Composition characterization of various viperidae snake venoms using MS-based proteomics N-glycoproteomics and N-glycomics.
Autor: | Abu Aisheh M; Department of Chemistry, Faculty of Science, Hacettepe University, 06800, Ankara, Turkey., Kayili HM; Department of Medical Engineering, Faculty of Engineering, Karabük University, 78000, Karabük, Turkey., Numanoglu Cevik Y; Microbiology Reference Laboratory, Turkish Public Health Institute, Ministery of Health, 06430, Ankara, Turkey., Kanat MA; Microbiology and Reference Laboratory and Biological Products Department, General Directorate of Public Health, Minister of Health, 06430, Ankara, Turkey., Salih B; Department of Chemistry, Faculty of Science, Hacettepe University, 06800, Ankara, Turkey. Electronic address: bekir@hacettepe.edu.tr. |
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Jazyk: | angličtina |
Zdroj: | Toxicon : official journal of the International Society on Toxinology [Toxicon] 2023 Nov; Vol. 235, pp. 107328. Date of Electronic Publication: 2023 Oct 25. |
DOI: | 10.1016/j.toxicon.2023.107328 |
Abstrakt: | Viperidae snake species is widely abundant and responsible for most envenomation cases in Turkey. The structural and compositional profiles of snake venom have been investigated to study the venom component variation across different species and to profile the venom biological activity variation against prey. In this context, we used proteomics, glycoproteomics and glycomics strategies to characterize the protein, glycoproteins and glycan structural and compositional profiles of various snake venoms in the Viperidae family. Moreover, we compared these profiles using the downstream bioinformatics and machine learning classification modules. The overall mass spectrometry profiles identified 144 different proteins, 36 glycoproteins and 78 distinct N-glycan structures varying in composition across the five venoms. A high amount of the characterized proteins belongs to the glycosylated protein family Trypsin-like serine protease (Tryp_SPc), Disintegrin (DISIN), and ADAM Cysteine-Rich (ACR). Most identified N-glycans have a complex chain carrying galactosylated N-glycans abundantly. The glycan composition data obtained from glycoproteomics aligns consistently with the findings from glycomics. The clustering and principal component analyses (PCA) illustrated the composition-based similarities and differences between each snake venom species' proteome, glycoproteome and glycan profiles. Specifically, the N-glycan profiles of M. xanthina (Mx) and V. a. ammodytes (Vaa) venoms were identical and difficult to differentiate; in contrast, their proteome profiles were distinct. Interestingly, the variety of the proteins across the species highlighted the impact of glycosylation on the diversity of the glycosylated protein families. This proposed high throughput approach provides accurate and comprehensive profiles of the composition and function of various Viperidae snake venoms. Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (Copyright © 2023 Elsevier Ltd. All rights reserved.) |
Databáze: | MEDLINE |
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