Identification and functional analysis of a novel bradykinin inhibitory peptide in the venoms of New World Crotalinae pit vipers

A novel undecapeptide has been isolated and structurally characterized from the venoms of three species of New World pit vipers from the subfamily, Crotalinae. These include the Mexican moccasin ( Agkistrodon bilineatus), the prairie rattlesnake ( Crotalus viridis viridis), and the South American bu...

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Bibliographic Details
Published in:	Biochemical and biophysical research communications 2005-12, Vol.338 (3), p.1587-1592
Main Authors:	James Graham, Robert Leslie, Graham, Ciaren, McClean, Stephen, Chen, Tianbao, O’Rourke, Martin, Hirst, David, Theakston, David, Shaw, Chris
Format:	Article
Language:	eng
Subjects:	Amino Acid Sequence Animals Bradykinin Bradykinin - antagonists & inhibitors Bradykinin - metabolism Chromatography, Gel Chromatography, High Pressure Liquid Crotalid Venoms - chemistry Male Mass spectrometry Molecular Sequence Data Peptide Peptides - chemistry Peptides - isolation & purification Peptides - pharmacology Rats Rats, Wistar Snake venom Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Tail - drug effects Vasoconstriction Viperidae
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Summary:	A novel undecapeptide has been isolated and structurally characterized from the venoms of three species of New World pit vipers from the subfamily, Crotalinae. These include the Mexican moccasin ( Agkistrodon bilineatus), the prairie rattlesnake ( Crotalus viridis viridis), and the South American bushmaster ( Lachesis muta). The peptide was purified from all three venoms using a combination of gel permeation chromatography and reverse-phase HPLC. Automated Edman degradation sequencing and MALDI-TOF mass spectrometry established its peptide primary structure as: Thr-Pro-Pro-Ala-Gly-Pro-Asp-Val-Gly-Pro-Arg-OH, with a non-protonated molecular mass of 1063.18 Da. A synthetic replicate of the peptide was found to be an antagonist of bradykinin action at the rat vascular B2 receptor. This is the first bradykinin inhibitory peptide isolated from snake venom. Database searching revealed the peptide to be highly structurally related (10/11 residues) with a domain residing between the bradykinin-potentiating peptide and C-type natriuretic peptide domains of a recently cloned precursor from tropical rattlesnake ( Crotalus durissus terrificus) venom gland. BIP thus represents a novel biological entity from snake venom.
ISSN:	0006-291X 1090-2104