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J Proteomics. 2009 Mar 6;72(2):241-55. doi: 10.1016/j.jprot.2009.01.001. Epub 2009 Jan 11.

Bothrops insularis venomics: a proteomic analysis supported by transcriptomic-generated sequence data.

Author information

1
Oswaldo Cruz Foundation, IOC, Laboratory of Toxinology, Rio de Janeiro, Brazil. rhv4u@ioc.fiocruz.br

Abstract

A joint transcriptomic and proteomic approach employing two-dimensional electrophoresis, liquid chromatography and mass spectrometry was carried out to identify peptides and proteins expressed by the venom gland of the snake Bothrops insularis, an endemic species of Queimada Grande Island, Brazil. Four protein families were mainly represented in processed spots, namely metalloproteinase, serine proteinase, phospholipase A(2) and lectin. Other represented families were growth factors, the developmental protein G10, a disintegrin and putative novel bradykinin-potentiating peptides. The enzymes were present in several isoforms. Most of the experimental data agreed with predicted values for isoelectric point and M(r) of proteins found in the transcriptome of the venom gland. The results also support the existence of posttranslational modifications and of proteolytic processing of precursor molecules which could lead to diverse multifunctional proteins. This study provides a preliminary reference map for proteins and peptides present in Bothrops insularis whole venom establishing the basis for comparative studies of other venom proteomes which could help the search for new drugs and the improvement of venom therapeutics. Altogether, our data point to the influence of transcriptional and post-translational events on the final venom composition and stress the need for a multivariate approach to snake venomics studies.

PMID:
19211044
DOI:
10.1016/j.jprot.2009.01.001
[Indexed for MEDLINE]

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