Hepatitis E Virus Cysteine Protease Has Papain Like Properties Validated by in silico Modeling and Cell-Free Inhibition Assays
Identifieur interne : 000342 ( an2020/Analysis ); précédent : 000341; suivant : 000343Hepatitis E Virus Cysteine Protease Has Papain Like Properties Validated by in silico Modeling and Cell-Free Inhibition Assays
Auteurs : Shweta Saraswat ; Meenakshi Chaudhary ; Deepak SehgalSource :
- Frontiers in Cellular and Infection Microbiology [ 2235-2988 ] ; 2020.
Abstract
Hepatitis E virus (HEV) has emerged as a global health concern during the last decade. In spite of a high mortality rate in pregnant women with fulminant hepatitis, no antiviral drugs or licensed vaccine is available in India. HEV-protease is a pivotal enzyme responsible for ORF1 polyprotein processing leading to cleavage of the non-structural enzymes involved in virus replication. HEV-protease region encoding 432–592 amino acids of Genotype-1 was amplified, expressed in Sf21 cells and purified in its native form. The recombinant enzyme was biochemically characterized using SDS-PAGE, Western blotting and Immunofluorescence. The enzyme activity and the inhibition studies were conducted using Zymography, FTC-casein based protease assay and ORF1 polyprotein digestion. To conduct ORF1 digestion assay, the polyprotein, natural substrate of HEV-protease, was expressed in
Url:
DOI: 10.3389/fcimb.2019.00478
PubMed: 32039053
PubMed Central: 6989534
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Hepatitis E Virus Cysteine Protease Has Papain Like Properties Validated by <italic>in silico</italic> Modeling and Cell-Free Inhibition Assays</title><author><name sortKey="Saraswat, Shweta" sort="Saraswat, Shweta" uniqKey="Saraswat S" first="Shweta" last="Saraswat">Shweta Saraswat</name></author><author><name sortKey="Chaudhary, Meenakshi" sort="Chaudhary, Meenakshi" uniqKey="Chaudhary M" first="Meenakshi" last="Chaudhary">Meenakshi Chaudhary</name></author><author><name sortKey="Sehgal, Deepak" sort="Sehgal, Deepak" uniqKey="Sehgal D" first="Deepak" last="Sehgal">Deepak Sehgal</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">32039053</idno><idno type="pmc">6989534</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6989534</idno><idno type="RBID">PMC:6989534</idno><idno type="doi">10.3389/fcimb.2019.00478</idno><date when="2020">2020</date><idno type="wicri:Area/Pmc/Corpus">000573</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000573</idno><idno type="wicri:Area/Pmc/Curation">000573</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000573</idno><idno type="wicri:Area/Pmc/Checkpoint">000030</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000030</idno><idno type="wicri:Area/Ncbi/Merge">000819</idno><idno type="wicri:Area/Ncbi/Curation">000819</idno><idno type="wicri:Area/Ncbi/Checkpoint">000819</idno><idno type="wicri:Area/Main/Merge">000344</idno><idno type="wicri:Area/Main/Curation">000342</idno><idno type="wicri:Area/Main/Exploration">000342</idno><idno type="wicri:Area/an2020/Extraction">000342</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Hepatitis E Virus Cysteine Protease Has Papain Like Properties Validated by <italic>in silico</italic> Modeling and Cell-Free Inhibition Assays</title><author><name sortKey="Saraswat, Shweta" sort="Saraswat, Shweta" uniqKey="Saraswat S" first="Shweta" last="Saraswat">Shweta Saraswat</name></author><author><name sortKey="Chaudhary, Meenakshi" sort="Chaudhary, Meenakshi" uniqKey="Chaudhary M" first="Meenakshi" last="Chaudhary">Meenakshi Chaudhary</name></author><author><name sortKey="Sehgal, Deepak" sort="Sehgal, Deepak" uniqKey="Sehgal D" first="Deepak" last="Sehgal">Deepak Sehgal</name></author></analytic><series><title level="j">Frontiers in Cellular and Infection Microbiology</title><idno type="eISSN">2235-2988</idno><imprint><date when="2020">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Hepatitis E virus (HEV) has emerged as a global health concern during the last decade. In spite of a high mortality rate in pregnant women with fulminant hepatitis, no antiviral drugs or licensed vaccine is available in India. HEV-protease is a pivotal enzyme responsible for ORF1 polyprotein processing leading to cleavage of the non-structural enzymes involved in virus replication. HEV-protease region encoding 432–592 amino acids of Genotype-1 was amplified, expressed in Sf21 cells and purified in its native form. The recombinant enzyme was biochemically characterized using SDS-PAGE, Western blotting and Immunofluorescence. The enzyme activity and the inhibition studies were conducted using Zymography, FTC-casein based protease assay and ORF1 polyprotein digestion. To conduct ORF1 digestion assay, the polyprotein, natural substrate of HEV-protease, was expressed in <italic>E. coli</italic> and purified. Cleavage of 186 kDa ORF1 polyprotein by the recombinant HEV-protease lead to appearance of non-structural proteins viz. Methyltransferase, Protease, Helicase and RNA dependent RNA polymerase which were confirmed through immunoblotting using antibodies generated against specific epitopes of the enzymes. FTC-casein substrate was used for kinetic studies to determine Km and Vmax of the enzyme and also the effect of different metal ions and other protease inhibitors. A 95% inhibition was observed with E-64 which was validated through <italic>in silico</italic> analysis. The correlation coefficient between inhibition and docking score of Inhibitors was found to have a significant value of <italic>r</italic><sup>2</sup> = 0.75. The predicted 3D model showed two domain architecture structures similar to Papain like cysteine protease though they differed in arrangements of alpha helices and beta sheets. Hence, we propose that HEV-protease has characteristics of “Papain-like cysteine protease,” as determined through structural homology, active site residues and class-specific inhibition. 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Siddell</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Chaudhary, Meenakshi" sort="Chaudhary, Meenakshi" uniqKey="Chaudhary M" first="Meenakshi" last="Chaudhary">Meenakshi Chaudhary</name><name sortKey="Saraswat, Shweta" sort="Saraswat, Shweta" uniqKey="Saraswat S" first="Shweta" last="Saraswat">Shweta Saraswat</name><name sortKey="Sehgal, Deepak" sort="Sehgal, Deepak" uniqKey="Sehgal D" first="Deepak" last="Sehgal">Deepak Sehgal</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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