|How to cite this article:
Wiwanitkit S, Wiwanitkit V. Prediction of enzyme cleavage possibility on Ebola virus glycoprotein by PeptideCutter. Ann Trop Med Public Health 2015;8:317
|How to cite this URL:
Wiwanitkit S, Wiwanitkit V. Prediction of enzyme cleavage possibility on Ebola virus glycoprotein by PeptideCutter. Ann Trop Med Public Health [serial online] 2015 [cited 2020 Dec 2];8:317. Available from: https://www.atmph.org/text.asp?2015/8/6/317/162632
As a new emerging disease, knowledge on Ebola virus genomics and proteomics is still limited. Basically, the structure of the virus is strongly related to viral infectivity as well as drug and vaccine response. For the Ebola virus, the cleavage at its glycoprotein has been proved for the relation to the required process for fusion that is needed for cellular infection.  Here, the authors perform a proteomics study to assess several enzymes regarding their ability to make a cleavage. The standard proteomics tool, PeptideCutter (Swiss Institute of Bioinformatics) (http://web.expasy.org/peptide_cutter/) was used (the tool was used in several previous proteomics studies , ). Several enzymes can display cleavage ability [Table 1], whereas caspase 1, caspase 2, caspase 3, caspase 4, caspase 5, caspase 6, caspase 7, caspase 8, caspase 9, caspase 10, enterokinase, factor Xa, granzyme B, and tobacco etch virus protease have no ability. This information can be good basic data for further biochemical and proteomics studies.
|Table 1: Enzymes that can make a cleavage
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