Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura

Ranidae)

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

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Peptidomic analysis of norepinephrine-stimulated skin secretions from Hose's rock frog Odorrana hosii (Boulenger, 1891) led to the isolation of 8 peptides with differential antibacterial activities. Structural characterization demonstrated that the peptides belonged to the esculentin-1 (1 peptide), esculentin-2 (1 peptide), brevinin-1 (2 peptides), brevinin-2 (2 peptides), and nigrocin-2 (2 peptides) families of antimicrobial peptides. Similar analysis of skin secretions from the Malaysian fire frog Hylarana picturata (Boulenger, 1920) led to the isolation and characterization of peptides belonging to the brevinin-1 (2 peptides), brevinin-2 (5 peptides), and temporin (1 peptide) families. The differences in antimicrobial activities of paralogous peptides provide insight into structure-activity relationships, emphasizing the importance of cationicity in determining potency. The substitution Lys11 → Gln in brevinin-1HSa (FLPAVLRVAAKIVPTVFCAISKKC) from O. hosii abolishes growth inhibitory activity against Escherichia coli but has no effect on the high potency (MIC = 8 μg/ml) against Staphylococcus aureus. In contrast, the substitution (Gly4 → Asp) in brevinin-2PTb (GFKGAFKNVMFGIAKSAGKSALNALACKIDKSC) from H. picturata reduces activity against both E. coli and S. aureus. Cladistic analysis based upon the amino acid sequences of the brevinin-2 peptides from Asian frogs provides evidence for sister taxon relationships between O. hosii and O. livida and between H. picturata and H. güntheri.

Original languageEnglish
Pages (from-to)465-473
Number of pages9
JournalToxicon
Volume52
Issue number3
DOIs
Publication statusPublished - Sep 1 2008

Fingerprint

Ranidae
Anura
Skin
Peptides
Escherichia coli
Staphylococcus aureus
Substitution reactions
Hose
Structure-Activity Relationship
Viperidae

Keywords

  • Antimicrobial peptide
  • Brevinin
  • Esculentin
  • Frog skin
  • Nigrocin
  • Phylogeny

ASJC Scopus subject areas

  • Toxicology

Cite this

Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura : Ranidae). / Conlon, J. Michael; Kolodziejek, Jolanta; Nowotny, Norbert; Leprince, Jérôme; Vaudry, Hubert; Coquet, Laurent; Jouenne, Thierry; King, Jay D.

In: Toxicon, Vol. 52, No. 3, 01.09.2008, p. 465-473.

Research output: Contribution to journalArticle

Conlon, J. Michael ; Kolodziejek, Jolanta ; Nowotny, Norbert ; Leprince, Jérôme ; Vaudry, Hubert ; Coquet, Laurent ; Jouenne, Thierry ; King, Jay D. / Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura : Ranidae). In: Toxicon. 2008 ; Vol. 52, No. 3. pp. 465-473.
@article{5c6b37015fd74ca39f2b2c508bcb8027,
title = "Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura: Ranidae)",
abstract = "Peptidomic analysis of norepinephrine-stimulated skin secretions from Hose's rock frog Odorrana hosii (Boulenger, 1891) led to the isolation of 8 peptides with differential antibacterial activities. Structural characterization demonstrated that the peptides belonged to the esculentin-1 (1 peptide), esculentin-2 (1 peptide), brevinin-1 (2 peptides), brevinin-2 (2 peptides), and nigrocin-2 (2 peptides) families of antimicrobial peptides. Similar analysis of skin secretions from the Malaysian fire frog Hylarana picturata (Boulenger, 1920) led to the isolation and characterization of peptides belonging to the brevinin-1 (2 peptides), brevinin-2 (5 peptides), and temporin (1 peptide) families. The differences in antimicrobial activities of paralogous peptides provide insight into structure-activity relationships, emphasizing the importance of cationicity in determining potency. The substitution Lys11 → Gln in brevinin-1HSa (FLPAVLRVAAKIVPTVFCAISKKC) from O. hosii abolishes growth inhibitory activity against Escherichia coli but has no effect on the high potency (MIC = 8 μg/ml) against Staphylococcus aureus. In contrast, the substitution (Gly4 → Asp) in brevinin-2PTb (GFKGAFKNVMFGIAKSAGKSALNALACKIDKSC) from H. picturata reduces activity against both E. coli and S. aureus. Cladistic analysis based upon the amino acid sequences of the brevinin-2 peptides from Asian frogs provides evidence for sister taxon relationships between O. hosii and O. livida and between H. picturata and H. g{\"u}ntheri.",
keywords = "Antimicrobial peptide, Brevinin, Esculentin, Frog skin, Nigrocin, Phylogeny",
author = "Conlon, {J. Michael} and Jolanta Kolodziejek and Norbert Nowotny and J{\'e}r{\^o}me Leprince and Hubert Vaudry and Laurent Coquet and Thierry Jouenne and King, {Jay D.}",
year = "2008",
month = "9",
day = "1",
doi = "10.1016/j.toxicon.2008.06.017",
language = "English",
volume = "52",
pages = "465--473",
journal = "Toxicon",
issn = "0041-0101",
publisher = "Elsevier Limited",
number = "3",

