Histamine-releasing and antimicrobial peptides from the skin secretions of the dusky gopher frog, Rana sevosa

Graham, Ciaren and Richter, Stephen C. and McClean, Stephen and O’Kane, Edmund and Flatt, Peter R. and Shaw, Chris (2006) Histamine-releasing and antimicrobial peptides from the skin secretions of the dusky gopher frog, Rana sevosa. Peptides, 27` (6). pp. 1313-1319. ISSN 0196-9781

Full content URL: http://dx.doi.org/10.1016/j.peptides.2005.11.021

Full text not available from this repository.

Item Type:Article
Item Status:Live Archive

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.

Additional Information: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.
Keywords:Antimicrobial, Peptides, Mass Spectrometry, Histamine, Rana sevosa, HPLC
Subjects:C Biological Sciences > C510 Applied Microbiology
C Biological Sciences > C560 Biotechnology
Divisions:College of Science > School of Life Sciences
ID Code:7333
Deposited On:22 Jan 2013 14:39

Repository Staff Only: item control page