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The distinct N-terminomes of Bothrops jararaca newborn and adult venoms.

ABSTRACT: In this study we applied the Terminal Amine Isotopic Labeling of Substrates (TAILS) technology to characterize the natural N-terminome of newborn and adult Bothrops jararaca venoms.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Bothrops Jararaca (jararaca) (bothrops Jajaraca)

SUBMITTER: Debora Andrade Silva

LAB HEAD: Solange Maria de Toledo Serrano

PROVIDER: PXD022696 | Pride | 2021-05-15

REPOSITORIES: Pride

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			Action	DRS
	Adult_evidence.txt	Txt
	Adult_peptides.txt	Txt
	Adult_proteinGroups.txt	Txt
	ListofRawfiles.xlsx	Xlsx
	Newborn_evidence.txt	Txt

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Publications

The distinct N-terminomes of Bothrops jararaca newborn and adult venoms.

Andrade-Silva Débora D Nishiyama Milton Y MY Stuginski Daniel R DR Zelanis André A Serrano Solange M T SMT

Biochimica et biophysica acta. Proteins and proteomics 20210313 7

Using approaches of transcriptomics and proteomics we have shown that the phenotype of Bothrops jararaca venom undergoes a significant rearrangement upon neonate to adult transition. Most regulatory processes in biology are intrinsically related to modifications of protein structure, function, and abundance. However, it is unclear to which extent intrinsic proteolysis affects toxins and snake venom phenotypes upon ontogenesis. Here we assessed the natural N-terminome of Bothrops jararaca newborn ...[more]

PMID: 33722654

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A systemic view of active site specificity profiling of the snake venom metalloprotease HF3 using Proteomic Identification of Cleavage Sites and N-terminomics TAILS

Project description:Snake venom metalloproteinases play important roles in the pathological effects of Viperidae venoms including severe local tissue damage, hemorrhage and coagulopathy. Hemorrhagic Factor 3 (HF3), a metalloproteinase isolated from Bothrops jararaca venom, induces severe local hemorrhage. Previous proteomic studies have shown that HF3 targets important ECM components, including collagens and proteoglycans, and plasma proteins. However, the full substrate repertoire of this metalloproteinase is unknown. Using Proteomic Identification of Cleavage Sites (PICS), a tryptic library derived from THP-1 monocytic cells was used as substrate for identifying protease cleavage sites and sequence preferences in peptides. 1,252 cleavage sites were detected and revealed a clear preference for Leu at P1′ position. A Terminal Amine Isotopic Labeling of Substrates (TAILS) analysis of the incubation of HF3 with mouse embryonic fibroblasts (MEF) secretome resulted in the identification of more than 3,600 cleavage sites in proteins, and confirmed the predominance of Leu at P1′ position. Various substrates were detected including ECM and focal adhesion proteins, and the cysteine proteinase inhibitor, cystatin-C. Interestingly, 597 peptides matched to annotated cleavage sites in the TopFIND database, suggesting that these cleavages might have been generated by other proteases activated upon incubation with HF3, including caspases -3 and -7, cathepsins D and E, granzyme B, and MMPs 2 and 9. Taken together, these results greatly expand the known substrate degradome of HF3, and reveals potential new targets which may serve as basis to better elucidate the complex pathophysiology of snake envenomation.

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