Literature DB >> 24522289

Molecular models of the Mojave rattlesnake (Crotalus scutulatus scutulatus) venom metalloproteinases reveal a structural basis for differences in hemorrhagic activities.

Ruben K Dagda1, Sardar E Gasanov, Boris Zhang, William Welch, Eppie D Rael.   

Abstract

Rattlesnake venom can differ in composition and in metalloproteinase-associated activities. The molecular basis for this intra-species variation in Crotalus scutulatus scutulatus (Mojave rattlesnake) remains an enigma. To understand the molecular basis for intra-species variation of metalloproteinase-associated activities, we modeled the three-dimensional structures of four metalloproteinases based on the amino acid sequence of four variations of the proteinase domain of the C. s. scutulatus metalloproteinase gene (GP1, GP2, GP3, and GP4). For comparative purposes, we modeled the atrolysin metalloproteinases of C. atrox as well. All molecular models shared the same topology. While the atrolysin metalloproteinase molecular models contained highly conserved substrate binding sites, the Mojave rattlesnake metalloproteinases showed higher structural divergence when superimposed onto each other. The highest structural divergence among the four C. s. scutulatus molecular models was located at the northern cleft wall and the S'1-pocket of the substrate binding site, molecular regions that modulate substrate selectivity. Molecular dynamics and field potential maps for each C. s. scutulatus metalloproteinase model demonstrated that the non-hemorrhagic metalloproteinases (GP2 and GP3) contain highly basic molecular and field potential surfaces while the hemorrhagic metalloproteinases GP1 and atrolysin C showed extensive acidic field potential maps and shallow but less dynamic active site pockets. Hence, differences in the spatial arrangement of the northern cleft wall, the S'1-pocket, and the physico-chemical environment surrounding the catalytic site contribute to differences in metalloproteinase activities in the Mojave rattlesnake. Our results provide a structural basis for variation of metalloproteinase-associated activities in the rattlesnake venom of the Mojave rattlesnake.

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Year:  2014        PMID: 24522289      PMCID: PMC4049379          DOI: 10.1007/s10867-013-9339-3

Source DB:  PubMed          Journal:  J Biol Phys        ISSN: 0092-0606            Impact factor:   1.365


  56 in total

1.  Isolation of two hemorrhagic toxins from Crotalus basiliscus basiliscus (Mexican west coast rattlesnake) venom and their effect on blood clotting and complement.

Authors:  O Molina; R K Seriel; M Martinez; M L Sierra; A Varela-Ramirez; E D Rael
Journal:  Int J Biochem       Date:  1990

2.  Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases.

Authors:  E N Baramova; J D Shannon; J B Bjarnason; J W Fox
Journal:  Arch Biochem Biophys       Date:  1989-11-15       Impact factor: 4.013

3.  Snake population venomics: proteomics-based analyses of individual variation reveals significant gene regulation effects on venom protein expression in Sistrurus rattlesnakes.

Authors:  H Lisle Gibbs; Libia Sanz; Juan J Calvete
Journal:  J Mol Evol       Date:  2009-01-30       Impact factor: 2.395

4.  Expression, activation, and processing of the recombinant snake venom metalloproteinase, pro-atrolysin E.

Authors:  K Shimokawa; L G Jia; X M Wang; J W Fox
Journal:  Arch Biochem Biophys       Date:  1996-11-15       Impact factor: 4.013

5.  Characterization of three fibrinogenolytic proteases isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus).

Authors:  K F Huang; C C Hung; S H Chiou
Journal:  Biochem Mol Biol Int       Date:  1993-12

Review 6.  Hemorrhagic metalloproteinases from snake venoms.

Authors:  J B Bjarnason; J W Fox
Journal:  Pharmacol Ther       Date:  1994       Impact factor: 12.310

7.  Hemorrhagic and Mojave toxins in the venoms of the offspring of two Mojave rattlesnakes (Crotalus scutulatus scutulatus).

Authors:  E D Rael; C S Lieb; N Maddux; A Varela-Ramirez; J Perez
Journal:  Comp Biochem Physiol B       Date:  1993-11

8.  Comparison of venom composition and biological activities of the subspecies Crotalus lepidus lepidus, Crotalus lepidus klauberi and Crotalus lepidus morulus from Mexico.

