LL-37, the only human member of the cathelicidin family of antimicrobial peptides

Dürr, Ulrich H.N.; Sudheendra, U.S.; Ramamoorthy, Ayyalusamy

doi:10.1016/j.bbamem.2006.03.030

Cited by 1,049Antimicrobial Peptides and ActivitiesAntimicrobial agents and applicationsS100 Proteins and Annexins

LL-37, the only human member of the cathelicidin family of antimicrobial peptides

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Dürr, Ulrich H.N., Sudheendra, U.S., Ramamoorthy, Ayyalusamy·2006·Biochimica et Biophysica Acta (BBA) - Biomembranes

DOI 10.1016/j.bbamem.2006.03.030

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Abstract

Antimicrobial peptides and their precursor molecules form a central part of human and mammalian innate immunity. The underlying genes have been thoroughly investigated and compared for a considerable number of species, allowing for phylogenetic characterization. On the phenotypical side, an ever-increasing number of very varied and distinctive influences of antimicrobial peptides on the innate immune system are reported. The basic biophysical understanding of mammalian antimicrobial peptides, however, is still very limited. This is especially unsatisfactory since knowledge of structural properties will greatly help in the understanding of their immunomodulatory functions. The focus of this review article will be on LL-37, the only cathelicidin-derived antimicrobial peptide found in humans. LL-37 is a 37-residue, amphipathic, helical peptide found throughout the body and has been shown to exhibit a broad spectrum of antimicrobial activity. It is expressed in epithelial cells of the testis, skin, the gastrointestinal tract, and the respiratory tract, and in leukocytes such as monocytes, neutrophils, T cells, NK cells, and B cells. It has been found to have additional defensive roles such as regulating the inflammatory response and chemo-attracting cells of the adaptive immune system to wound or infection sites, binding and neutralizing LPS, and promoting re-epthelialization and wound closure. The article aims to report the known biophysical facts, with an emphasis on structural evidence, and to set them into relation with insights gained on phylogenetically related antimicrobial peptides in other species. The multitude of immuno-functional roles is only outlined. We believe that this review will aid the future work on the biophysical, biochemical and immunological investigations of this highly intriguing molecule.

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Among eutherians, primates and rodents have a single cathelicidin gene.
“Among eutherians, primates and rodents have a single cathelicidin gene 52,53”
From Genome analysis of the platypus reveals unique signatures of evolution (2008) · cites this paper as [52]
Section 1.2 (Cathelicidins) reports a single cathelicidin in humans, rhesus monkeys, mice, rats, and guinea pigs. It also identifies rabbits as a rodent exception with a second cathelicidin, so the claim is too broad for rodents as a group. (LLM, conf=0.90)
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K.A. Henzler Wildman, PhD Thesis. The mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37, (2003). University of Michigan, Ann Arbor.

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Authors: Dürr, U. H. N., Sudheendra, U. S., & Ramamoorthy, A.
Affiliations: University of Michigan (US)
Corresponding author: Ramamoorthy, Ayyalusamy
ORCID: Ramamoorthy, Ayyalusamy
Venue: Biochimica et Biophysica Acta (BBA) - Biomembranes
Publisher: Elsevier BV
Published: 2006-09
Volume: 1758
Issue: 9
Pages: 1408-1425
ISSN: 0005-2736 (ISSN-L)
DOI: 10.1016/j.bbamem.2006.03.030
OpenAlex: W2063116767
Cited by: 1,049
References: 213
Citations by year: 2026: 48 · 2025: 50 · 2024: 64 · 2023: 63 · 2022: 63 · 2021: 73 · 2020: 70 · 2019: 69 · 2018: 59 · 2017: 64 · 2016: 58 · 2015: 47 · 2014: 42 · 2013: 48 · 2012: 32
FWCI: 4.58
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2547 d)
Locations: Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Allergy and Infectious Diseases (AI 054515, R01AI054515)
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 › S100 Proteins and Annexins
Keywords: LL-37, cathelicidin, antimicrobial peptides, innate immunity, peptide structure, amphipathic helical peptides, antimicrobial activity, immunomodulation, inflammation regulation, chemotaxis, LPS neutralization, wound healing, epithelial cells, leukocytes
MeSH terms: Amino Acid Sequence, Animals, Humans, Immunity, Innate, Lipopolysaccharides, Molecular Sequence Data, Gene Expression, Antimicrobial Cationic Peptides, Cathelicidins

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LL-37, the only human member of the cathelicidin family of antimicrobial peptides

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