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Serine protease isoforms in Gloydius intermedius venom: Full sequences, molecular phylogeny and evolutionary
Zhang-Min Yang1, Hui Yu2, Zhen-Zhen Liu2
1National Laboratory for Development of Endangered Drug Resources in Northwest China, College of Life Sciences, Shaanxi Normal University, Xi'an, Shaanxi, 710062, China; Innovation Center for Qinba region Stainable Development, College of Life Sciences, Shaanxi Normal University, Xi'an, Shaanxi, 710062, China.
Journal of Proteomics
|May 31, 2017
Summary
Nine venom serine proteases (vSPs) from Gloydius intermedius were analyzed, revealing diverse isoforms and evolutionary insights. Neurotoxic venoms contain more hypotensive vSPs, suggesting therapeutic potential.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Venomous snakes, particularly pitvipers, possess complex venom compositions.
- Serine proteases (vSPs) are a major component of snake venoms, contributing to diverse physiological effects.
- Gloydius intermedius venom composition and the evolutionary history of its vSPs remain incompletely understood.
Purpose of the Study:
- To comprehensively characterize the nine distinct venom serine proteases (vSPs) of Gloydius intermedius.
- To elucidate the evolutionary relationships and diversification of these vSPs within pitvipers.
- To investigate the correlation between vSP types and venom toxicity (neurotoxic vs. hemorrhagic).
Main Methods:
- Transcriptomic and sub-proteomic analyses to identify and sequence vSPs.
- cDNA cloning and sequencing for full amino acid sequence determination.
- Quantitative PCR (qPCR) for expression level analysis.
- High-Performance Liquid Chromatography (HPLC) and Liquid Chromatography-Mass Spectrometry/Mass Spectrometry (LC-MS/MS) for purification and identification.
- Amidolytic activity assays using chromogenic substrates.
- Molecular phylogenetic analysis to determine evolutionary relationships.
Main Results:
- Nine paralogous vSPs (GiSPs) were identified in Gloydius intermedius venom.
- Full amino acid sequences revealed catalytic triads and potential N-glycosylation sites.
- Expression levels correlated with EST hit-numbers; kallikrein-like and plasminogen activator-like vSPs were abundant.
- Phylogenetic analysis identified six major vSP subtypes, indicating ancient diversification.
- Sequence similarities suggest vSP evolution predates Asian pitviper migration to the New World.
- Neurotoxic G. intermedius venoms showed higher levels of hypotensive vSPs compared to hemorrhagic venoms.
Conclusions:
- Gloydius intermedius venom exhibits a diverse repertoire of vSPs with ancient evolutionary origins.
- The composition of vSPs, particularly the abundance of hypotensive isoforms in neurotoxic venom, provides insights into venom function.
- Understanding vSP variation and evolution aids in identifying potential therapeutic or diagnostic agents from snake venoms.
Keywords:
Full protein sequenceGloydius intermedius, venom serine proteasePeptide mass fingerprintingPhylogenetic analysisQuantitative real-time PCRMore Related Videos
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