Mojave toxin in venom of Crotalus helleri (Southern Pacific Rattlesnake): molecular and geographic characterization

Mojave toxin (MT) was detected in five of 25 Crotalus helleri (Southern Pacific rattlesnake) sampled using anti-MT antibodies and nucleotide sequence analysis. All of the venoms that were positive for MT were collected from Mt San Jacinto in Riverside Co., California. Since this population is geogra...

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Veröffentlicht in:Toxicon (Oxford) 2004-12, Vol.44 (7), p.781-791
Hauptverfasser: French, Wendy J., Hayes, William K., Bush, Sean P., Cardwell, Michael D., Bader, Julia O., Rael, Eppie D.
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container_issue 7
container_start_page 781
container_title Toxicon (Oxford)
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creator French, Wendy J.
Hayes, William K.
Bush, Sean P.
Cardwell, Michael D.
Bader, Julia O.
Rael, Eppie D.
description Mojave toxin (MT) was detected in five of 25 Crotalus helleri (Southern Pacific rattlesnake) sampled using anti-MT antibodies and nucleotide sequence analysis. All of the venoms that were positive for MT were collected from Mt San Jacinto in Riverside Co., California. Since this population is geographically isolated from C. scutulatus scutulatus (Mojave rattlesnake), it is unlikely that this finding is due to recent hybridization. MT concentration differences between C. helleri and C. s. scutulatus reflected the presence of ‘isoforms’ of the toxin in the venom. Whereas C. s. scutulatus generally has several isoforms of the toxin (detected by Western blotting), only one ‘isoform’ that focused at pI 5.1 was detected in C. helleri. Both acidic and basic subunits of MT sequences were obtained from C. helleri DNA with primers specific for MT, but only from snakes that had MT in their venom. The sequence identity of the C. helleri acidic subunit to the C. s. scutulatus subunit was 84.9%, whereas the sequence identity of the C. helleri basic subunit was 97% to the C. s. scutulatus basic subunit. Using casein, fibrin, and hide powder azure as substrates, assays for proteolytic activity suggested that C. helleri possesses several different types of metalloproteinases in their venom. However, proteolytic activity was not detected, or present in reduced amounts, in specimens having MT. Clinical neurotoxicity following envenomation by certain populations of C. helleri may be due to MT.
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Using casein, fibrin, and hide powder azure as substrates, assays for proteolytic activity suggested that C. helleri possesses several different types of metalloproteinases in their venom. However, proteolytic activity was not detected, or present in reduced amounts, in specimens having MT. Clinical neurotoxicity following envenomation by certain populations of C. helleri may be due to MT.</description><subject>Animal poisons toxicology. 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Antivenoms</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>California</topic><topic>Caseins - metabolism</topic><topic>Chromogenic Compounds - metabolism</topic><topic>Crotalid Venoms - genetics</topic><topic>Crotalid Venoms - metabolism</topic><topic>Crotalus</topic><topic>Crotalus helleri</topic><topic>Crotalus scutulatus</topic><topic>DNA Primers</topic><topic>DNA sequence</topic><topic>Fibrin - metabolism</topic><topic>Geography</topic><topic>Medical sciences</topic><topic>Metalloproteinases</topic><topic>Mojave toxin</topic><topic>Molecular Sequence Data</topic><topic>Neurotoxins - genetics</topic><topic>Neurotoxins - metabolism</topic><topic>Organic Chemicals</topic><topic>Protein Isoforms</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology</topic><topic>Species Specificity</topic><topic>Toxicology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>French, Wendy J.</creatorcontrib><creatorcontrib>Hayes, William K.</creatorcontrib><creatorcontrib>Bush, Sean P.</creatorcontrib><creatorcontrib>Cardwell, Michael D.</creatorcontrib><creatorcontrib>Bader, Julia O.</creatorcontrib><creatorcontrib>Rael, Eppie D.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Toxicon (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>French, Wendy J.</au><au>Hayes, William K.</au><au>Bush, Sean P.</au><au>Cardwell, Michael D.</au><au>Bader, Julia O.</au><au>Rael, Eppie D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mojave toxin in venom of Crotalus helleri (Southern Pacific Rattlesnake): molecular and geographic characterization</atitle><jtitle>Toxicon (Oxford)</jtitle><addtitle>Toxicon</addtitle><date>2004-12-01</date><risdate>2004</risdate><volume>44</volume><issue>7</issue><spage>781</spage><epage>791</epage><pages>781-791</pages><issn>0041-0101</issn><eissn>1879-3150</eissn><coden>TOXIA6</coden><abstract>Mojave toxin (MT) was detected in five of 25 Crotalus helleri (Southern Pacific rattlesnake) sampled using anti-MT antibodies and nucleotide sequence analysis. All of the venoms that were positive for MT were collected from Mt San Jacinto in Riverside Co., California. Since this population is geographically isolated from C. scutulatus scutulatus (Mojave rattlesnake), it is unlikely that this finding is due to recent hybridization. MT concentration differences between C. helleri and C. s. scutulatus reflected the presence of ‘isoforms’ of the toxin in the venom. Whereas C. s. scutulatus generally has several isoforms of the toxin (detected by Western blotting), only one ‘isoform’ that focused at pI 5.1 was detected in C. helleri. Both acidic and basic subunits of MT sequences were obtained from C. helleri DNA with primers specific for MT, but only from snakes that had MT in their venom. The sequence identity of the C. helleri acidic subunit to the C. s. scutulatus subunit was 84.9%, whereas the sequence identity of the C. helleri basic subunit was 97% to the C. s. scutulatus basic subunit. Using casein, fibrin, and hide powder azure as substrates, assays for proteolytic activity suggested that C. helleri possesses several different types of metalloproteinases in their venom. However, proteolytic activity was not detected, or present in reduced amounts, in specimens having MT. Clinical neurotoxicity following envenomation by certain populations of C. helleri may be due to MT.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>15500854</pmid><doi>10.1016/j.toxicon.2004.08.008</doi><tpages>11</tpages></addata></record>
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subjects Animal poisons toxicology. Antivenoms
Animals
Base Sequence
Biological and medical sciences
Blotting, Western
California
Caseins - metabolism
Chromogenic Compounds - metabolism
Crotalid Venoms - genetics
Crotalid Venoms - metabolism
Crotalus
Crotalus helleri
Crotalus scutulatus
DNA Primers
DNA sequence
Fibrin - metabolism
Geography
Medical sciences
Metalloproteinases
Mojave toxin
Molecular Sequence Data
Neurotoxins - genetics
Neurotoxins - metabolism
Organic Chemicals
Protein Isoforms
Sequence Alignment
Sequence Analysis, DNA
Sequence Homology
Species Specificity
Toxicology
title Mojave toxin in venom of Crotalus helleri (Southern Pacific Rattlesnake): molecular and geographic characterization
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