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J Proteome Res. 2007 Jul;6(7):2792-801. Epub 2007 Jun 14.

Proteomic and peptidomic characterization of the venom from the Chinese bird spider, Ornithoctonus huwena Wang.

Author information

1
Key Laboratory of Protein Chemistry and Developmental Biology of the Ministry of Education, Life Science College, Hunan Normal University, Changsha 410081, People's Republic of China.

Abstract

The bird spider Ornithoctonus huwena Wang is a very venomous spider in China. Several compounds with different types of biological activities have been identified previously from the venom of this spider. In this study, we have performed a proteomic and peptidomic analysis of the venom. The venom was preseparated into two parts: the venom proteins with molecular weight (MW) higher than 10,000 and the venom peptides with MW lower than 10 000. Using one-dimensional gel electrophoresis (1-DE), two-dimensional gel electrophoresis (2-DE), and mass spectrometry, 90 proteins were identified, including some important enzymes, binding proteins, and some proteins with significant biological functions. For venom peptides, a combination of cation-exchange and reversed-phase chromatography was employed. More than 100 components were detected by mass spectrometry, and 47 peptides were sequenced by Edman degradation. The peptides display structural and pharmacological diversity and share little sequence similarity with peptides from other animal venoms, which indicates the venom of O. huwena Wang is unique. The venom peptides can be classified into several superfamilies. Also it is revealed that gene duplication and focal hypermutation have taken place during the evolution of the spider toxins.

PMID:
17567163
DOI:
10.1021/pr0700192
[Indexed for MEDLINE]

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