Purification and characterization of antimicrobial peptides from the Caribbean frog, Leptodactylus validus (Anura: Leptodactylidae)

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

doi:10.1016/j.peptides.2008.04.005

Purification and characterization of antimicrobial peptides from the Caribbean frog, Leptodactylus validus (Anura: Leptodactylidae)

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

School of Biomedical Sciences

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

18 Citations (Scopus)

Abstract

Peptidomic analysis of norepinephrine-stimulated skin secretions from the Caribbean frog Leptodactylus validus Garman, 1888 led to the identification of three peptides with previously undescribed sequences that were structurally similar to those of antimicrobial peptides isolated from other species of leptodactylid frogs. These paralogs have been termed ocellatin-V1 (GVVDILKGAGKDLLAHALSKLSEKV.NH₂), ocellatin-V2 (GVLDILKGAGKDLLAHALSKISEKV.NH₂), and ocellatin-V3 (GVLDILTGAGKDLLAHALSKLSEKV.NH₂). The very low antimicrobial potency (MIC > 200 μM) against Escherichia coli and Staphylococcus aureus associated with the peptides is probably a consequence of their lack of amphipathicity and reduced cationicity compared with active members of the ocellatin family from related species.

Original language	English
Pages (from-to)	1287-1292
Number of pages	6
Journal	Peptides
Volume	29
Issue number	8
DOIs	https://doi.org/10.1016/j.peptides.2008.04.005
Publication status	Published (in print/issue) - Aug 2008

Keywords

Amphipathic α-helix
Antimicrobial
Frog skin
Ocellatin

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title = "Purification and characterization of antimicrobial peptides from the Caribbean frog, Leptodactylus validus (Anura: Leptodactylidae)",

abstract = "Peptidomic analysis of norepinephrine-stimulated skin secretions from the Caribbean frog Leptodactylus validus Garman, 1888 led to the identification of three peptides with previously undescribed sequences that were structurally similar to those of antimicrobial peptides isolated from other species of leptodactylid frogs. These paralogs have been termed ocellatin-V1 (GVVDILKGAGKDLLAHALSKLSEKV.NH2), ocellatin-V2 (GVLDILKGAGKDLLAHALSKISEKV.NH2), and ocellatin-V3 (GVLDILTGAGKDLLAHALSKLSEKV.NH2). The very low antimicrobial potency (MIC > 200 μM) against Escherichia coli and Staphylococcus aureus associated with the peptides is probably a consequence of their lack of amphipathicity and reduced cationicity compared with active members of the ocellatin family from related species.",

keywords = "Amphipathic α-helix, Antimicrobial, Frog skin, Ocellatin",

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

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AU - King, Jay D.

AU - Leprince, Jérôme

AU - Vaudry, Hubert

AU - Coquet, Laurent

AU - Jouenne, Thierry

AU - Conlon, J. Michael

PY - 2008/8

Y1 - 2008/8

N2 - Peptidomic analysis of norepinephrine-stimulated skin secretions from the Caribbean frog Leptodactylus validus Garman, 1888 led to the identification of three peptides with previously undescribed sequences that were structurally similar to those of antimicrobial peptides isolated from other species of leptodactylid frogs. These paralogs have been termed ocellatin-V1 (GVVDILKGAGKDLLAHALSKLSEKV.NH2), ocellatin-V2 (GVLDILKGAGKDLLAHALSKISEKV.NH2), and ocellatin-V3 (GVLDILTGAGKDLLAHALSKLSEKV.NH2). The very low antimicrobial potency (MIC > 200 μM) against Escherichia coli and Staphylococcus aureus associated with the peptides is probably a consequence of their lack of amphipathicity and reduced cationicity compared with active members of the ocellatin family from related species.

AB - Peptidomic analysis of norepinephrine-stimulated skin secretions from the Caribbean frog Leptodactylus validus Garman, 1888 led to the identification of three peptides with previously undescribed sequences that were structurally similar to those of antimicrobial peptides isolated from other species of leptodactylid frogs. These paralogs have been termed ocellatin-V1 (GVVDILKGAGKDLLAHALSKLSEKV.NH2), ocellatin-V2 (GVLDILKGAGKDLLAHALSKISEKV.NH2), and ocellatin-V3 (GVLDILTGAGKDLLAHALSKLSEKV.NH2). The very low antimicrobial potency (MIC > 200 μM) against Escherichia coli and Staphylococcus aureus associated with the peptides is probably a consequence of their lack of amphipathicity and reduced cationicity compared with active members of the ocellatin family from related species.

KW - Amphipathic α-helix

KW - Antimicrobial

KW - Frog skin

KW - Ocellatin

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DO - 10.1016/j.peptides.2008.04.005

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SN - 0196-9781

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JO - Peptides

JF - Peptides

IS - 8

ER -

Purification and characterization of antimicrobial peptides from the Caribbean frog, Leptodactylus validus (Anura: Leptodactylidae)

Abstract

Keywords

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