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Special Issue "Snake Venoms"

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A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: closed (15 September 2011)

Special Issue Editor

Guest Editor
Dr. Ken Winkel

University of Melbourne, Australia
Website | E-Mail
Fax: +61 3 9348 2048
Interests: clinical effects of animal venoms and effectiveness of antivenoms; global health; history of venom research; research translation; popular culture and venoms/venomous creatures; the study of animal venoms and toxins; toxinology; biodiversity and medicine

Published Papers (3 papers)

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Research

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Open AccessArticle Molecular Conversion of Muscarinic Acetylcholine Receptor M5 to Muscarinic Toxin 7 (MT7)-Binding Protein
Toxins 2011, 3(11), 1393-1404; doi:10.3390/toxins3111393
Received: 19 September 2011 / Revised: 11 October 2011 / Accepted: 3 November 2011 / Published: 11 November 2011
Cited by 2 | PDF Full-text (971 KB) | HTML Full-text | XML Full-text
Abstract
Muscarinic toxin 7 (MT7) is a mamba venom peptide that binds selectively to the M1 muscarinic acetylcholine receptor. We have previously shown that the second (ECL2) and third (ECL3) extracellular loops of the M1 receptor are critically involved in binding the
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Muscarinic toxin 7 (MT7) is a mamba venom peptide that binds selectively to the M1 muscarinic acetylcholine receptor. We have previously shown that the second (ECL2) and third (ECL3) extracellular loops of the M1 receptor are critically involved in binding the peptide. In this study we used a mutagenesis approach on the M5 subtype of the receptor family to find out if this possesses a similar structural architecture in terms of toxin binding as the M1 receptor. An M5 receptor construct (M5-E175Y184E474), mutated at the formerly deciphered critical residues on ECL2 and 3, gained the ability to bind MT7, but with rather low affinity as determined in a functional assay (apparent Ki = 24 nM; apparent Ki for M1 = 0.5 nM). After screening for different domains and residues, we found a specific residue (P179 to L in M5) in the middle portion of ECL2 that was necessary for high affinity binding of MT7 (M5-EL179YE, apparent Ki = 0.5 nM). Mutation of P179 to A confirmed a role for the leucine side chain in the binding of MT7. Together the results reveal new binding interactions between receptors and the MT7 peptide and strengthen the hypothesis that ECL2 sequence is of utmost importance for MT binding to muscarinic receptors. Full article
(This article belongs to the Special Issue Snake Venoms)
Open AccessArticle Molecular Analysis of the Interaction of the Snake Venom Rhodocytin with the Platelet Receptor CLEC-2
Toxins 2011, 3(8), 991-1003; doi:10.3390/toxins3080991
Received: 6 July 2011 / Revised: 21 July 2011 / Accepted: 8 August 2011 / Published: 10 August 2011
Cited by 3 | PDF Full-text (687 KB) | HTML Full-text | XML Full-text
Abstract
The Malayan pit viper, Calloselasma rhodostoma, produces a potent venom toxin, rhodocytin (aggretin) which causes platelet aggregation. Rhodocytin is a ligand for the receptor CLEC-2 on the surface of platelets. The interaction of these two molecules initiates a signaling pathway which results
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The Malayan pit viper, Calloselasma rhodostoma, produces a potent venom toxin, rhodocytin (aggretin) which causes platelet aggregation. Rhodocytin is a ligand for the receptor CLEC-2 on the surface of platelets. The interaction of these two molecules initiates a signaling pathway which results in platelet activation and aggregation. We have previously solved the crystal structures of CLEC-2 and of rhodocytin, and have proposed models by which tetrameric rhodocytin may interact with either two monomers of CLEC-2, or with one or two copies of dimeric CLEC-2. In the current study we use a range of approaches to analyze the molecular interfaces and dynamics involved in the models of the interaction of rhodocytin with either one or two copies of dimeric CLEC-2, and their implications for clustering of CLEC-2 on the platelet surface. Full article
(This article belongs to the Special Issue Snake Venoms)
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Review

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Open AccessReview Pharmacological Aspects of Vipera xantina palestinae Venom
Toxins 2011, 3(11), 1420-1432; doi:10.3390/toxins3111420
Received: 14 September 2011 / Revised: 3 October 2011 / Accepted: 1 November 2011 / Published: 14 November 2011
Cited by 8 | PDF Full-text (665 KB) | HTML Full-text | XML Full-text
Abstract
In Israel, Vipera xantina palestinae (V.x.p.) is the most common venomous snake, accounting for several hundred cases of envenomation in humans and domestic animals every year, with a mortality rate of 0.5 to 2%. In this review we will briefly address
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In Israel, Vipera xantina palestinae (V.x.p.) is the most common venomous snake, accounting for several hundred cases of envenomation in humans and domestic animals every year, with a mortality rate of 0.5 to 2%. In this review we will briefly address the research developments relevant to our present understanding of the structure and function of V.x.p. venom with emphasis on venom disintegrins. Venom proteomics indicated the presence of four families of pharmacologically active compounds: (i) neurotoxins; (ii) hemorrhagins; (iii) angioneurin growth factors; and (iv) different types of integrin inhibitors. Viperistatin, a α1β1selective KTS disintegrin and VP12, a α2β1 selective C-type lectin were discovered. These snake venom proteins represent promising tools for research and development of novel collagen receptor selective drugs. These discoveries are also relevant for future improvement of antivenom therapy towards V.x.p. envenomation. Full article
(This article belongs to the Special Issue Snake Venoms)

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