TY - JOUR
T1 - Functional and structural diversification of the Anguimorpha lizard venom system
AU - Fry, Bryan G
AU - Winter, Kelly Lee
AU - Norman, Jeanette A
AU - Roelants, Kim
AU - Nabuurs, Rob JA
AU - van Osch, Matthias JP
AU - Teeuwisse, Wouter M
AU - van der Weerd, Louise
AU - McNaughton, Judith E
AU - Kwok, Hang Fai
AU - Scheib, Holger
AU - Greisman, Laura
AU - Kochva, Elazar
AU - Miller, Laurence J
AU - Gao, Fan
AU - Karas, John
AU - Scanlon, Denis
AU - Lin, Feng
AU - Kuruppu, Don M Sanjaya
AU - Shaw, Chris
AU - Wong, Lily
AU - Hodgson, Wayne Clarence
PY - 2010
Y1 - 2010
N2 - Venom has only been recently discovered to be a basal trait of the Anguimorpha lizards. Consequently, very little is known about the timings of toxin recruitment events, venom protein molecular evolution, or even the relative physical diversifications of the venom system itself. A multidisciplinary approach was used to examine the evolution across the full taxonomical range of this a??130 million-year-old clade. Analysis of cDNA libraries revealed complex venom transcriptomes. Most notably, three new cardioactive peptide toxin types were discovered (celestoxin, cholecystokinin, and YY peptides). The latter two represent additional examples of convergent use of genes in toxic arsenals, both having previously been documented as components of frog skin defensive chemical secretions. Two other novel venom gland-overexpressed modified versions of other protein frameworks were also recovered from the libraries (epididymal secretory protein and ribonuclease). Lectin, hyaluronidase, and veficolin toxin types were sequenced for the first time from lizard venoms and shown to be homologous to the snake venom forms. In contrast, phylogenetic analyses demonstrated that the lizard natriuretic peptide toxins were recruited independently of the form in snake venoms. The de novo evolution of helokinestatin peptide toxin encoding domains within the lizard venom natriuretic gene was revealed to be exclusive to the helodermatid/anguid subclade. New isoforms were sequenced for cysteine-rich secretory protein, kallikrein, and phospholipase A(2) toxins. Venom gland morphological analysis revealed extensive evolutionary tinkering. Anguid glands are characterized by thin capsules and mixed glands, serous at the bottom of the lobule and....
AB - Venom has only been recently discovered to be a basal trait of the Anguimorpha lizards. Consequently, very little is known about the timings of toxin recruitment events, venom protein molecular evolution, or even the relative physical diversifications of the venom system itself. A multidisciplinary approach was used to examine the evolution across the full taxonomical range of this a??130 million-year-old clade. Analysis of cDNA libraries revealed complex venom transcriptomes. Most notably, three new cardioactive peptide toxin types were discovered (celestoxin, cholecystokinin, and YY peptides). The latter two represent additional examples of convergent use of genes in toxic arsenals, both having previously been documented as components of frog skin defensive chemical secretions. Two other novel venom gland-overexpressed modified versions of other protein frameworks were also recovered from the libraries (epididymal secretory protein and ribonuclease). Lectin, hyaluronidase, and veficolin toxin types were sequenced for the first time from lizard venoms and shown to be homologous to the snake venom forms. In contrast, phylogenetic analyses demonstrated that the lizard natriuretic peptide toxins were recruited independently of the form in snake venoms. The de novo evolution of helokinestatin peptide toxin encoding domains within the lizard venom natriuretic gene was revealed to be exclusive to the helodermatid/anguid subclade. New isoforms were sequenced for cysteine-rich secretory protein, kallikrein, and phospholipase A(2) toxins. Venom gland morphological analysis revealed extensive evolutionary tinkering. Anguid glands are characterized by thin capsules and mixed glands, serous at the bottom of the lobule and....
UR - http://www.ncbi.nlm.nih.gov/pubmed/20631207
U2 - 10.1074/mcp.M110.001370
DO - 10.1074/mcp.M110.001370
M3 - Article
VL - 9
SP - 2369
EP - 2390
JO - Molecular & Cellular Proteomics
JF - Molecular & Cellular Proteomics
SN - 1535-9476
IS - 11
ER -