Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae)

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

doi:10.1016/j.cbpc.2009.04.003

Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae)

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

Department of Biochemistry

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

16 Citations (Scopus)

Abstract

Peptide-based defenses of ranid frogs from Mexico and Central America have been studied in much less detail than those from North America. Peptides belonging to the brevinin-1 (5 peptides), palustrin-2 (1 peptide), and ranatuerin-2 (3 peptides) families were isolated from norepinephrine-stimulated skin secretions of the Costa Rican frog, Lithobates vaillanti (Ranidae) and characterized structurally. Brevinin-1VLa (FLGAIAGVAAKFLPKVFCFITKKC) and brevinin-1VLc (FLPVIASVAAKVLPK VFCFITKKC) showed particularly high growth-inhibitory potency (MIC ≤ 3 μM) against a Gram-positive microorganism Staphylococcus aureus and the opportunistic yeast pathogen Candida albicans and potent cytolytic activity (LC₅₀ ≤ 8 μM) against both human erythrocytes and HepG2 hepatoma-derived cells. The peptides were also active against a Gram-negative microorganism Escherichia coli (MIC ≤ 50 μM). Substitutions in brevinin-1VLd (Lys¹¹ → Asn) and brevinin-1VLe (Lys¹¹ → Ser) that decrease cationicity result in loss of activity against E. coli. Ranatuerin-2VLb (GIMDTIKGAAKDLAGQLLDKLKCKITKC) showed relatively weak antimicrobial activity (MIC ≥ 75 μM) but selective cytolytic activity against HepG2 tumor cells (LC₅₀ = 30 μM) compared with erythrocytes (LC₅₀ > 200 μM). In addition, a dodecapeptide (RICYAMWIPYPC) were isolated from the secretions that were devoid of antimicrobial activity. This component contains an Ala-Met bond that constitutes the scissile bond in the selective elastase inhibitor, elafin but the peptide did not inhibit pancreatic elastase at concentrations up to 100 μM.

Original language	English
Pages (from-to)	150-154
Number of pages	5
Journal	Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
Volume	150
Issue number	2
DOIs	https://doi.org/10.1016/j.cbpc.2009.04.003
Publication status	Published - Aug 2009

Keywords

Antimicrobial peptide
Brevinin-1
Lithobates
Palustrin-2
Ranatuerin-2

ASJC Scopus subject areas

Biochemistry
Physiology
Aquatic Science
Animal Science and Zoology
Toxicology
Cell Biology
Health, Toxicology and Mutagenesis

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10.1016/j.cbpc.2009.04.003

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Conlon, J. M., Raza, H., Coquet, L., Jouenne, T., Leprince, J., Vaudry, H., & King, J. D. (2009). Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae). Comparative Biochemistry and Physiology - C Toxicology and Pharmacology, 150(2), 150-154. https://doi.org/10.1016/j.cbpc.2009.04.003

Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae). / Conlon, J. Michael; Raza, Haider; Coquet, Laurent et al.

In: Comparative Biochemistry and Physiology - C Toxicology and Pharmacology, Vol. 150, No. 2, 08.2009, p. 150-154.

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

Conlon, JM, Raza, H, Coquet, L, Jouenne, T, Leprince, J, Vaudry, H & King, JD 2009, 'Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae)', Comparative Biochemistry and Physiology - C Toxicology and Pharmacology, vol. 150, no. 2, pp. 150-154. https://doi.org/10.1016/j.cbpc.2009.04.003

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title = "Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae)",

abstract = "Peptide-based defenses of ranid frogs from Mexico and Central America have been studied in much less detail than those from North America. Peptides belonging to the brevinin-1 (5 peptides), palustrin-2 (1 peptide), and ranatuerin-2 (3 peptides) families were isolated from norepinephrine-stimulated skin secretions of the Costa Rican frog, Lithobates vaillanti (Ranidae) and characterized structurally. Brevinin-1VLa (FLGAIAGVAAKFLPKVFCFITKKC) and brevinin-1VLc (FLPVIASVAAKVLPK VFCFITKKC) showed particularly high growth-inhibitory potency (MIC ≤ 3 μM) against a Gram-positive microorganism Staphylococcus aureus and the opportunistic yeast pathogen Candida albicans and potent cytolytic activity (LC50 ≤ 8 μM) against both human erythrocytes and HepG2 hepatoma-derived cells. The peptides were also active against a Gram-negative microorganism Escherichia coli (MIC ≤ 50 μM). Substitutions in brevinin-1VLd (Lys11 → Asn) and brevinin-1VLe (Lys11 → Ser) that decrease cationicity result in loss of activity against E. coli. Ranatuerin-2VLb (GIMDTIKGAAKDLAGQLLDKLKCKITKC) showed relatively weak antimicrobial activity (MIC ≥ 75 μM) but selective cytolytic activity against HepG2 tumor cells (LC50 = 30 μM) compared with erythrocytes (LC50 > 200 μM). In addition, a dodecapeptide (RICYAMWIPYPC) were isolated from the secretions that were devoid of antimicrobial activity. This component contains an Ala-Met bond that constitutes the scissile bond in the selective elastase inhibitor, elafin but the peptide did not inhibit pancreatic elastase at concentrations up to 100 μM.",

