SAFETYLIT WEEKLY UPDATE

We compile citations and summaries of about 400 new articles every week.
RSS Feed

HELP: Tutorials | FAQ
CONTACT US: Contact info

Search Results

Journal Article

Citation

Leonardi A, Biass D, Kordis D, Stöcklin R, Favreau P, Krizaj I. J. Proteome Res. 2012; 11(10): 5046-5058.

Copyright

(Copyright © 2012, American Chemical Society)

DOI

10.1021/pr3006155

PMID

22928724

Abstract

For some decades, cone snail venoms have been providing peptides, generally termed conopeptides, that exhibit a large diversity of pharmacological properties. However, little attention has been devoted to the high molecular mass (HMM) proteins in venoms of mollusks. In order to shed more light on cone snail venom HMM components, the proteins of dissected and injected venom of a fish-hunting cone snail, Conus consors, were extensively assessed. HMM venom proteins were separated by two-dimensional polyacrylamide gel electrophoresis and analyzed by mass spectrometry (MS). The MS data were interpreted using UniProt database, EST libraries from C. consors venom duct and salivary gland, and their genomic information. Numerous protein families were discovered in the lumen of the venom duct and assigned a biological function, thus pointing to their potential role in venom production and maturation. Interestingly, the study also revealed original proteins defining new families of unknown function. Only two groups of HMM proteins passing the venom selection process - echotoxins and hyaluronidases - were clearly present in the injected venom. They are suggested to contribute to the envenomation process. This newly devised integrated HMM proteomic analysis is a big step towards identification of the protein arsenal used in a cone snail venom apparatus for venom production, maturation and function.


Language: en

NEW SEARCH


All SafetyLit records are available for automatic download to Zotero & Mendeley
Print