Cited by 1,198Antimicrobial Peptides and ActivitiesAntimicrobial agents and applicationsImmune Response and Inflammation

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Innate antimicrobial peptide protects the skin from invasive bacterial infection

Nizet, Victor, Ohtake, Takaaki, Lauth, Xavier, Trowbridge, Janet, Rudisill, Jennifer, Dorschner, Robert A., Pestonjamasp, Vasumati, Piraino, Joseph, Huttner, Kenneth, Gallo, Richard L.·2001·Nature

DOI 10.1038/35106587

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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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Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.
Zasloff, M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5449 · Cited by 2,305
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
Defensins. Natural peptide antibiotics of human neutrophils.
Ganz, T., Selsted, M. E., Szklarek, D., Harwig, S. S. L., Daher, K. A., Bainton, D. F., & Lehrer, R. I. (1985) · Journal of Clinical Investigation · doi:10.1172/jci112120 · Cited by 1,416
Ll-37, the Neutrophil Granule–And Epithelial Cell–Derived Cathelicidin, Utilizes Formyl Peptide Receptor–Like 1 (Fprl1) as a Receptor to Chemoattract Human Peripheral Blood Neutrophils, Monocytes, and T Cells
Yang, D., Chen, Q., Schmidt, A. P., Anderson, G. M., Wang, J., Wooters, J., Oppenheim, J. J., & Chertov, O. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1069 · Cited by 1,238
Human β-Defensin-1 Is a Salt-Sensitive Antibiotic in Lung That Is Inactivated in Cystic Fibrosis
Goldman, M. J., Anderson, G. M., Stolzenberg, E. D., Kari, U. P., ZASLOFF, M. A., & Wilson, J. M. (1997) · Cell · doi:10.1016/s0092-8674(00)81895-4 · Cited by 1,077
Complete genome sequence of an M1 strain of Streptococcus pyogenes
Ferretti, J. J., McShan, W. M., Ajdić, D., Savić, D. J., Savić, G., Lyon, K., Primeaux, C., Sezate, S. A., Suvorov, A. N., Kenton, S., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.071559398 · Cited by 936
The Human Gene FALL39 and Processing of the Cathelin Precursor to the Antibacterial Peptide LL‐37 in Granulocytes
Gudmundsson, G. H., Agerberth, B., Odeberg, J., Bergman, T., Olsson, B., & Salcedo, R. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0325z.x · Cited by 579
Cutaneous Injury Induces the Release of Cathelicidin Anti-Microbial Peptides Active Against Group A Streptococcus
Dorschner, R. A., Pestonjamasp, V. K., Tamakuwala, S., Ohtake, T., Rudisill, J., Nizet, V., Agerberth, B., Gudmundsson, G. H., & Gallo, R. L. (2001) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2001.01340.x · Cited by 567
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Identification of Defensin-1, Defensin-2, and CAP37/Azurocidin as T-cell Chemoattractant Proteins Released from Interleukin-8-stimulated Neutrophils
Chertov, O., Michiel, D. F., Xu, L., Wang, J., Tani, K., Murphy, W. J., Longo, D. L., Taub, D. D., & Oppenheim, J. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.2935 · Cited by 548
Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator
Islam, D., Bandholtz, L., Nilsson, J., Wigzell, H., Christensson, B., Agerberth, B., & Gudmundsson, G. H. (2001) · Nature Medicine · doi:10.1038/84627 · Cited by 429

