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Innate antimicrobial peptide protects the skin from invasive bacterial infection
Abstract
In mammals, several gene families encode peptides with antibacterial activity, such as the beta-defensins and cathelicidins. These peptides are expressed on epithelial surfaces and in neutrophils, and have been proposed to provide a first line of defence against infection by acting as 'natural antibiotics'. The protective effect of antimicrobial peptides is brought into question by observations that several of these peptides are easily inactivated and have diverse cellular effects that are distinct from antimicrobial activity demonstrated in vitro. To investigate the function of a specific antimicrobial peptide in a mouse model of cutaneous infection, we applied a combined mammalian and bacterial genetic approach to the cathelicidin antimicrobial gene family. The mature human (LL-37) and mouse (CRAMP) peptides are encoded by similar genes (CAMP and Cnlp, respectively), and have similar alpha-helical structures, spectra of antimicrobial activity and tissue distribution. Here we show that cathelicidins are an important native component of innate host defence in mice and provide protection against necrotic skin infection caused by Group A Streptococcus (GAS).
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“This is aided by the skin—the epidermis in particular—up-regulating and secreting antimicrobial peptides early in response to barrier damage and exposure to microbes (Fig. 2) (36, 37).”
From Wound repair and regeneration: Mechanisms, signaling, and translation (2014) · cites this paper as [37]
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Antimicrobial peptides of multicellular organisms
Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457
Wound repair and regeneration: Mechanisms, signaling, and translation
Eming, S. A., Martin, P., & Tomic-Canic, M. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3009337 · Cited by 3,562
Defensins: antimicrobial peptides of innate immunity
Ganz, T. (2003) · Nature Reviews Immunology · doi:10.1038/nri1180 · Cited by 3,066
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Self-citationAntimicrobial Peptides: An Emerging Category of Therapeutic Agents
Mahlapuu, M., Håkansson, J., Ringstad, L., & Björn, C. (2016) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2016.00194 · Cited by 2,020
Metadata
- Authors
- Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R. A., Pestonjamasp, V., Piraino, J., Huttner, K., & Gallo, R. L.
- Affiliations
- University of California San Diego (US)
- Massachusetts General Hospital (US)
- Corresponding author
- Gallo, Richard L.
- Venue
- Nature
- Published
- 2001-11
- Volume
- 414
- Issue
- 6862
- Pages
- 454-457
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1964758221
- Cited by
- 1,198
- References
- 30
- Citations by year
- 2026: 12 · 2025: 16 · 2024: 29 · 2023: 21 · 2022: 25 · 2021: 26 · 2020: 51 · 2019: 37 · 2018: 45 · 2017: 42 · 2016: 46 · 2015: 58 · 2014: 74 · 2013: 61 · 2012: 57
- FWCI
- 36.82
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Antimicrobial agents and applications
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- antimicrobial peptides, cathelicidin, LL-37, cramps, innate immunity, skin infections, Streptococcus pyogenes, host defense, beta-defensins
- MeSH terms
- Animals, Female, Immunity, Innate, Male, Mice, Inbred C57BL, Mutation, Proteins, Recombinant Fusion Proteins, Streptococcal Infections, Streptococcus pyogenes, Skin Diseases, Bacterial, Mice, Knockout, Antimicrobial Cationic Peptides, Drug Resistance, Bacterial, Mice, Cathelicidins
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