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. 2015 May 8;10(5):e0092091.
doi: 10.1371/journal.pone.0092091. eCollection 2015.

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

Alex Chapeaurouge  1 , Md Abu Reza  2 , Stephen P Mackessy  3 , Paulo C Carvalho  4 , Richard H Valente  5 , André Teixeira-Ferreira  5 , Jonas Perales  5 , Qingsong Lin  2 , R Manjunatha Kini  6
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Interrogating the Venom of the Viperid Snake Sistrurus catenatus edwardsii by a Combined Approach of Electrospray and MALDI Mass Spectrometry

Alex Chapeaurouge et al. PLoS One. .

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.

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Conflict of interest statement

Competing Interests: The authors have declared that no competing interests exist.

Figures

Fig 1
Fig 1. Sequence coverages of some of the predicted venom gland proteins of S. c. edwardsii as revealed by the combined approach of MALDI and ESI tandem mass spectrometry.
Protein sequences including specific domains are indicted by colored bars; below these, corresponding peptides identified by ESI (black lines) and MALDI (red lines) are indicated.
Fig 2
Fig 2. Sequence alignment of the metalloproteinases of the venom of S. c. edwardsii.
Different colors indicate the unique peptides identified by tandem mass spectrometry of the corresponding proteins.
Fig 3
Fig 3. Sequence alignment of the serine proteinases of the venom of S. c. edwardsii.
Different colors indicate the unique peptides identified by tandem mass spectrometry of the corresponding proteins.
See this image and copyright information in PMC

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