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Gao, C., Zhang, L., Zhang, Y., Wallace, D. P., Lopez‐Soler, R. I., Higgins, P. J., & Zhang, W. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00279.2017 · Cited by 10
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Anghel, R., Jitaru, D., Bădescu, L., Ciocoiu, M., & Bădescu, M. (2014) · Journal of Biomedical Science and Engineering · doi:10.4236/jbise.2014.78052 · Cited by 10
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Effects of feeding rate on the expression of antimicrobial polypeptides and on susceptibility to Ichthyophthirius multifiliis in hybrid striped (sunshine) bass (Morone saxatilis ♂×M. chrysops ♀)
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Lineage−CD34+CD31+ Cells That Appear in Association with Severe Burn Injury Are Inhibitory on the Production of Antimicrobial Peptides by Epidermal Keratinocytes
Yoshida, S., Lee, J. O., Nakamura, K., Suzuki, S., Hendon, D. N., Kobayashi, M., & Suzuki, F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0082926 · Cited by 9
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Isolation and characterization of HepP: a virulence-related Pseudomonas aeruginosa heparinase
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Do Antimicrobial Peptides and Antimicrobial-Peptide Resistance Play Important Roles During Bacterial Infection?
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Bicarbonate Effects on Antibacterial Immunity and Mucus Glycobiology in the Cystic Fibrosis Lung: A Review With Selected Experimental Observations
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Samy, R. P., Thwin, M. M., Chow, V. T. K., Ho, B., & Gopalakrishnakone, P. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-012-6_15 · Cited by 8
KR12 peptide associated with cyclodextrin: Antimicrobial and antitumor activities
Teixeira, K. I. R., Cortés, M. E., Santos, R. A. S., de Oliveira, F., & Sinisterra, R. D. (2016) · Biointerphases · doi:10.1116/1.4968880 · Cited by 8
The Resistance to Host Antimicrobial Peptides in Infections Caused by Daptomycin-Resistant Staphylococcus aureus
Bhuiyan, M. S., Jiang, J., Kostoulias, X., Theegala, R., Lieschke, G. J., & Peleg, A. Y. (2021) · Antibiotics · doi:10.3390/antibiotics10020096 · Cited by 8
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Shen, J., Lu, X., Jin, X., Ding, J., Li, X., Mei, H., Chu, F., & Zhu, J. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.09.007 · Cited by 8
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Ramos, R. R., Domingues, L., & Gama, M. (2011) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) · Cited by 8
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FOTI, D. P., Greco, M., Cantiello, F., Damiano, R., Gulletta, E., Pujia, A., & Montalcini, T. (2014) · European Journal of Inflammation · doi:10.1177/1721727x1401200215 · Cited by 8
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Güerri‐Fernández, R., Díez‐Pérez, A., Mellibovsky, L., & Gómez, J. M. (2009) · Medicina Clínica · doi:10.1016/j.medcli.2008.10.044 · Cited by 8
A silver metal–organic cage with antibacterial activity for wound healing
Chen, L., Cheng, J., Wang, L., Fan, W., Lu, Z., & Zheng, L. (2023) · RSC Advances · doi:10.1039/d3ra04013e · Cited by 7
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Mansouri, P., Chalangari, R., Martits‐Chalangari, K., & Saffarian, Z. (2013) · Springer eBooks · doi:10.1007/978-3-642-39495-9_25 · Cited by 7
Bacterial soft tissue infection in psoriasis despite induction of epidermal antimicrobial peptides
Steinz, K., Schubert, S., Harder, J., Gerdes, S., Mrowietz, U., & Gläser, R. (2014) · Experimental Dermatology · doi:10.1111/exd.12538 · Cited by 7
Lysozyme-Antimicrobial Peptide Fusion Protein Promotes the Diabetic Wound Size Reduction in Streptozotocin (STZ)-Induced Diabetic Rats
Chen, Q., Li, W., Wang, J., Qu, X., & Wang, G. (2018) · Medical Science Monitor · doi:10.12659/msm.912596 · Cited by 7
Transcriptional regulation of cathelicidin genes in chicken bone marrow cells
Lee, S. I., Jang, H. J., Jeon, M.-H., Lee, M. O., Kim, J. S., Jeon, I., & Byun, S. J. (2016) · Poultry Science · doi:10.3382/ps/pev361 · Cited by 7
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Mammalian antimicrobial peptides: defensins and cathelicidins
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Kotra, S. R. (2014) · Journal of Microbiology and Infectious Diseases · doi:10.5799/ahinjs.02.2014.01.0117 · Cited by 6
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Exogenous LL-37 but not homogenates of desquamated oral epithelial cells shows activity against Streptococcus mutans
