TITLE

Interrogating the Venom of the Viperid Snake Sistrurus catenatus edwardsii by a Combined Approach of Electrospray and MALDI Mass Spectrometry

AUTHOR(S)
Chapeaurouge, Alex; Reza, Md Abu; Mackessy, Stephen P.; Carvalho, Paulo C.; Valente, Richard H.; Teixeira-Ferreira, André; Perales, Jonas; Lin, Qingsong; Kini, R. Manjunatha
PUB. DATE
May 2015
SOURCE
PLoS ONE;May2015, Vol. 10 Issue 5, p1
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The complete sequence characterization of snake venom proteins by mass spectrometry is rather challenging due to the presence of multiple isoforms from different protein families. In the present study, we investigated the tryptic digest of the venom of the viperid snake Sistrurus catenatus edwardsii by a combined approach of liquid chromatography coupled to either electrospray (online) or MALDI (offline) mass spectrometry. These different ionization techniques proved to be complementary allowing the identification a great variety of isoforms of diverse snake venom protein families, as evidenced by the detection of the corresponding unique peptides. For example, ten out of eleven predicted isoforms of serine proteinases of the venom of S. c. edwardsii were distinguished using this approach. Moreover, snake venom protein families not encountered in a previous transcriptome study of the venom gland of this snake were identified. In essence, our results support the notion that complementary ionization techniques of mass spectrometry allow for the detection of even subtle sequence differences of snake venom proteins, which is fundamental for future structure-function relationship and possible drug design studies.
ACCESSION #
102969432

 

Share

Read the Article

Courtesy of THE LIBRARY OF VIRGINIA

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics