Proteomic characterization and comparison of Malaysian Tropidolaemus wagleri and Cryptelytrops purpureomaculatus venom using shotgun-proteomics
Tropidolaemus wagleri and Cryptelytrops purpureomaculatus are venomous pit viper species commonly found in Malaysia. Tandem mass spectrometry analysis of the crude venoms has detected different proteins in T. wagleri and C.purpureomaculatus. They were classified into 13 venom protein families consi...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English English English |
| Published: |
Multidisciplinary Digital Publishing Institute (MDPI)
2016
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| Online Access: | http://irep.iium.edu.my/52355/1/2016_Syafiq_Toxins_Proteomic%20of%20Viper%20Venom.pdf http://irep.iium.edu.my/52355/7/52355_Proteomic%20characterization_WOS_SCOPUS.pdf http://irep.iium.edu.my/52355/12/52355_Proteomic%20characterization%20and%20comparison_scopus.pdf http://irep.iium.edu.my/52355/ http://www.mdpi.com/2072-6651/8/10/299/htm |
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| Summary: | Tropidolaemus wagleri and Cryptelytrops purpureomaculatus are venomous pit viper species commonly found in Malaysia. Tandem mass spectrometry analysis of the crude venoms has
detected different proteins in T. wagleri and C.purpureomaculatus. They were classified into 13 venom protein families consisting of enzymatic and nonenzymatic proteins. Enzymatic families detected in T. wagleri and C. purpureomaculatus venom were snake venom metalloproteinase, phospholipase A2, L-amino acid oxidase, serine proteases, 50-nucleotidase, phosphodiesterase, and phospholipase B. In addition, glutaminyl cyclotransferase was detected in C. purpureomaculatus. C-type lectin-like proteins were common nonenzymatic components in both species. Waglerin was present and unique to T. wagleri—it was not in C. purpureomaculatus venom. In contrast, cysteine-rich secretory protein,bradykinin-potentiating peptide, and C-type natriuretic peptide were present in C. purpureomaculatus venom. Composition of the venom proteome of T. wagleri and C. purpureomaculatus provides useful information to guide production of effective antivenom and identification of proteins with potential therapeutic applications. |
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