The alyteserins: Two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae)

J. Michael Conlon; Anni Demandt; Per F. Nielsen; Jérôme Leprince; Hubert Vaudry; Douglas C. Woodhams

doi:10.1016/j.peptides.2009.03.004

The alyteserins: Two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae)

J. Michael Conlon
, Anni Demandt
, Per F. Nielsen
, Jérôme Leprince
, Hubert Vaudry
, Douglas C. Woodhams

School of Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

50 Citations (Scopus)

Abstract

Two families of structurally related C-terminally α-amidated antimicrobial peptides have been identified in norepinephrine-stimulated skin secretions of the midwife toad Alytes obstetricans (Alytidae). The alyteserin-1 peptides (Gly-Leu-Lys-(Asp/Glu)-Ile-Phe-Lys-Ala-Gly-Leu-Gly-Ser-Leu-Val-Lys-(Gly/Asn)-Ile-Ala-Ala-His-Val-Ala-(Asn/Ser).NH₂) show limited structural similarity to the ascaphins from the skins of frogs of the family Leiopelmatidae. Alyteserin-2a (Ile-Leu-Gly-Lys-Leu-Leu-Ser-Thr-Ala-Ala-Gly-Leu-Leu-Ser-Asn-Leu.NH₂) and alyteserin-2b and -2c (Ile-Leu-Gly-Ala-Ile-Leu-Pro-Leu-Val-Ser-Gly-Leu-Leu-Ser-(Asn/Ser)-Lys-Leu.NH₂) show limited sequence identity with bombinin H6, present in the skins of frogs of the family Bombinatoridae. The alyteserin-1 peptides show selective growth inhibitory activity against the Gram-negative bacteria Escherichia coli (MIC = 25 μM) whereas alyteserin-2a is more potent against the Gram-positive bacteria Staphylococcus aureus (MIC = 50 μM). The hemolytic activity against human erythrocytes of all peptides tested is relatively weak (LC₅₀ > 100 μM). The data demonstrate that the frogs belonging to the family Alytidae are among those producing dermal antimicrobial peptides that may represent a component of the animal's system of innate immunity.

Original language	English
Pages (from-to)	1069-1073
Number of pages	5
Journal	Peptides
Volume	30
Issue number	6
DOIs	https://doi.org/10.1016/j.peptides.2009.03.004
Publication status	Published (in print/issue) - Jun 2009

Funding

This work was supported by a grant from the Terry Fox Fund for Cancer Research and a Faculty Support Grant from U.A.E. University. The authors thank Ms Eman Ahmed for technical assistance and Jos Kielgast for collecting specimens.

Keywords

Alyteserin
Alytidae
Antimicrobial peptide
Ascaphin
Bombinin
Frog skin

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10.1016/j.peptides.2009.03.004

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title = "The alyteserins: Two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae)",

abstract = "Two families of structurally related C-terminally α-amidated antimicrobial peptides have been identified in norepinephrine-stimulated skin secretions of the midwife toad Alytes obstetricans (Alytidae). The alyteserin-1 peptides (Gly-Leu-Lys-(Asp/Glu)-Ile-Phe-Lys-Ala-Gly-Leu-Gly-Ser-Leu-Val-Lys-(Gly/Asn)-Ile-Ala-Ala-His-Val-Ala-(Asn/Ser).NH2) show limited structural similarity to the ascaphins from the skins of frogs of the family Leiopelmatidae. Alyteserin-2a (Ile-Leu-Gly-Lys-Leu-Leu-Ser-Thr-Ala-Ala-Gly-Leu-Leu-Ser-Asn-Leu.NH2) and alyteserin-2b and -2c (Ile-Leu-Gly-Ala-Ile-Leu-Pro-Leu-Val-Ser-Gly-Leu-Leu-Ser-(Asn/Ser)-Lys-Leu.NH2) show limited sequence identity with bombinin H6, present in the skins of frogs of the family Bombinatoridae. The alyteserin-1 peptides show selective growth inhibitory activity against the Gram-negative bacteria Escherichia coli (MIC = 25 μM) whereas alyteserin-2a is more potent against the Gram-positive bacteria Staphylococcus aureus (MIC = 50 μM). The hemolytic activity against human erythrocytes of all peptides tested is relatively weak (LC50 > 100 μM). The data demonstrate that the frogs belonging to the family Alytidae are among those producing dermal antimicrobial peptides that may represent a component of the animal's system of innate immunity.",

keywords = "Alyteserin, Alytidae, Antimicrobial peptide, Ascaphin, Bombinin, Frog skin",

author = "Conlon, \{J. Michael\} and Anni Demandt and Nielsen, \{Per F.\} and J{\'e}r{\^o}me Leprince and Hubert Vaudry and Woodhams, \{Douglas C.\}",

year = "2009",

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language = "English",

volume = "30",

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AU - Vaudry, Hubert

AU - Woodhams, Douglas C.

