Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis

J. Michael Conlon; Eman Ahmed; Laurent Coquet; Thierry Jouenne; Jérôme Leprince; Hubert Vaudry; Jay D. King

doi:10.1016/j.toxicon.2009.02.018

Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis

J. Michael Conlon
, Eman Ahmed
, Laurent Coquet
, Thierry Jouenne
, Jérôme Leprince
, Hubert Vaudry
, Jay D. King

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

19 Citations (Scopus)

Abstract

Six structurally similar and strongly cationic peptides belonging to the brevinin-1 family were isolated from skin secretions of the plains leopard frog Lithobates blairi and the lowland leopard frog Lithobates yavapaiensis on the basis of their antimicrobial activities. Brevinin-1BLc (FLPIIAGIAAKFLPKIFCTISKKC) from L. blairi represented the most potent peptide (MIC = 25 μM Escherichia coli, MIC = 1.5 μM Staphylococcus aureus, MIC = 3 μM Candida albicans, LC₅₀ = 9 μM human erythrocytes and LC₅₀ = 6 μM HepG2 human hepatoma-derived cells). The appreciably lower antimicrobial potencies of brevinin-1Ya and -1Yc from L. yavapaiensis correlate with the decreases in cationicity produced by the amino acid substitutions Lys¹¹ → Asn (brevinin-1Ya) and Pro¹⁴ → Glu (brevinin-1Yc). In addition, a peptide isolated from the skin secretions of L. yavapaiensis belonging to the ranatuerin-2 family (ranatuerin-2Ya; GLMDTIKGVAKTVAASWLDKLKCKIT GC) inhibited the growth of E. coli (MIC = 50 μM) and S. aureus (MIC = 50 μM). In contrast to brevinin-1BLc, ranatuerin-2Ya showed appreciably greater cytolytic activity against HepG2 cells (LC₅₀ = 20 μM) than against erythrocytes (LC₅₀ > 100 μM).

Original language	English
Pages (from-to)	699-705
Number of pages	7
Journal	Toxicon
Volume	53
Issue number	7-8
DOIs	https://doi.org/10.1016/j.toxicon.2009.02.018
Publication status	Published - Jun 2009
Externally published	Yes

Keywords

Antimicrobial peptide
Brevinin-1
Frog skin
Lithobates
Ranatuerin-2

ASJC Scopus subject areas

Toxicology

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10.1016/j.toxicon.2009.02.018

Cite this

@article{4eff11a3308241dab9bd56d2c046e0c9,

title = "Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis",

abstract = "Six structurally similar and strongly cationic peptides belonging to the brevinin-1 family were isolated from skin secretions of the plains leopard frog Lithobates blairi and the lowland leopard frog Lithobates yavapaiensis on the basis of their antimicrobial activities. Brevinin-1BLc (FLPIIAGIAAKFLPKIFCTISKKC) from L. blairi represented the most potent peptide (MIC = 25 μM Escherichia coli, MIC = 1.5 μM Staphylococcus aureus, MIC = 3 μM Candida albicans, LC50 = 9 μM human erythrocytes and LC50 = 6 μM HepG2 human hepatoma-derived cells). The appreciably lower antimicrobial potencies of brevinin-1Ya and -1Yc from L. yavapaiensis correlate with the decreases in cationicity produced by the amino acid substitutions Lys11 → Asn (brevinin-1Ya) and Pro14 → Glu (brevinin-1Yc). In addition, a peptide isolated from the skin secretions of L. yavapaiensis belonging to the ranatuerin-2 family (ranatuerin-2Ya; GLMDTIKGVAKTVAASWLDKLKCKIT GC) inhibited the growth of E. coli (MIC = 50 μM) and S. aureus (MIC = 50 μM). In contrast to brevinin-1BLc, ranatuerin-2Ya showed appreciably greater cytolytic activity against HepG2 cells (LC50 = 20 μM) than against erythrocytes (LC50 > 100 μM).",

keywords = "Antimicrobial peptide, Brevinin-1, Frog skin, Lithobates, Ranatuerin-2",

author = "Conlon, \{J. Michael\} and Eman Ahmed and Laurent Coquet and Thierry Jouenne and J{\'e}r{\^o}me Leprince and Hubert Vaudry and King, \{Jay D.\}",

note = "Funding Information: 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 Prof. H. Raza, U.A.E University for a gift of Hep2G cells, and Annie John for technical assistance. The authors also thank Sandy Wilson, Nate Nelson, and Christopher Hutson, Sedgwick County Zoo and Stephane Poulin, Sonora Desert Museum for providing frog specimens. ",

year = "2009",

month = jun,

doi = "10.1016/j.toxicon.2009.02.018",

language = "English",

volume = "53",

pages = "699--705",

journal = "Toxicon",

issn = "0041-0101",

publisher = "Elsevier Ltd",

number = "7-8",

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TY - JOUR

T1 - Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis

AU - Conlon, J. Michael

AU - Ahmed, Eman

AU - Coquet, Laurent

AU - Jouenne, Thierry

AU - Leprince, Jérôme

AU - Vaudry, Hubert

AU - King, Jay D.

