Selective arginines are important for the antibacterial activity and host cell interaction of human α‐defensin 5
Open accessAbstract
Defensins constitute a major family of natural antimicrobial peptides that protect the host against microbial invasion. Here, we report on the antibacterial properties and cellular interaction of Human Defensin 5 as a function of its positive charge and hydrophobicity. We find that selective replacement of arginine residues in HD‐5 by alanine or charge‐neutral lysine residues reduces antibacterial killing as well as host cell interaction. We identify arginines at positions 9 and 28 in the HD‐5 sequence as particularly important for its function. Replacement of arginine at position 13 to Histidine, as observed in a Crohn's disease patient, reduced bacterial killing strain‐selectively. Finally, we find that HD‐5 interacts with host cells via receptor‐mediated mechanisms.
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Some antimicrobial peptide classes, such as human alpha-defensins and plant gamma-defensins, need arginines exposed on the peptide surface, and their removal or substitution reduced bacterial killing activity.
“It has been demonstrated that some antimicrobial peptide classes, such as human a-defensins [32] and plant c-defensins [33], need arginines exposed on the peptide surface and their removal or substitution reduced bacterial killing activity.”
From Structural insights into <i>Cn</i>‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water (2015) · cites this paper as [32]
Cites
Defensins: antimicrobial peptides of innate immunity
Ganz, T. (2003) · Nature Reviews Immunology · doi:10.1038/nri1180 · Cited by 3,066 · see citing works
β-Defensins: Linking Innate and Adaptive Immunity Through Dendritic and T Cell CCR6
Yang, D., Chertov, O., Bykovskaia, S. N., Chen, Q., Buffo, M. J., Shogan, J., Anderson, M., Schröder, J. M., Wang, J. M., Howard, O. M. Z., et al. (1999) · Science · doi:10.1126/science.286.5439.525 · Cited by 1,809 · see citing works
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Santana, M. J., de Oliveira, A. L., Queiroz Júnior, L. H. K., Mandal, S. M., Matos, C. O., de O. Dias, R., Franco, O. L., & Lião, L. M. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.01.029 · Cited by 21 · see citing works
- Authors
- de Leeuw, E., Rajabi, M., Zou, G., Pazgier, M., & Lu, W.
- Affiliations
- University of Maryland, Baltimore (US)
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2009-07-07
- Volume
- 583
- Issue
- 15
- Pages
- 2507-2512
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2019382903
- Cited by
- 64
- References
- 2
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 6 · 2018: 3 · 2017: 4 · 2016: 4 · 2015: 9 · 2014: 3 · 2013: 6 · 2012: 9
- FWCI
- 5.46
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (AI056264)
- National Institute of Allergy and Infectious Diseases (AI 061482, AI 056264, R21AI056264, R01AI072732, R01AI061482)
- 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 › Immune Response and Inflammation
- Keywords
- antimicrobial peptides, arginine residues, antibacterial activity, host cell interactions, peptide charge, hydrophobicity, Crohn's disease
- MeSH terms
- Alanine, Amino Acid Sequence, Anti-Bacterial Agents, Arginine, Crohn Disease, Humans, Microbial Sensitivity Tests, Molecular Sequence Data, Protein Structure, Tertiary, alpha-Defensins, Antimicrobial Cationic Peptides, Microbial Viability
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