Structure-activity relationships of the intramolecular disulfide bonds in coprisin, a defensin from the dung beetle
Open accessAbstract
Defensins, which are small cationic molecules produced by organisms as part of their innate immune response, share a common structural scaffold that is stabilized by three disulfide bridges. Coprisin is a 43-amino acid defensin-like peptide from Copris tripartitus. Here, we report the intramolecular disulfide connectivity of cysteine-rich coprisin, and show that it is the same as in other insect defensins. The disulfide bond pairings of coprisin were determined by combining the enzymatic cleavage and mass analysis. We found that the loss of any single disulfide bond in coprisin eliminated all antibacterial, but not antifungal, activity. Circular dichroism (CD) analysis showed that two disulfide bonds, Cys20-Cys39 and Cys24-Cys41, stabilize coprisin's α-helical region. Moreover, a BLAST search against UniProtKB database revealed that coprisin's α-helical region is highly homologous to those of other insect defensins.
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Coprisin, a defensin-like 43-mer peptide with three disulfide bonds, has been suggested to be a crucial participant in reactive oxygen species, especially hydroxyl radicals.
“Coprisin, a defensin-like 43-mer peptide with three disulfide bonds [187], has been suggested to be a crucial participant in reactive oxygen species (ROS), especially hydroxyl radicals (•OH) [188].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [187]
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References 19 · Cited by 25
- Authors
- Lee, J., Lee, D., Choi, H., Kim, H. H., Kim, H., Hwang, J. S., Lee, D. G., & Kim, J. I.
- Affiliations
- Kyungpook National University (KR)
- Daejin University (KR)
- Gwangju Institute of Science and Technology (KR)
- Corresponding author
- Kim, Jae Il
- Venue
- BMB Reports
- Published
- 2014-11-30
- Volume
- 47
- Issue
- 11
- Pages
- 625-630
- ISSN
- 1976-6696 (ISSN-L)
- PMC
- PMC4281341
- OpenAlex
- W2037497267
- Cited by
- 25
- References
- 19
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 5 · 2020: 1 · 2018: 3 · 2017: 3 · 2016: 3 · 2015: 1
- FWCI
- 1.90
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc
- Locations
- BMB Reports (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- National Research Foundation
- Rural Development Administration (PJ008158, NRF-C1ABA001-2011-0018559)
- National Research Foundation of Korea
- Ministry of Education, Science and Technology (2013R1A1A2009798)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- defensins, intramolecular disulfide bond, disulfide connectivity, Copris tripartitus, dung beetles, antibacterial activity, antifungal activity, alpha-helix stabilization, innate immunity, insect peptides, structure-activity relationship
- MeSH terms
- Amino Acid Sequence, Animals, Anti-Bacterial Agents, Antifungal Agents, Coleoptera, Circular Dichroism, Cysteine, Disulfides, Fungi, Gram-Negative Bacteria, Gram-Positive Bacteria, Microbial Sensitivity Tests, Molecular Sequence Data, Structure-Activity Relationship, Sequence Alignment, Protein Structure, Secondary, Insect Proteins, Catalytic Domain
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