University of Querétaro, Queretaro 76230, Mexico

5. Cuerpo Academico Salud Animal y Microbiología Ambiental, Autonomous University of Queretaro, Queretaro 76230, Mexico

Abstract

Anti-microbial peptides play a vital role in the defense mechanisms of various organisms performing functions that range from the elimination of microorganisms, through diverse mechanisms, to the modulation of the immune response, providing protection to the host. Among these peptides, cathelicidins, a well-studied family of anti-microbial peptides, are found in various animal species, including reptiles. Due to the rise in anti-microbial resistance, these compounds have been suggested as potential candidates for developing new drugs. In this study, we identified and characterized a cathelicidin-like peptide called Aquiluscidin (Aq-CATH) from transcripts obtained from the skin and oral mucosa of the Querétaro’s dark rattlesnake, Crotalus aquilus. The cDNA was cloned, sequenced, and yielded a 566-base-pair sequence. Using bioinformatics, we predicted that the peptide precursor contains a signal peptide, a 101-amino-acid conserved cathelin domain, an anionic region, and a 34-amino-acid mature peptide in the C-terminal region. Aq-CATH and a derived 23-amino-acid peptide (Vcn-23) were synthesized, and their anti-microbial activity was evaluated against various species of bacteria in in vitro assays. The minimal inhibitory concentrations against bacteria ranged from 2 to 8 μg/mL for both peptides. Furthermore, at concentrations of up to 50 μM, they exhibited no significant hemolytic activity (<2.3% and <1.2% for Aquiluscidin and Vcn-23, respectively) against rat erythrocytes and displayed no significant cytotoxic activity at low concentrations (>65% cell viability at 25 µM). Finally, this study represents the first identification of an antimicrobial peptide in Crotalus aquilus, which belongs to the cathelicidin family and exhibits the characteristic features of these peptides. Both Aq-CATH and its derived molecule, Vcn-23, displayed remarkable inhibitory activity against all tested bacteria, highlighting their potential as promising candidates for further antimicrobial research.

Funder

FOPER-UAQ

FONDEC-UAQ

CONAHCyT

Publisher

MDPI AG

Subject

Virology,Microbiology (medical),Microbiology

Reference58 articles.

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3. O’Neill, J. (2023, May 03). Review on Anti-Microbial Resistance Anti-Microbial Resistance: Tackling a Crisis for the Health and Wealth of Nations. London: Review on Anti-Microbial Resistance. Available online: https://amr-review.org/sites/default/files/AMR%20Review%20Paper%20-%20Tackling%20a%20crisis%20for%20the%20health%20and%20wealth%20of%20nations_1.pdf.

4. Anti-microbial Peptides under Clinical Trials;Greber;Curr. Top. Med. Chem.,2017

5. Wu, R., Patocka, J., Nepovimova, E., Oleksak, P., Valis, M., Wu, W., and Kuca, K. (2021). Marine Invertebrate Peptides: Antimicrobial Peptides. Front. Microbiol., 12.

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