Kassorins: novel innate immune system peptides from skin secretions of the African hyperoliid frogs, Kassina maculata and Kassina senegalensis.
Abstract: From defensive skin secretions acquired from two species of African hyperoliid frogs, Kassina maculata and Kassina senegalensis, we have isolated two structurally related, C-terminally amidated tridecapeptides of novel primary structure that exhibit a broad spectrum of biological activity. In reflection of their structural novelty and species of origin, we named the peptides kassorin M (FLEGLLNTVTGLLamide; 1387.8 Da) and kassorin S (FLGGILNTITGLLamide; 1329.8 Da), respectively. The primary structure and organisation of the biosynthetic precursors of kassorins M and S were deduced from cloned skin secretion-derived cDNA. Both open-reading frames encoded a single copy of kassorin M and S, respectively, located at the C-terminus. Kassorins display limited structural similarities to vespid chemotactic peptides (7/13 residues), temporin A (5/13 residues), the N-terminus of Lv-ranaspumin, a foam nest surfactant protein of the frog, Leptodactylus vastus, and an N-terminal domain of the equine sweat surfactant protein, latherin. Both peptides elicit histamine release from rat peritoneal mast cells. However, while kassorin S was found to possess antibacterial activity against Staphylococcus aureus, kassorin M was devoid of such activity. In contrast, kassorin M was found to contract the smooth muscle of guinea pig urinary bladder (EC(50) = 4.66 nM) and kassorin S was devoid of this activity. Kassorins thus represent the prototypes of a novel family of peptides from the amphibian innate immune system as occurring in defensive skin secretions.
Copyright © 2010 Elsevier Ltd. All rights reserved.
Publication Date: 2010-11-01 PubMed ID: 21040978DOI: 10.1016/j.molimm.2010.09.018Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study reveals the discovery of two unique peptides, kassorin M and kassorin S, derived from the skin secretions of African hyperoliid frogs, the Kassina maculata and Kassina senegalensis. These novel peptides exhibit a diverse range of biological activities, with potential implications for both immunology and medical science.
Isolation of Peptides from Frog Skin Secretion
- The research focused on defensive skin secretions obtained from two species of African hyperoliid frogs, the Kassina maculata and the Kassina senegalensis.
- Through study and analysis, the researchers isolated two structurally related but unique tridecapeptides (peptides composed of 13 amino acids).
- In accordance with their structural novelty and origin species, these peptides were named kassorin M and kassorin S.
Structural Analysis of Kassorins
- The researchers deduced the primary structure and organization of the biosynthetic precursors (previous steps in the synthesis process) of kassorins M and S from cloned skin secretion-derived cDNA.
- The peptides had limited structural similarities to other known chemotactic peptides and proteins, indicating novelty.
Biological Activity of Kassorins
- Both kassorins were found to trigger histamine release from rat peritoneal mast cells, indicating immunological activity.
- However, their reactions differed when tested against bacteria and smooth muscle contraction: kassorin S demonstrated antibacterial activity against Staphylococcus aureus, while kassorin M lacked this property.
- On the other hand, kassorin M caused contraction of the smooth muscle in the urinary bladder of a guinea pig, which was not observed for kassorin S.
Significance of the Study
- Kassorins represent a new class of peptides recognized in the amphibian innate immune system, present within defensive skin secretions.
- Understanding the behavior and structure of these peptides could provide valuable insights for immunological research and may lead to the development of new treatments for various medical conditions.
Cite This Article
APA
Chen H, Wang L, Zeller M, Hornshaw M, Wu Y, Zhou M, Li J, Hang X, Cai J, Chen T, Shaw C.
(2010).
Kassorins: novel innate immune system peptides from skin secretions of the African hyperoliid frogs, Kassina maculata and Kassina senegalensis.
Mol Immunol, 48(4), 442-451.
https://doi.org/10.1016/j.molimm.2010.09.018 Publication
Researcher Affiliations
- Molecular Therapeutics Research, School of Pharmacy, Medical Biology Centre, Queen's University, Belfast BT9 7BL, Northern Ireland, UK.
MeSH Terms
- Africa
- Amino Acid Sequence
- Animals
- Anti-Infective Agents / pharmacology
- Anura / immunology
- Base Sequence
- Candida albicans / drug effects
- Cloning, Molecular
- DNA, Complementary / genetics
- Guinea Pigs
- Immunity, Innate / immunology
- In Vitro Techniques
- Mass Spectrometry
- Microbial Sensitivity Tests
- Molecular Sequence Data
- Muscle, Smooth / drug effects
- Peptides / chemistry
- Peptides / isolation & purification
- Peptides / metabolism
- Rats
- Sequence Alignment
- Skin / drug effects
- Skin / metabolism
- Staphylococcus aureus / drug effects
- Urinary Bladder / drug effects
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