N1 - Funding Information: 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 Prof. H. Raza, U.A.E University for a gift of Hep2G cells, and Annie John for technical assistance. The authors also thank Sandy Wilson, Nate Nelson, and Christopher Hutson, Sedgwick County Zoo and Stephane Poulin, Sonora Desert Museum for providing frog specimens.

PY - 2009/6

Y1 - 2009/6

N2 - Six structurally similar and strongly cationic peptides belonging to the brevinin-1 family were isolated from skin secretions of the plains leopard frog Lithobates blairi and the lowland leopard frog Lithobates yavapaiensis on the basis of their antimicrobial activities. Brevinin-1BLc (FLPIIAGIAAKFLPKIFCTISKKC) from L. blairi represented the most potent peptide (MIC = 25 μM Escherichia coli, MIC = 1.5 μM Staphylococcus aureus, MIC = 3 μM Candida albicans, LC50 = 9 μM human erythrocytes and LC50 = 6 μM HepG2 human hepatoma-derived cells). The appreciably lower antimicrobial potencies of brevinin-1Ya and -1Yc from L. yavapaiensis correlate with the decreases in cationicity produced by the amino acid substitutions Lys11 → Asn (brevinin-1Ya) and Pro14 → Glu (brevinin-1Yc). In addition, a peptide isolated from the skin secretions of L. yavapaiensis belonging to the ranatuerin-2 family (ranatuerin-2Ya; GLMDTIKGVAKTVAASWLDKLKCKIT GC) inhibited the growth of E. coli (MIC = 50 μM) and S. aureus (MIC = 50 μM). In contrast to brevinin-1BLc, ranatuerin-2Ya showed appreciably greater cytolytic activity against HepG2 cells (LC50 = 20 μM) than against erythrocytes (LC50 > 100 μM).

AB - Six structurally similar and strongly cationic peptides belonging to the brevinin-1 family were isolated from skin secretions of the plains leopard frog Lithobates blairi and the lowland leopard frog Lithobates yavapaiensis on the basis of their antimicrobial activities. Brevinin-1BLc (FLPIIAGIAAKFLPKIFCTISKKC) from L. blairi represented the most potent peptide (MIC = 25 μM Escherichia coli, MIC = 1.5 μM Staphylococcus aureus, MIC = 3 μM Candida albicans, LC50 = 9 μM human erythrocytes and LC50 = 6 μM HepG2 human hepatoma-derived cells). The appreciably lower antimicrobial potencies of brevinin-1Ya and -1Yc from L. yavapaiensis correlate with the decreases in cationicity produced by the amino acid substitutions Lys11 → Asn (brevinin-1Ya) and Pro14 → Glu (brevinin-1Yc). In addition, a peptide isolated from the skin secretions of L. yavapaiensis belonging to the ranatuerin-2 family (ranatuerin-2Ya; GLMDTIKGVAKTVAASWLDKLKCKIT GC) inhibited the growth of E. coli (MIC = 50 μM) and S. aureus (MIC = 50 μM). In contrast to brevinin-1BLc, ranatuerin-2Ya showed appreciably greater cytolytic activity against HepG2 cells (LC50 = 20 μM) than against erythrocytes (LC50 > 100 μM).

KW - Antimicrobial peptide

KW - Brevinin-1

KW - Frog skin

KW - Lithobates

KW - Ranatuerin-2

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UR - https://www.scopus.com/pages/publications/67349214101#tab=citedBy

U2 - 10.1016/j.toxicon.2009.02.018

DO - 10.1016/j.toxicon.2009.02.018

M3 - Article

C2 - 19254736

AN - SCOPUS:67349214101

SN - 0041-0101

VL - 53

SP - 699

EP - 705

JO - Toxicon

JF - Toxicon

IS - 7-8

ER -

Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis

Abstract

Keywords

ASJC Scopus subject areas

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