Authors:  Gerardo Martínez-Romero; Alexandra Rucavado; David Lazcano; José María Gutiérrez; Miguel Borja; Bruno Lomonte; Yolanda Garza-García; Alejandro Zugasti-Cruz
Journal:  Toxicon       Date:  2013-05-31       Impact factor: 3.033

9.  Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin.

Authors:  F X Gomis-Rüth; L F Kress; J Kellermann; I Mayr; X Lee; R Huber; W Bode
Journal:  J Mol Biol       Date:  1994-06-17       Impact factor: 5.469

10.  Integrated "omics" profiling indicates that miRNAs are modulators of the ontogenetic venom composition shift in the Central American rattlesnake, Crotalus simus simus.

Authors:  Jordi Durban; Alicia Pérez; Libia Sanz; Aarón Gómez; Fabián Bonilla; Santos Rodríguez; Danilo Chacón; Mahmood Sasa; Yamileth Angulo; José M Gutiérrez; Juan J Calvete
Journal:  BMC Genomics       Date:  2013-04-10       Impact factor: 3.969

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  7 in total

1.  Unraveling the distinctive features of hemorrhagic and non-hemorrhagic snake venom metalloproteinases using molecular simulations.

Authors:  Raoni Almeida de Souza; Natalia Díaz; Ronaldo Alves Pinto Nagem; Rafaela Salgado Ferreira; Dimas Suárez
Journal:  J Comput Aided Mol Des       Date:  2015-12-16       Impact factor: 3.686

2.  The Compartment Syndrome Associated with Deep Vein Thrombosis due to Rattlesnake Bite: A Case Report.

Authors:  Radu Ciprian Tincu; Zoie Ghiorghiu; Dana Tomescu; Radu Alexandru Macovei
Journal:  Balkan Med J       Date:  2017-04-13       Impact factor: 2.021

3.  The Possible Role of Nonbilayer Structures in Regulating ATP Synthase Activity in Mitochondrial Membranes.

Authors:  S E Gasanov; A A Kim; R K Dagda
Journal:  Biophysics (Oxf)       Date:  2016-10-19

4.  Phenotypic Variation in Mojave Rattlesnake (Crotalus scutulatus) Venom Is Driven by Four Toxin Families.

Authors:  Jason L Strickland; Andrew J Mason; Darin R Rokyta; Christopher L Parkinson
Journal:  Toxins (Basel)       Date:  2018-03-23       Impact factor: 4.546

5.  Evidence for divergent patterns of local selection driving venom variation in Mojave Rattlesnakes (Crotalus scutulatus).

Authors:  Jason L Strickland; Cara F Smith; Andrew J Mason; Drew R Schield; Miguel Borja; Gamaliel Castañeda-Gaytán; Carol L Spencer; Lydia L Smith; Ann Trápaga; Nassima M Bouzid; Gustavo Campillo-García; Oscar A Flores-Villela; Daniel Antonio-Rangel; Stephen P Mackessy; Todd A Castoe; Darin R Rokyta; Christopher L Parkinson
Journal:  Sci Rep       Date:  2018-12-04       Impact factor: 4.379

6.  Snake Venom Cytotoxins, Phospholipase A2s, and Zn2+-dependent Metalloproteinases: Mechanisms of Action and Pharmacological Relevance.

Authors:  Sardar E Gasanov; Ruben K Dagda; Eppie D Rael
Journal:  J Clin Toxicol       Date:  2014-01-25

7.  Insights into the Mechanisms Involved in Strong Hemorrhage and Dermonecrosis Induced by Atroxlysin-Ia, a PI-Class Snake Venom Metalloproteinase.

Authors:  Luciana Aparecida Freitas-de-Sousa; Mônica Colombini; Mônica Lopes-Ferreira; Solange M T Serrano; Ana Maria Moura-da-Silva
Journal:  Toxins (Basel)       Date:  2017-08-02       Impact factor: 4.546

  7 in total

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