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N2 - Two families of structurally related C-terminally α-amidated antimicrobial peptides have been identified in norepinephrine-stimulated skin secretions of the midwife toad Alytes obstetricans (Alytidae). The alyteserin-1 peptides (Gly-Leu-Lys-(Asp/Glu)-Ile-Phe-Lys-Ala-Gly-Leu-Gly-Ser-Leu-Val-Lys-(Gly/Asn)-Ile-Ala-Ala-His-Val-Ala-(Asn/Ser).NH2) show limited structural similarity to the ascaphins from the skins of frogs of the family Leiopelmatidae. Alyteserin-2a (Ile-Leu-Gly-Lys-Leu-Leu-Ser-Thr-Ala-Ala-Gly-Leu-Leu-Ser-Asn-Leu.NH2) and alyteserin-2b and -2c (Ile-Leu-Gly-Ala-Ile-Leu-Pro-Leu-Val-Ser-Gly-Leu-Leu-Ser-(Asn/Ser)-Lys-Leu.NH2) show limited sequence identity with bombinin H6, present in the skins of frogs of the family Bombinatoridae. The alyteserin-1 peptides show selective growth inhibitory activity against the Gram-negative bacteria Escherichia coli (MIC = 25 μM) whereas alyteserin-2a is more potent against the Gram-positive bacteria Staphylococcus aureus (MIC = 50 μM). The hemolytic activity against human erythrocytes of all peptides tested is relatively weak (LC50 > 100 μM). The data demonstrate that the frogs belonging to the family Alytidae are among those producing dermal antimicrobial peptides that may represent a component of the animal's system of innate immunity.

AB - Two families of structurally related C-terminally α-amidated antimicrobial peptides have been identified in norepinephrine-stimulated skin secretions of the midwife toad Alytes obstetricans (Alytidae). The alyteserin-1 peptides (Gly-Leu-Lys-(Asp/Glu)-Ile-Phe-Lys-Ala-Gly-Leu-Gly-Ser-Leu-Val-Lys-(Gly/Asn)-Ile-Ala-Ala-His-Val-Ala-(Asn/Ser).NH2) show limited structural similarity to the ascaphins from the skins of frogs of the family Leiopelmatidae. Alyteserin-2a (Ile-Leu-Gly-Lys-Leu-Leu-Ser-Thr-Ala-Ala-Gly-Leu-Leu-Ser-Asn-Leu.NH2) and alyteserin-2b and -2c (Ile-Leu-Gly-Ala-Ile-Leu-Pro-Leu-Val-Ser-Gly-Leu-Leu-Ser-(Asn/Ser)-Lys-Leu.NH2) show limited sequence identity with bombinin H6, present in the skins of frogs of the family Bombinatoridae. The alyteserin-1 peptides show selective growth inhibitory activity against the Gram-negative bacteria Escherichia coli (MIC = 25 μM) whereas alyteserin-2a is more potent against the Gram-positive bacteria Staphylococcus aureus (MIC = 50 μM). The hemolytic activity against human erythrocytes of all peptides tested is relatively weak (LC50 > 100 μM). The data demonstrate that the frogs belonging to the family Alytidae are among those producing dermal antimicrobial peptides that may represent a component of the animal's system of innate immunity.

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KW - Alytidae

KW - Antimicrobial peptide

KW - Ascaphin

KW - Bombinin

KW - Frog skin

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U2 - 10.1016/j.peptides.2009.03.004

DO - 10.1016/j.peptides.2009.03.004

M3 - Article

C2 - 19463738

AN - SCOPUS:67349117100

SN - 0196-9781

VL - 30

SP - 1069

EP - 1073

JO - Peptides

JF - Peptides

IS - 6

ER -

The alyteserins: Two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae)

Abstract

Funding

Keywords

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