Cited by 1,107Antimicrobial Peptides and ActivitiesInvertebrate Immune Response MechanismsAntimicrobial agents and applications

Anti-microbial peptides: from invertebrates to vertebrates

Bulet, Philippe, Stöcklin, Reto, Menin, Laure·2004·Immunological Reviews

Abstract

Gene-encoded anti-microbial peptides (AMPs) are widespread in nature, as they are synthesized by microorganisms as well as by multicellular organisms from both the vegetal and the animal kingdoms. These naturally occurring AMPs form a first line of host defense against pathogens and are involved in innate immunity. Depending on their tissue distribution, AMPs ensure either a systemic or a local protection of the organism against environmental pathogens. They are classified into three major groups: (i) peptides with an alpha-helical conformation (insect cecropins, magainins, etc.), (ii) cyclic and open-ended cyclic peptides with pairs of cysteine residues (defensins, protegrin, etc.), and (iii) peptides with an over-representation of some amino acids (proline rich, histidine rich, etc.). Most AMPs display hydrophobic and cationic properties, have a molecular mass below 25-30 kDa, and adopt an amphipathic structure (alpha-helix, beta-hairpin-like beta-sheet, beta-sheet, or alpha-helix/beta-sheet mixed structures) that is believed to be essential to their anti-microbial action. Interestingly, in recent years, a series of novel AMPs have been discovered as processed forms of large proteins. Despite the extreme diversity in their primary and secondary structures, all natural AMPs have the in vitro particularity to affect a large number of microorganisms (bacteria, fungi, yeast, virus, etc.) with identical or complementary activity spectra. This review focuses on AMPs forming alpha-helices, beta-hairpin-like beta-sheets, beta-sheets, or alpha-helix/beta-sheet mixed structures from invertebrate and vertebrate origins. These molecules show some promise for therapeutic use.

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Crossref · 10.1111/j.0105-2896.2004.0124.x

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  • AMPs can be secreted in the outer parts of the body and play functions in the control/establishment of ectosymbiosis, as described for the hydrothermal worm Alvinella pompejana.

    “AMPs are chemical components that take part in both the internal and external immune defenses (i.e., they can be secreted in the outer parts of the body), thus playing functions in the control/establishment of ectosymbiosis as described for the hydrothermal worm Alvinella pompejana (19–21).”

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Authors
Bulet, P., Stöcklin, R., & Menin, L.
Affiliations
Atheris Laboratories (Switzerland) (CH)
Corresponding author
Bulet, Philippe
Venue
Immunological Reviews
Publisher
Wiley
Published
2004-03-05
Volume
198
Issue
1
Pages
169-184
ISSN
  • 0105-2896 (ISSN-L)
  • 1600-065X
OpenAlex
W2089175291
Cited by
1,107
References
87
Citations by year
2026: 17 · 2025: 33 · 2024: 47 · 2023: 35 · 2022: 46 · 2021: 41 · 2020: 43 · 2019: 34 · 2018: 50 · 2017: 50 · 2016: 50 · 2015: 60 · 2014: 57 · 2013: 56 · 2012: 67
FWCI
7.41
Type
journal article
Language
en
Open access
closed
Locations
  • Immunological Reviews (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
  • Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
Keywords
antimicrobial peptides, innate immunity, host defense against infection, alpha-helical peptides, β-sheet peptides, cecropin, magainin, defensins, protegrins, proline-rich peptides, histidine-rich peptides
MeSH terms
Amino Acid Sequence, Animals, Anti-Bacterial Agents, Invertebrates, Models, Molecular, Molecular Sequence Data, Peptides, Cyclic, Vertebrates, Protein Structure, Secondary, Protein Structure, Tertiary, Antimicrobial Cationic Peptides

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