}

TY - JOUR

T1 - Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura

T2 - Ranidae)

AU - Conlon, J. Michael

AU - Kolodziejek, Jolanta

AU - Nowotny, Norbert

AU - Leprince, Jérôme

AU - Vaudry, Hubert

AU - Coquet, Laurent

AU - Jouenne, Thierry

AU - King, Jay D.

PY - 2008/9/1

Y1 - 2008/9/1

N2 - Peptidomic analysis of norepinephrine-stimulated skin secretions from Hose's rock frog Odorrana hosii (Boulenger, 1891) led to the isolation of 8 peptides with differential antibacterial activities. Structural characterization demonstrated that the peptides belonged to the esculentin-1 (1 peptide), esculentin-2 (1 peptide), brevinin-1 (2 peptides), brevinin-2 (2 peptides), and nigrocin-2 (2 peptides) families of antimicrobial peptides. Similar analysis of skin secretions from the Malaysian fire frog Hylarana picturata (Boulenger, 1920) led to the isolation and characterization of peptides belonging to the brevinin-1 (2 peptides), brevinin-2 (5 peptides), and temporin (1 peptide) families. The differences in antimicrobial activities of paralogous peptides provide insight into structure-activity relationships, emphasizing the importance of cationicity in determining potency. The substitution Lys11 → Gln in brevinin-1HSa (FLPAVLRVAAKIVPTVFCAISKKC) from O. hosii abolishes growth inhibitory activity against Escherichia coli but has no effect on the high potency (MIC = 8 μg/ml) against Staphylococcus aureus. In contrast, the substitution (Gly4 → Asp) in brevinin-2PTb (GFKGAFKNVMFGIAKSAGKSALNALACKIDKSC) from H. picturata reduces activity against both E. coli and S. aureus. Cladistic analysis based upon the amino acid sequences of the brevinin-2 peptides from Asian frogs provides evidence for sister taxon relationships between O. hosii and O. livida and between H. picturata and H. güntheri.

AB - Peptidomic analysis of norepinephrine-stimulated skin secretions from Hose's rock frog Odorrana hosii (Boulenger, 1891) led to the isolation of 8 peptides with differential antibacterial activities. Structural characterization demonstrated that the peptides belonged to the esculentin-1 (1 peptide), esculentin-2 (1 peptide), brevinin-1 (2 peptides), brevinin-2 (2 peptides), and nigrocin-2 (2 peptides) families of antimicrobial peptides. Similar analysis of skin secretions from the Malaysian fire frog Hylarana picturata (Boulenger, 1920) led to the isolation and characterization of peptides belonging to the brevinin-1 (2 peptides), brevinin-2 (5 peptides), and temporin (1 peptide) families. The differences in antimicrobial activities of paralogous peptides provide insight into structure-activity relationships, emphasizing the importance of cationicity in determining potency. The substitution Lys11 → Gln in brevinin-1HSa (FLPAVLRVAAKIVPTVFCAISKKC) from O. hosii abolishes growth inhibitory activity against Escherichia coli but has no effect on the high potency (MIC = 8 μg/ml) against Staphylococcus aureus. In contrast, the substitution (Gly4 → Asp) in brevinin-2PTb (GFKGAFKNVMFGIAKSAGKSALNALACKIDKSC) from H. picturata reduces activity against both E. coli and S. aureus. Cladistic analysis based upon the amino acid sequences of the brevinin-2 peptides from Asian frogs provides evidence for sister taxon relationships between O. hosii and O. livida and between H. picturata and H. güntheri.

KW - Antimicrobial peptide

KW - Brevinin

KW - Esculentin

KW - Frog skin

KW - Nigrocin

KW - Phylogeny

UR - http://www.scopus.com/inward/record.url?scp=50549092676&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=50549092676&partnerID=8YFLogxK

U2 - 10.1016/j.toxicon.2008.06.017

DO - 10.1016/j.toxicon.2008.06.017

M3 - Article

VL - 52

SP - 465

EP - 473

JO - Toxicon

JF - Toxicon

SN - 0041-0101

IS - 3

ER -