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2017 ; 9
(9
): ä Nephropedia Template TP
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A Review and Database of Snake Venom Proteomes
#MMPMID28927001
Tasoulis T
; Isbister GK
Toxins (Basel)
2017[Sep]; 9
(9
): ä PMID28927001
show ga
Advances in the last decade combining transcriptomics with established proteomics
methods have made possible rapid identification and quantification of protein
families in snake venoms. Although over 100 studies have been published, the
value of this information is increased when it is collated, allowing rapid
assimilation and evaluation of evolutionary trends, geographical variation, and
possible medical implications. This review brings together all compositional
studies of snake venom proteomes published in the last decade. Compositional
studies were identified for 132 snake species: 42 from 360 (12%) Elapidae
(elapids), 20 from 101 (20%) Viperinae (true vipers), 65 from 239 (27%)
Crotalinae (pit vipers), and five species of non-front-fanged snakes.
Approximately 90% of their total venom composition consisted of eight protein
families for elapids, 11 protein families for viperines and ten protein families
for crotalines. There were four dominant protein families: phospholipase A?s (the
most common across all front-fanged snakes), metalloproteases, serine proteases
and three-finger toxins. There were six secondary protein families: cysteine-rich
secretory proteins, l-amino acid oxidases, kunitz peptides, C-type
lectins/snaclecs, disintegrins and natriuretic peptides. Elapid venoms contained
mostly three-finger toxins and phospholipase A?s and viper venoms
metalloproteases, phospholipase A?s and serine proteases. Although 63 protein
families were identified, more than half were present in <5% of snake species
studied and always in low abundance. The importance of these minor component
proteins remains unknown.