Cathelicidin family of antimicrobial peptides: Proteolytic processing and protease resistance
Abstract
Cathelicidins are a gene family of antimicrobial peptides produced as inactive precursors. Signal peptidase removes the N-terminal signal sequence, while peptidylglycine alpha-amidating monooxygenase often amidates and cleaves the C-terminal region. Removal of the cathelin domain liberates the active antimicrobial peptide. For mammalian sequences, this cleavage usually occurs through the action of elastase, but other tissue-specific processing enzymes may also operate. Once released, these bioactive peptides are susceptible to proteolytic degradation. We propose that some mature cathelicidins are naturally resistant to proteases due to their unusual primary structures. Among mammalian cathelicidins, proline-rich sequences should resist attack by serine proteases because proline prevents cleavage of the scissile bond. In hagfish cathelicidins, the unusual amino acid bromotryptophan may make the active peptides less susceptible to proteolysis for steric reasons. Such protease resistance could extend the pharmacokinetic lifetimes of cathelicidins in vivo, sustaining antimicrobial activity.
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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 [180]
The cathelicidin family shares primary sequence homology with the cystatins, of the cysteine proteinase inhibitor family, although amino acid residues considered important in these cystatins are often missing.
“The cathelicidins family shares primary sequence homology with the cystatins, of the cysteine proteinase inhibitor family, although amino acid residues considered important in these cystatins are often missing [180,181].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [180]
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- Authors
- Shinnar, A. E., Butler, K. L., & Park, H. J.
- Affiliations
- Columbia University (US)
- Corresponding author
- Shinnar, Ann Eisenberg
- Venue
- Bioorganic Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-12
- Volume
- 31
- Issue
- 6
- Pages
- 425-436
- ISSN
- 0045-2068 (ISSN-L)
- OpenAlex
- W1966733674
- Cited by
- 170
- References
- 50
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 12 · 2023: 11 · 2022: 3 · 2021: 9 · 2020: 5 · 2019: 6 · 2018: 8 · 2017: 5 · 2016: 9 · 2015: 11 · 2014: 14 · 2013: 10 · 2012: 4
- FWCI
- 3.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Bioorganic Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Keywords
- cathelicidin, antimicrobial peptides, proteolytic processing, protease resistance, signal peptidase, peptidylglycine alpha-amidating monooxygenase, proline-rich sequences, serine protease, pharmacokinetics
- MeSH terms
- Amino Acid Sequence, Animals, Arginine, Binding Sites, Multigene Family, Hagfishes, Humans, Mixed Function Oxygenases, Molecular Sequence Data, Multienzyme Complexes, Endopeptidases, Proline, Proteins, Tryptophan, Cysteine Proteinase Inhibitors, Sequence Homology, Amino Acid, Protein Sorting Signals, Antimicrobial Cationic Peptides, Cathelicidins
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