Prediction of enzyme cleavage possibility on Ebola virus glycoprotein by PeptideCutter

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

Dear Sir,

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. [1] 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 [2],[3] ). 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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Conflicts of interest

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References

 

1.
Brecher M, Schornberg KL, Delos SE, Fusco ML, Saphire EO, White JM. Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change. J Virol 2012;86:364-72.
2.
Lafarga T, O’Connor P, Hayes M. Identification of novel dipeptidyl peptidase-IV and angiotensin-I-converting enzyme inhibitory peptides from meat proteins using in silico analysis. Peptides 2014;59:53-62.
3.
Lafarga T, O’Connor P, Hayes M. In silico methods to identify meat-derived prolyl endopeptidase inhibitors. Food Chem 2015;175:337-43.

Source of Support: None, Conflict of Interest: None

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DOI: 10.4103/1755-6783.162632

Tables

[Table 1]

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