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Role of T cells
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He, B., Li, Y., Li, M., Kang, M., Liu, X., Huang, J., Wang, D., Lam, J. W. Y., & Tang, B. Z. (2024) · Angewandte Chemie · doi:10.1002/ange.202405030 · Cited by 5
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In silico characterisation of stand-alone response regulators of Streptococcus pyogenes
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Hosting for the cruel and the inconsequential
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Peptides épithéliaux antimicrobiens
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Tissue-engineered skin products
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Holani, R., Rathnayaka, C., Blyth, G. A. D., Babbar, A., Lahiri, P., Young, D. W., Dufour, A., Hollenberg, M. D., McKay, D. M., & Cobo, E. R. (2022) · Journal of Innate Immunity · doi:10.1159/000526121 · Cited by 4
Studies on distribution of α1-antitrypsin, lysozyme, lactoferrin, and mast cell enzymes in diseased middle ear mucosa
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Spatial distribution of antimicrobial peptides and mast cells in the skin of the external auditory canal
Yoon, Y. J., & Lee, E. J. (2011) · The Journal of Laryngology & Otology · doi:10.1017/s0022215111002271 · Cited by 4
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Brown, L., Schlechte, J., Rashid, M., Lou, Y., Nguyen, A., Hassanabad, M. F., Hiroki, C. H., Cobo, E. R., Hollenberg, M. D., Mcdonald, B., et al. (2026) · Science · doi:10.1126/science.adv0377 · Cited by 3
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Alalwani, S. M., Sierigk, J., Herr, C., Pinkenburg, O., & Bals, R. (2009) · Journal of Cystic Fibrosis · doi:10.1016/s1569-1993(09)60092-8 · Cited by 2
Secondary necrosis of apoptotic neutrophils induced by the human cathelicidin LL-37 is not proinflammatory to phagocytosing macrophages
Li, H., Barlow, P. G., Bylund, J., Mackellar, A., Björstad, Å., Conlon, J., Hiemstra, P. S., Haslett, C., Gray, M., Simpson, A. J., et al. (2009) · Cytokine · doi:10.1016/j.cyto.2009.07.484 · Cited by 3
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Owais, M., Ansari, M. A., Ahmad, I., Zia, Q., Pierard, G., & Chauhan, A. (2010) · Springer eBooks · doi:10.1007/978-3-642-12173-9_15 · Cited by 3
Vitamin D Deficiency in Critically Ill Patients
Lee, J., & Lee, J. M. (2017) · Surgical Metabolism and Nutrition · doi:10.18858/smn.2017.8.2.17 · Cited by 3
Effect of calcitriol supplementation on infectious biomarkers in patients with positive systemic inflammatory response: A Randomized Controlled Trial
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Antimicrobial Peptides as First-Line Effector Molecules of the Human Innate Immune System
Gläser, R., Harder, J., & Schröder, J. (2007) · Nucleic acids and molecular biology · doi:10.1007/978-3-540-73930-2_9 · Cited by 3
Wound Repair and Antimicrobial Peptides
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Self-citation
Transcriptional Profile of Escherichia coli in Response to Novispirin G10
Kruse, T., Christensen, B. B., Raventós, D., Nielsen, A. K., Nielsen, J. D., Vukmirovic, N., & Kristensen, H. (2009) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-009-9169-0 · Cited by 3
Helping the Host: Induction of Antimicrobial Peptides as a Novel Therapeutic Strategy Against Infections
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Cytotoxic Effects and Biocompatibility of Antimicrobial Materials
Bazaka, O., & Bazaka, K. (2015) · Springer eBooks · doi:10.1007/978-3-319-18594-1_7 · Cited by 3
A deficiency in cathelicidin reduces lung tumor growth in NNK/NTHi-induced A/J mice.
Yao, Y., Wu, J., Zhou, H., Firrman, J., Xiao, W., Sun, Z., & Li, D. (2018) · Europe PMC (PubMed Central) · Cited by 3
Epidermal Physiology
Rousselle, P., Gentilhomme, E., & Neveux, Y. (2017) · Springer eBooks · doi:10.1007/978-3-319-32383-1_36 · Cited by 3

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.
ORCID: Nizet, Victor
Ohtake, Takaaki
Dorschner, Robert A.
Gallo, Richard L.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2001-11
Volume: 414
Issue: 6862
Pages: 454-457
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/35106587
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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Innate antimicrobial peptide protects the skin from invasive bacterial infection

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