Genetic Basis for Variation of Metalloproteinase-Associated Biochemical Activity in Venom of the Mojave Rattlesnake (Crotalus scutulatus scutulatus)

The metalloproteinase composition and biochemical profiles of rattlesnake venom can be highly variable among rattlesnakes of the same species. We have previously shown that the neurotoxic properties of the Mojave rattlesnake (Crotalus scutulatus scutulatus) are associated with the presence of the Mo...

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Main Authors: Ruben K. Dagda, Sardar Gasanov, Ysidro De La OIII, Eppie D. Rael, Carl S. Lieb
Format: Article
Language:English
Published: Wiley 2013-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2013/251474
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author Ruben K. Dagda
Sardar Gasanov
Ysidro De La OIII
Eppie D. Rael
Carl S. Lieb
author_facet Ruben K. Dagda
Sardar Gasanov
Ysidro De La OIII
Eppie D. Rael
Carl S. Lieb
author_sort Ruben K. Dagda
collection DOAJ
description The metalloproteinase composition and biochemical profiles of rattlesnake venom can be highly variable among rattlesnakes of the same species. We have previously shown that the neurotoxic properties of the Mojave rattlesnake (Crotalus scutulatus scutulatus) are associated with the presence of the Mojave toxin A subunit suggesting the existence of a genetic basis for rattlesnake venom composition. In this report, we hypothesized the existence of a genetic basis for intraspecies variation in metalloproteinase-associated biochemical properties of rattlesnake venom of the Mojave rattlesnake. To address this question, we PCR-amplified and compared the genomic DNA nucleotide sequences that code for the mature metalloproteinase domain of fourteen Mojave rattlesnakes captured from different geographical locations across the southwest region of the United States. In addition, the venoms from the same rattlesnakes were tested for their ability to hydrolyze fibrinogen, fibrin, casein, and hide powder azure and for induction of hemorrhage in mice. Overall, based on genomic sequencing and biochemical data, we classified Mojave rattlesnake venom into four distinct groups of metalloproteinases. These findings indicate that differences in nucleotide sequences encoding the mature proteinase domain and noncoding regions contribute to differences in venom metalloproteinase activities among rattlesnakes of the same species.
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spelling doaj-art-ee98dbb94593484e817071ccd394874f2025-02-03T05:59:52ZengWileyBiochemistry Research International2090-22472090-22552013-01-01201310.1155/2013/251474251474Genetic Basis for Variation of Metalloproteinase-Associated Biochemical Activity in Venom of the Mojave Rattlesnake (Crotalus scutulatus scutulatus)Ruben K. Dagda0Sardar Gasanov1Ysidro De La OIII2Eppie D. Rael3Carl S. Lieb4Pharmacology Department, University of Nevada School of Medicine, Manville Building 19A, Reno, NV 89557, USAScience Department, Tashkent Ulugbek International School, 5-A J. Shoshiy Street, 100100 Tashkent, UzbekistanDepartment of Biological Sciences, University of Texas at El Paso, 500 West University Avenue, El Paso, TX 79968, USADepartment of Biological Sciences, University of Texas at El Paso, 500 West University Avenue, El Paso, TX 79968, USADepartment of Biological Sciences, University of Texas at El Paso, 500 West University Avenue, El Paso, TX 79968, USAThe metalloproteinase composition and biochemical profiles of rattlesnake venom can be highly variable among rattlesnakes of the same species. We have previously shown that the neurotoxic properties of the Mojave rattlesnake (Crotalus scutulatus scutulatus) are associated with the presence of the Mojave toxin A subunit suggesting the existence of a genetic basis for rattlesnake venom composition. In this report, we hypothesized the existence of a genetic basis for intraspecies variation in metalloproteinase-associated biochemical properties of rattlesnake venom of the Mojave rattlesnake. To address this question, we PCR-amplified and compared the genomic DNA nucleotide sequences that code for the mature metalloproteinase domain of fourteen Mojave rattlesnakes captured from different geographical locations across the southwest region of the United States. In addition, the venoms from the same rattlesnakes were tested for their ability to hydrolyze fibrinogen, fibrin, casein, and hide powder azure and for induction of hemorrhage in mice. Overall, based on genomic sequencing and biochemical data, we classified Mojave rattlesnake venom into four distinct groups of metalloproteinases. These findings indicate that differences in nucleotide sequences encoding the mature proteinase domain and noncoding regions contribute to differences in venom metalloproteinase activities among rattlesnakes of the same species.http://dx.doi.org/10.1155/2013/251474
spellingShingle Ruben K. Dagda
Sardar Gasanov
Ysidro De La OIII
Eppie D. Rael
Carl S. Lieb
Genetic Basis for Variation of Metalloproteinase-Associated Biochemical Activity in Venom of the Mojave Rattlesnake (Crotalus scutulatus scutulatus)
Biochemistry Research International
title Genetic Basis for Variation of Metalloproteinase-Associated Biochemical Activity in Venom of the Mojave Rattlesnake (Crotalus scutulatus scutulatus)
title_full Genetic Basis for Variation of Metalloproteinase-Associated Biochemical Activity in Venom of the Mojave Rattlesnake (Crotalus scutulatus scutulatus)
title_fullStr Genetic Basis for Variation of Metalloproteinase-Associated Biochemical Activity in Venom of the Mojave Rattlesnake (Crotalus scutulatus scutulatus)
title_full_unstemmed Genetic Basis for Variation of Metalloproteinase-Associated Biochemical Activity in Venom of the Mojave Rattlesnake (Crotalus scutulatus scutulatus)
title_short Genetic Basis for Variation of Metalloproteinase-Associated Biochemical Activity in Venom of the Mojave Rattlesnake (Crotalus scutulatus scutulatus)
title_sort genetic basis for variation of metalloproteinase associated biochemical activity in venom of the mojave rattlesnake crotalus scutulatus scutulatus
url http://dx.doi.org/10.1155/2013/251474
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