TY - JOUR
T1 - Seeing beyond the tip of the iceberg
T2 - A deep analysis of the venome of the Brazilian Rattlesnake, Crotalus durissus terrificus
AU - Melani, Rafael D.
AU - Araujo, Gabriel D.T.
AU - Carvalho, Paulo C.
AU - Goto, Livia
AU - Nogueira, Fábio C.S.
AU - Junqueira, Magno
AU - Domont, Gilberto B.
N1 - Funding Information:
This work was supported by Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES – Grant No. 063/2010 – Edital Toxinologia) and the FAPERJ/Rio de Janeiro Proteomics Network. The authors would like to thank for the generous donation of venom samples and the CPLL beads Dr. Ana Maria Moura da Silva, Laboratory of Immunopathology, Butantan Institute, Brazil, and Dr. Pier Giorgio Righetti, Politecnico di Milano, Italy, respectively. We are also grateful to A.W. Goering for his help with English editing of the manuscript.
Publisher Copyright:
© 2015 The Authors.
PY - 2015/9/1
Y1 - 2015/9/1
N2 - The complete characterization of the snake venom protein components is a requirement for a systems-wide understanding of their biological context. In this work, we provide a deep proteomic characterization of Crotalus durissus terrificus venom using different bottom-up approaches. We identified more than five times more protein families than the sum of all identifications previously reported. For the first time in this sub-species, we report the identification of three new toxin families: CRISP, phospholipase-B, and SVVEGF. This work also describes proteins involved in regulation of toxin synthesis and processing that are present in venom.
AB - The complete characterization of the snake venom protein components is a requirement for a systems-wide understanding of their biological context. In this work, we provide a deep proteomic characterization of Crotalus durissus terrificus venom using different bottom-up approaches. We identified more than five times more protein families than the sum of all identifications previously reported. For the first time in this sub-species, we report the identification of three new toxin families: CRISP, phospholipase-B, and SVVEGF. This work also describes proteins involved in regulation of toxin synthesis and processing that are present in venom.
KW - Bottom-up approaches
KW - CPLL
KW - Crotalus durissus terrificus venom
KW - IEF
KW - In-solution digestion
KW - Shotgun
UR - http://www.scopus.com/inward/record.url?scp=84940960941&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84940960941&partnerID=8YFLogxK
U2 - 10.1016/j.euprot.2015.05.006
DO - 10.1016/j.euprot.2015.05.006
M3 - Article
AN - SCOPUS:84940960941
SN - 2212-9685
VL - 8
SP - 144
EP - 156
JO - EuPA Open Proteomics
JF - EuPA Open Proteomics
ER -