TY - JOUR
T1 - Venomous extract protein profile of Brazilian tarantula Grammostola iheringi
T2 - Searching for potential biotechnological applications
AU - Borges, Marcia H.
AU - Figueiredo, Suely G.
AU - Leprevost, Felipe V.
AU - De Lima, Maria Elena
AU - Cordeiro, Marta do N.
AU - Diniz, Marcelo R.V.
AU - Moresco, James
AU - Carvalho, Paulo C.
AU - Yates, John R.
N1 - Funding Information:
We would like to acknowledge the funding support from INCTTox (INCTTOX/CNPq 573790/2008-6), Fapemig (CBB — BIP-00080-14), Capes Toxinologia (Capes 063/10 — 23038.006280/2011-07). This study had a grant from CNPq Process 245558/2012-8 and National Institute of Health grants: P41 GM103533, R01 MH067880, R01 MH100175, and UCLA/NHLBI Proteomics Centers (HHSN268201000035C). We would like to express our special recognition to Maria Nelman Antunes and Claudio Livio da Silva for having manipulated the spiders and collected the venom extracts. Thanks to Nutrinsecta for providing some grillus species used for the diet of spiders. We thank Verilaine Silvério for assistance with the flowchart image.
Funding Information:
We would like to acknowledge the funding support from INCTTox ( INCTTOX/CNPq 573790/2008-6 ), Fapemig ( CBB — BIP-00080-14 ), Capes Toxinologia ( Capes 063/10 — 23038.006280/2011-07 ). This study had a grant from CNPq Process 245558/2012-8 and National Institute of Health grants: P41 GM103533 , R01 MH067880 , R01 MH100175 , and UCLA/NHLBI Proteomics Centers ( HHSN268201000035C ). We would like to express our special recognition to Maria Nelman Antunes and Claudio Livio da Silva for having manipulated the spiders and collected the venom extracts. Thanks to Nutrinsecta for providing some grillus species used for the diet of spiders. We thank Verilaine Silvério for assistance with the flowchart image.
Publisher Copyright:
© 2016 Elsevier B.V.
PY - 2016/3/16
Y1 - 2016/3/16
N2 - Tarantula spiders, Theraphosidae family, are spread throughout most tropical regions of the world. Despite their size and reputation, there are few reports of accidents. However, like other spiders, their venom is considered a remarkable source of toxins, which have been selected through millions of years of evolution. The present work provides a proteomic overview of the fascinating complexity of the venomous extract of the Grammostola iheringi tarantula, obtained by electrical stimulation of the chelicerae. For analysis a bottom-up proteomic approach Multidimensional Protein Identification Technology (MudPIT) was used. Based on bioinformatics analyses, PepExplorer, a similarity-driven search tool that identifies proteins based on phylogenetically close organisms, a total of 395 proteins were identified in this venomous extract. Most of the identifications (~. 70%) were classified as predicted (21%), hypothetical (6%) and putative (37%), while a small group (6%) had no predicted function. Identified molecules matched with neurotoxins that act on ions channels; proteases, such as serine proteases, metalloproteinases, cysteine proteinases, aspartic proteinases, carboxypeptidases and cysteine-rich secretory enzymes (CRISP) and some molecules with unknown target. Additionally, non-classical venom proteins were also identified. Up to now, this study represents, to date, the first broad characterization of the composition of G. iheringi venomous extract. Our data provides a tantalizing insight into the diversity of proteins in this venom and their biotechnological potential. Significance: Animal venoms contain a diversity of molecules able to bind to specific cell targets. Due to their biochemical and physiological properties, these molecules are interesting for medical and biotechnological purposes. In this study, a large number of components of the venomous extract of the spider Grammostola iheringi were identified by the MudPIT technique. It was demonstrated that this approach is a sensitive and adequate method to achieve a broad spectrum of information about animal venoms. Using this bottom-up proteomic method, classical and non-classical venom proteins were identified which stimulate new interest in the systematic research of their protein components.
AB - Tarantula spiders, Theraphosidae family, are spread throughout most tropical regions of the world. Despite their size and reputation, there are few reports of accidents. However, like other spiders, their venom is considered a remarkable source of toxins, which have been selected through millions of years of evolution. The present work provides a proteomic overview of the fascinating complexity of the venomous extract of the Grammostola iheringi tarantula, obtained by electrical stimulation of the chelicerae. For analysis a bottom-up proteomic approach Multidimensional Protein Identification Technology (MudPIT) was used. Based on bioinformatics analyses, PepExplorer, a similarity-driven search tool that identifies proteins based on phylogenetically close organisms, a total of 395 proteins were identified in this venomous extract. Most of the identifications (~. 70%) were classified as predicted (21%), hypothetical (6%) and putative (37%), while a small group (6%) had no predicted function. Identified molecules matched with neurotoxins that act on ions channels; proteases, such as serine proteases, metalloproteinases, cysteine proteinases, aspartic proteinases, carboxypeptidases and cysteine-rich secretory enzymes (CRISP) and some molecules with unknown target. Additionally, non-classical venom proteins were also identified. Up to now, this study represents, to date, the first broad characterization of the composition of G. iheringi venomous extract. Our data provides a tantalizing insight into the diversity of proteins in this venom and their biotechnological potential. Significance: Animal venoms contain a diversity of molecules able to bind to specific cell targets. Due to their biochemical and physiological properties, these molecules are interesting for medical and biotechnological purposes. In this study, a large number of components of the venomous extract of the spider Grammostola iheringi were identified by the MudPIT technique. It was demonstrated that this approach is a sensitive and adequate method to achieve a broad spectrum of information about animal venoms. Using this bottom-up proteomic method, classical and non-classical venom proteins were identified which stimulate new interest in the systematic research of their protein components.
KW - Animal venom
KW - MudPIT
KW - Proteome
KW - Spider venom
KW - Tarantula
KW - Toxins
UR - http://www.scopus.com/inward/record.url?scp=84958259953&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84958259953&partnerID=8YFLogxK
U2 - 10.1016/j.jprot.2016.01.013
DO - 10.1016/j.jprot.2016.01.013
M3 - Article
C2 - 26828374
AN - SCOPUS:84958259953
SN - 1874-3919
VL - 136
SP - 35
EP - 47
JO - Journal of Proteomics
JF - Journal of Proteomics
ER -