Protein-species quantitative venomics: looking through a crystal ball
1 Structural and Functional Venomics Laboratory, Instituto de Biomedicina de Valencia, C.S.I.C, Jaime Roig 11, 46010 Valencia, Spain.
2 Skaggs School of Pharmacy & Pharmaceutical Sciences, University of California-San Diego, La Jolla, CA, USA.
3 Department of Physical and Analytical Chemistry, University of Oviedo, Oviedo, Spain.
4 Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica.
ABSTRACT
In this paper we discuss recent significant developments in the field of venom research, specifically the emergence of top-down proteomic applications that allow achieving compositional resolution at the level of the protein species present in the venom, and the absolute quantification of the venom proteins (the term “protein species” is used here to refer to all the different molecular forms in which a protein can be found. Please consult the special issue of Jornal of Proteomics “Towards deciphering proteomes via the proteoform, protein speciation, moonlighting and protein code concepts” published in 2016, vol. 134, pages 1-202). Challenges remain to be solved in order to achieve a compact and automated platform with which to routinely carry out comprehensive quantitative analysis of all toxins present in a venom. This short essay reflects the authors’ view of the immediate future in this direction for the proteomic analysis of venoms, particularly of snakes.
Key words: Snake venomics; Top-down proteomics; Top-down venomics; Protein species-resolved venomics; Absolute quantification; Inductively coupled plasma mass spectrometry
Funding
Research at IBV-CSIC was supported by grant BFU2013-42833-P from the Ministerio de Economía y Competitividad, Madrid, Spain. F.C.C. acknowledges pre-doctoral fellowship from the Ministry of Economy and Competitiveness of Spain (BES-2014-068032).
Received: January 24, 2017.
Accepted: April 19, 2017.
Revised: April 28, 2017.
Correspondence: jcalvete@ibv.csic.es