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

author = "Conlon, {J. Michael} and Haider Raza 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 UAE University. The authors thank Ms Eman Ahmed and Ms Annie John for technical assistance. The authors also thank Brian Kubicki, Costa Rican Amphibian Research Center for providing frog specimens.",

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doi = "10.1016/j.cbpc.2009.04.003",

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AU - Conlon, J. Michael

AU - Raza, Haider

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 UAE University. The authors thank Ms Eman Ahmed and Ms Annie John for technical assistance. The authors also thank Brian Kubicki, Costa Rican Amphibian Research Center for providing frog specimens.

PY - 2009/8

Y1 - 2009/8

N2 - Peptide-based defenses of ranid frogs from Mexico and Central America have been studied in much less detail than those from North America. Peptides belonging to the brevinin-1 (5 peptides), palustrin-2 (1 peptide), and ranatuerin-2 (3 peptides) families were isolated from norepinephrine-stimulated skin secretions of the Costa Rican frog, Lithobates vaillanti (Ranidae) and characterized structurally. Brevinin-1VLa (FLGAIAGVAAKFLPKVFCFITKKC) and brevinin-1VLc (FLPVIASVAAKVLPK VFCFITKKC) showed particularly high growth-inhibitory potency (MIC ≤ 3 μM) against a Gram-positive microorganism Staphylococcus aureus and the opportunistic yeast pathogen Candida albicans and potent cytolytic activity (LC50 ≤ 8 μM) against both human erythrocytes and HepG2 hepatoma-derived cells. The peptides were also active against a Gram-negative microorganism Escherichia coli (MIC ≤ 50 μM). Substitutions in brevinin-1VLd (Lys11 → Asn) and brevinin-1VLe (Lys11 → Ser) that decrease cationicity result in loss of activity against E. coli. Ranatuerin-2VLb (GIMDTIKGAAKDLAGQLLDKLKCKITKC) showed relatively weak antimicrobial activity (MIC ≥ 75 μM) but selective cytolytic activity against HepG2 tumor cells (LC50 = 30 μM) compared with erythrocytes (LC50 > 200 μM). In addition, a dodecapeptide (RICYAMWIPYPC) were isolated from the secretions that were devoid of antimicrobial activity. This component contains an Ala-Met bond that constitutes the scissile bond in the selective elastase inhibitor, elafin but the peptide did not inhibit pancreatic elastase at concentrations up to 100 μM.

AB - Peptide-based defenses of ranid frogs from Mexico and Central America have been studied in much less detail than those from North America. Peptides belonging to the brevinin-1 (5 peptides), palustrin-2 (1 peptide), and ranatuerin-2 (3 peptides) families were isolated from norepinephrine-stimulated skin secretions of the Costa Rican frog, Lithobates vaillanti (Ranidae) and characterized structurally. Brevinin-1VLa (FLGAIAGVAAKFLPKVFCFITKKC) and brevinin-1VLc (FLPVIASVAAKVLPK VFCFITKKC) showed particularly high growth-inhibitory potency (MIC ≤ 3 μM) against a Gram-positive microorganism Staphylococcus aureus and the opportunistic yeast pathogen Candida albicans and potent cytolytic activity (LC50 ≤ 8 μM) against both human erythrocytes and HepG2 hepatoma-derived cells. The peptides were also active against a Gram-negative microorganism Escherichia coli (MIC ≤ 50 μM). Substitutions in brevinin-1VLd (Lys11 → Asn) and brevinin-1VLe (Lys11 → Ser) that decrease cationicity result in loss of activity against E. coli. Ranatuerin-2VLb (GIMDTIKGAAKDLAGQLLDKLKCKITKC) showed relatively weak antimicrobial activity (MIC ≥ 75 μM) but selective cytolytic activity against HepG2 tumor cells (LC50 = 30 μM) compared with erythrocytes (LC50 > 200 μM). In addition, a dodecapeptide (RICYAMWIPYPC) were isolated from the secretions that were devoid of antimicrobial activity. This component contains an Ala-Met bond that constitutes the scissile bond in the selective elastase inhibitor, elafin but the peptide did not inhibit pancreatic elastase at concentrations up to 100 μM.

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KW - Lithobates

KW - Palustrin-2

KW - Ranatuerin-2

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Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae)

Abstract

Keywords

ASJC Scopus subject areas

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