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

Authors

Alex Chapeaurouge, Instituto Oswaldo Cruz, National University of Singapore
Md Abu Reza, National University of Singapore
Stephen P. Mackessy, University of Northern Colorado
Paulo C. Carvalho, Instituto Oswaldo Cruz, Carlos Chagas Institute
Richard H. Valente, Instituto Oswaldo Cruz
André Teixeira-Ferreira, Instituto Oswaldo Cruz
Jonas Perales, Instituto Oswaldo Cruz
Qingsong Lin, National University of Singapore
R. Manjunatha Kini, National University of Singapore, Virginia Commonwealth UniversityFollow

Document Type

Article

Original Publication Date

2015

Journal/Book/Conference Title

PLoS ONE

Volume

10

Issue

5

DOI of Original Publication

10.1371/journal.pone.0092091

Comments

Originally published at http://dx.doi.org/10.1371/journal.pone.0092091

Date of Submission

November 2015

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.

Rights

Copyright: © 2015 Chapeaurouge et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited

Is Part Of

VCU Biochemistry and Molecular Biology Publications