Histamine-releasing and antimicrobial peptides from the skin secretions of the Dusky Gopher frog, Rana sevosa

C Graham, SC Richter, Stephen McClean, E O'Kane, Peter Flatt, C Shaw

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Seven novel peptides were isolated from the skin secretions of the North American dusky gopher frog, Rana sevosa, on the basis of antimicrobial activity and histamine release from rat peritoneal mast cells. The peptides were purified to homogeneity using HPLC and characterized by electrospray ion-trap mass spectrometry, MALDI-TOF mass spectrometry and Edman sequencing. Bioinformatic analysis of primary structures revealed that the novel peptides could be assigned to four established families of ranid frog antimicrobial peptides, namely esculentin-1, esculentin-2, brevinin-1 and ranatuerin-2. The peptides were named in accordance with accepted terminology as ranatuerin 2SEa, etc., reflecting the peptide family name, the species of origin (SE for sevosa) and the isotype (a). Of major interest was the fact that brevinin 1SE displayed significant structural similarity to ponericin W5, an antibacterial venom peptide from the ant; Pachyconyla goeldii. This is a further example of amphibian skin defensive peptides showing striking structural similarities to peptides from insects. These data may shed some light on the functional biological relevance of defensive peptides that possess both antimicrobial and histamine-releasing activities. (c) 2005 Elsevier Inc. All rights reserved.
LanguageEnglish
Pages1313-1319
JournalPeptides
Volume27
Issue number6
DOIs
Publication statusPublished - Jun 2006

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Histamine
Skin
Peptides
Mass spectrometry
Venoms
Bioinformatics
Terminology
Rats
Ions

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title = "Histamine-releasing and antimicrobial peptides from the skin secretions of the Dusky Gopher frog, Rana sevosa",
abstract = "Seven novel peptides were isolated from the skin secretions of the North American dusky gopher frog, Rana sevosa, on the basis of antimicrobial activity and histamine release from rat peritoneal mast cells. The peptides were purified to homogeneity using HPLC and characterized by electrospray ion-trap mass spectrometry, MALDI-TOF mass spectrometry and Edman sequencing. Bioinformatic analysis of primary structures revealed that the novel peptides could be assigned to four established families of ranid frog antimicrobial peptides, namely esculentin-1, esculentin-2, brevinin-1 and ranatuerin-2. The peptides were named in accordance with accepted terminology as ranatuerin 2SEa, etc., reflecting the peptide family name, the species of origin (SE for sevosa) and the isotype (a). Of major interest was the fact that brevinin 1SE displayed significant structural similarity to ponericin W5, an antibacterial venom peptide from the ant; Pachyconyla goeldii. This is a further example of amphibian skin defensive peptides showing striking structural similarities to peptides from insects. These data may shed some light on the functional biological relevance of defensive peptides that possess both antimicrobial and histamine-releasing activities. (c) 2005 Elsevier Inc. All rights reserved.",
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Histamine-releasing and antimicrobial peptides from the skin secretions of the Dusky Gopher frog, Rana sevosa. / Graham, C; Richter, SC; McClean, Stephen; O'Kane, E; Flatt, Peter; Shaw, C.

In: Peptides, Vol. 27, No. 6, 06.2006, p. 1313-1319.

Research output: Contribution to journalArticle

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