CEEPC/IPM/CMSC - Abstrakt prezentace

(CEEPC/IPM/CMSC 2022 - FrP-36)
5 years of delving into the Naja ashei venom proteome

Aleksandra Bocian 1 *, Konrad K. Hus 1, Justyna Buczkowicz 1, Vladimir Petrílla 2,3, Jaroslav Legath 1,2

  1. Rzeszów University of Technology
  2. University of Veterinary Medicine and Pharmacy in Košice
  3. Zoological Garden Košice

Abstrakt

Naja ashei is the biggest African spitting cobra found in Kenya, Ethiopia, Somalia, and Uganda. This cobra was considered to be a morphologically distinct variant of the species N. nigricollis however, molecular analyses showed that despite greater differences in morphology, this species is more closely related to N. mossambica, a spitting cobra found in Mozambique. Since 2007 it is considered a separate species.
For the past five years, our team has been the only one in the world to study the proteomic composition of N. ashei venom. In our study, we used various venom separation methods (2D electrophoresis [1], ultrafiltration [2], ion exchange chromatography [3], and SEC chromatography) and mass spectrometry techniques (MALDI ToF and LC-MS).
From the earliest analyses, our research has indicated that, as in other cobras, the major components of N. ashei venom are PLA2 and 3FTx. All methods also identified SVMPs, CVF, CRISPs, and VNGF. With the increasing level of venom fractionation, new groups of proteins were discovered such as serine and cysteine proteases, L-amino acid oxidases, and antimicrobial peptides, among others. We have also found a mysterious group named by our team “Ig-like proteins” because it included proteins with an immunoglobulin domain, whose function is so far unknown. On the other hand, increasing the purity of the fractions for the most abundant protein groups resulted in the detection of many new peptides.. Thus, it can be concluded that in the case of such a complex proteome as snake venom, in which individual groups of proteins clearly differ in abundance, the picture of the proteome is significantly affected by both the way proteins are fractionated and the way MS data are analyzed.

* Korespondující autor: bocian@prz.edu.pl

Literatura

  1. Hus, K. K. et al. Molecules 23 (3) (2018)
  2. Hus K.K. et al. Biomolecules 10(9), 1282 (2020)
  3. Bocian A. et al. Molecules 25(2) (2020)

Partneři společnosti

LabRules LCMS LabRules GCMS

Partneři

Bruker HPST Merck Pragolab Amedis EastPort Shimadzu Waters