Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2010-4-19
pubmed:abstractText
Spider venoms are cocktails of toxic proteins and peptides, whose composition varies at many levels. Understanding patterns of variation in chemistry and bioactivity is fundamental for understanding factors influencing variation. The venom toxin sphingomyelinase D (SMase D) in sicariid spider venom (Loxosceles and Sicarius) causes dermonecrotic lesions in mammals. Multiple forms of venom-expressed genes with homology to SMase D are expressed in venoms of both genera. SMase D activity levels differ among major clades with American Sicarius vastly reduced relative to all Loxosceles and African Sicarius despite expression of SMase D homologs in venoms of American Sicarius. Here we report comparative analyses of protein composition and insecticidal activity of crude venoms from three Sicarius species, two from South Africa and one from Central America. Comparative 2-dimensional electrophoresis shows dense regions of proteins in the size range of SMase D in all three species, but there are differences in sizes and isoelectric points (pIs). Few proteins strictly co-migrate and there are clusters of proteins with similar pIs and molecular weights whose patterns of similarity do not necessarily reflect phylogenetic relatedness. In addition, PD(50) estimates on crickets indicate a small though significant decrease in potency of South American Sicarius venoms relative to African species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1879-3150
pubmed:author
pubmed:copyrightInfo
2010 Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1274-82
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Comparative analyses of venoms from American and African Sicarius spiders that differ in sphingomyelinase D activity.
pubmed:affiliation
Department of Biology, Lewis and Clark College, 0615 SW Palatine Hill Road, Portland, OR 97219, USA. pamela@lclark.edu
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't