Cathelicidin peptides as candidates for a novel class of antimicrobials
Abstract
Cathelicidin peptides are a numerous group of mammalian cationic antimicrobial peptides. Despite a common evolutionary origin of their genes, peptides display a remarkable variety of sizes, sequences and structures. Their spectra of antimicrobial activity are varied and cover a range of organisms that includes bacteria, fungi and enveloped viruses. In addition, they bind to and neutralize the effects of endotoxin. These features make this family of peptides good candidates in view of a therapeutic use. The most promising ones are currently under evaluation as leads for the development of novel anti-infectives, and synthetic variants are in an advanced stage of development for specific clinical applications. This review focuses on recent studies on the structure and in vitro and in vivo biological activities of these peptides. Keywords: Cathelicidin Peptides, Antimicrobials, anti-infective drugs, cationic antimicrobial peptides, protegrins, indolicidin, protegrin, vancomycin-resistant enterococcus faecalis
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Cathelicidins are cationic and amphiphilic peptides consisting of 12-97 amino acids, found in humans, other vertebrates and some species of fish.
“Cathelicidins, first discovered in bovine neutrophils by Zanetti et al. in the early 1990s, are cationic and amphiphilic peptides consisting of 12–97 amino acids, found in humans, other vertebrates and some species of fish [179].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [179]
Cathelicidins rapidly destroy lipoprotein membranes of microbes enveloped in phagosomes after fusion with lysosomes in macrophages.
“Cathelicidins rapidly destroy lipoprotein membranes of microbes enveloped in phagosomes after fusion with lysosomes in macrophages [179,180].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [179]
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Cathelicidins, multifunctional peptides of the innate immunity
Zanetti, M. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0403147 · Cited by 988 · see citing works
Self-citationCathelicidins - a family of multifunctional antimicrobial peptides
Bals, R., & Wilson, J. M. (2003) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-003-2186-9 · Cited by 427 · see citing works
Cathelicidin family of antimicrobial peptides: Proteolytic processing and protease resistance
Shinnar, A. E., Butler, K. L., & Park, H. J. (2003) · Bioorganic Chemistry · doi:10.1016/s0045-2068(03)00080-4 · Cited by 170 · see citing works
The Role of Reactive Species on Innate Immunity
Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142 · see citing works
Kitagawa, M., Shiraishi, T., Yamamoto, S., Kutomi, R., Ohkoshi, Y., Sato, T., Wakui, H., Itoh, H., Miyamoto, A., & Yokota, S.-I. (2017) · AMB Express · doi:10.1186/s13568-017-0430-1 · Cited by 39 · see citing works
- Authors
- Zanetti, M., Gennaro, R., Skerlavaj, B., Tomasinsig, L., & Circo, R.
- Affiliations
- University of Udine (IT)
- Corresponding author
- Circo, Raffaella
- Venue
- Current Pharmaceutical Design
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2002-04-01
- Volume
- 8
- Issue
- 9
- Pages
- 779-793
- ISSN
- 1381-6128 (ISSN-L)
- OpenAlex
- W2166357414
- Cited by
- 105
- References
- 0
- Citations by year
- 2023: 8 · 2022: 3 · 2021: 3 · 2020: 2 · 2019: 3 · 2018: 1 · 2017: 3 · 2016: 2 · 2015: 2 · 2014: 3 · 2013: 6 · 2012: 5
- FWCI
- 5.19
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Pharmaceutical Design (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System (University of Udine) (submittedVersion)
- ArTS Archivio della ricerca di Trieste (University of Trieste https://www.units.it/) (submittedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
- Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
- Keywords
- cationic antimicrobial peptides, antimicrobial peptides, anti-infective agents, protegrins, indolicidin, endotoxin neutralization, vancomycin-resistant Enterococcus faecalis, peptide structure, antibacterial activity, antifungal activity, antiviral activity
- MeSH terms
- Animals, Anti-Infective Agents, Anti-Bacterial Agents, Bacteria, Fungi, Humans, Lethal Dose 50, Structure-Activity Relationship, Viruses, Antimicrobial Cationic Peptides
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