Proteomic Visualization of Viperid Venoms: Complexity, Diversity and Similarity

Serrano, S.M.T.(1,2), Shannon, J.D.(1), Fox, J.W.(1) 

(1)Department of Microbiology, University of Virginia School of Medicine, Charlottesville, VA 22908, USA and (2)Laboratório de Bioquímica e Biofísica, Instituto Butantan, São Paulo, SP 05503-900, Brazil.

The complexity of viperid venoms has long been appreciated in the field of toxinology and medicine.  However, it is only recently that the depth of that complexity has become quantitatively accessible.  With the resurgence of 2D PAGE and the advances in mass spectrometry essentially all venom components can be visualized and identified given the effort and resources.  Here we present the use of various technologies for examining venom complexity and demonstrate their associated advantages and disadvantages.  2D PAGE comparisons between different genera of viperid venoms; different species of the same genus and specimens of the same genus and species demonstrate the similarity as well as the apparent diversity among these venoms. Finally, we have developed techniques to examine subpopulations of venom proteins (metalloproteinase proteome; serine proteinase proteome; and the glycoproteome). These tools will allow for a better understanding of venom complexity and toxic properties as well as enabling investigators with particular interests to focus on these subpopulations of proteins for further study.

CORRESPONDENCE TO:

Serrano, S.M.T., Laboratório de Bioquímica e Biofísica, Instituto Butantan, São Paulo, SP 05503-900, Brazil, Email: s_serrano@hotmail.com