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Article: In silico analysis of ORF1ab in coronavirus HKU1 genome reveals a unique putative cleavage site of coronavirus HKU1 3C-like protease

TitleIn silico analysis of ORF1ab in coronavirus HKU1 genome reveals a unique putative cleavage site of coronavirus HKU1 3C-like protease
Authors
Issue Date2005
PublisherCenter for Academic Publications Japan. The Journal's web site is located at http://www.sanbi.co.jp/capj/index.html
Citation
Microbiology And Immunology, 2005, v. 49 n. 10, p. 899-908 How to Cite?
AbstractRecently we have described the discovery and complete genome sequence of a novel coronavirus associated with pneumonia, coronavirus HKU1 (CoV-HKU1). In this study, a detailed in silica analysis of the ORF1ab, encoding the 7,182-amino acid replicase polyprotein in the CoV-HKU1 genome showed that the replicase polyprotein of CoV-HKU1 is cleaved by its papain-like proteases and 3C-like protease (3CLpro) into 16 polypeptides homologous to the corresponding polypeptides in other coronaviruses. Surprisingly, analysis of the putative cleavage sites of the 3CLpro revealed a unique putative cleavage site. In all known coronaviruses, the P1 positions at the cleavage sites of the 3CLpro are occupied by glutamine. This is also observed in CoV-HKU1, except for one site at the junction between nsp10 (helicase) and nsp11 (member of exonuclease family), where the P1 position is occupied by histidine. This amino acid substitution is due to a single nucleotide mutation in the CoV-HKU1 genome, CAG/A to CAT. This probably represents a novel cleavage site because the same mutation was consistently observed in CoV-HKU1 sequences from multiple specimens of different patients; the P2 and P1′-P12′ positions of this cleavage site are consistent between CoV-HKU1 and other coronaviruses; and as the helicase is one of the most conserved proteins in coronaviruses, cleavage between nsp10 and nsp11 should be an essential step for the generation of the mature functional helicase. Experiments, including purification and C-terminal amino acid sequencing of the CoV-HKU1 helicase and trans-cleavage assays of the CoV-HKU1 3CLpro will confirm the presence of this novel cleavage site.
Persistent Identifierhttp://hdl.handle.net/10722/79036
ISSN
2015 Impact Factor: 1.428
2015 SCImago Journal Rankings: 0.695
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWoo, PCYen_HK
dc.contributor.authorHuang, Yen_HK
dc.contributor.authorLau, SKPen_HK
dc.contributor.authorTsoi, HWen_HK
dc.contributor.authorYuen, KYen_HK
dc.date.accessioned2010-09-06T07:49:49Z-
dc.date.available2010-09-06T07:49:49Z-
dc.date.issued2005en_HK
dc.identifier.citationMicrobiology And Immunology, 2005, v. 49 n. 10, p. 899-908en_HK
dc.identifier.issn0385-5600en_HK
dc.identifier.urihttp://hdl.handle.net/10722/79036-
dc.description.abstractRecently we have described the discovery and complete genome sequence of a novel coronavirus associated with pneumonia, coronavirus HKU1 (CoV-HKU1). In this study, a detailed in silica analysis of the ORF1ab, encoding the 7,182-amino acid replicase polyprotein in the CoV-HKU1 genome showed that the replicase polyprotein of CoV-HKU1 is cleaved by its papain-like proteases and 3C-like protease (3CLpro) into 16 polypeptides homologous to the corresponding polypeptides in other coronaviruses. Surprisingly, analysis of the putative cleavage sites of the 3CLpro revealed a unique putative cleavage site. In all known coronaviruses, the P1 positions at the cleavage sites of the 3CLpro are occupied by glutamine. This is also observed in CoV-HKU1, except for one site at the junction between nsp10 (helicase) and nsp11 (member of exonuclease family), where the P1 position is occupied by histidine. This amino acid substitution is due to a single nucleotide mutation in the CoV-HKU1 genome, CAG/A to CAT. This probably represents a novel cleavage site because the same mutation was consistently observed in CoV-HKU1 sequences from multiple specimens of different patients; the P2 and P1′-P12′ positions of this cleavage site are consistent between CoV-HKU1 and other coronaviruses; and as the helicase is one of the most conserved proteins in coronaviruses, cleavage between nsp10 and nsp11 should be an essential step for the generation of the mature functional helicase. Experiments, including purification and C-terminal amino acid sequencing of the CoV-HKU1 helicase and trans-cleavage assays of the CoV-HKU1 3CLpro will confirm the presence of this novel cleavage site.en_HK
dc.languageengen_HK
dc.publisherCenter for Academic Publications Japan. The Journal's web site is located at http://www.sanbi.co.jp/capj/index.htmlen_HK
dc.relation.ispartofMicrobiology and Immunologyen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAmino Acid Substitutionen_HK
dc.subject.meshComputational Biologyen_HK
dc.subject.meshCoronavirus - geneticsen_HK
dc.subject.meshCysteine Endopeptidases - metabolismen_HK
dc.subject.meshGlutamineen_HK
dc.subject.meshHistidineen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshOpen Reading Frames - geneticsen_HK
dc.subject.meshPoint Mutationen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshSequence Alignmenten_HK
dc.subject.meshViral Proteins - chemistry - genetics - metabolismen_HK
dc.titleIn silico analysis of ORF1ab in coronavirus HKU1 genome reveals a unique putative cleavage site of coronavirus HKU1 3C-like proteaseen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0385-5600&volume=49&spage=899&epage=908&date=2005&atitle=In+silico+analysis+of+ORF1ab+in+coronavirus+HKU1+genome+reveals+a+unique+putative+cleavage+site+of+coronavirus+HKU1+3C-like+proteaseen_HK
dc.identifier.emailWoo, PCY:pcywoo@hkucc.hku.hken_HK
dc.identifier.emailLau, SKP:skplau@hkucc.hku.hken_HK
dc.identifier.emailTsoi, HW:hwtsoi@hkucc.hku.hken_HK
dc.identifier.emailYuen, KY:kyyuen@hkucc.hku.hken_HK
dc.identifier.authorityWoo, PCY=rp00430en_HK
dc.identifier.authorityLau, SKP=rp00486en_HK
dc.identifier.authorityTsoi, HW=rp00439en_HK
dc.identifier.authorityYuen, KY=rp00366en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid16237267-
dc.identifier.scopuseid_2-s2.0-27544447345en_HK
dc.identifier.hkuros114684en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-27544447345&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume49en_HK
dc.identifier.issue10en_HK
dc.identifier.spage899en_HK
dc.identifier.epage908en_HK
dc.identifier.isiWOS:000232434600003-
dc.publisher.placeJapanen_HK
dc.identifier.scopusauthoridWoo, PCY=7201801340en_HK
dc.identifier.scopusauthoridHuang, Y=35597414700en_HK
dc.identifier.scopusauthoridLau, SKP=7401596211en_HK
dc.identifier.scopusauthoridTsoi, HW=6603822102en_HK
dc.identifier.scopusauthoridYuen, KY=36078079100en_HK

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