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Article: Identification of lysine acetylation sites on MERS-CoV replicase pp1ab

TitleIdentification of lysine acetylation sites on MERS-CoV replicase pp1ab
Authors
KeywordsAcetylation
post-translational modifications
viruses
immunoaffinity
bioinformatics
Issue Date2020
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.mcponline.org/
Citation
Molecular & Cellular Proteomics, 2020, v. 19 n. 8, p. 1303-1309 How to Cite?
AbstractMERS is a life-threatening disease and MERS-CoV has the potential to cause the next pandemic. Protein acetylation is known to play a crucial role in host response to viral infection. Acetylation of viral proteins encoded by other RNA viruses have been reported to affect viral replication. It is therefore of interest to see whether MERS-CoV proteins are also acetylated. Viral proteins obtained from infected cells were trypsin-digested into peptides. Acetylated peptides were enriched by immunoprecipitation and subject to nano-LC-Orbitrap analysis. Bioinformatic analysis was performed to assess the conservation level of identified acetylation sites and to predict the upstream regulatory factors. A total of 12 acetylation sites were identified from 7 peptides, which all belong to the replicase polyprotein pp1ab. All identified acetylation sites were found to be highly conserved across MERS-CoV sequences in NCBI database. Upstream factors, including deacetylases of the SIRT1 and HDAC families as well as acetyltransferases of the TIP60 family, were predicted to be responsible for regulating the acetylation events identified. Western blotting confirms that acetylation events indeed occur on pp1ab protein by expressing NSP4 in HEK293 cells. Acetylation events on MERS-CoV viral protein pp1ab were identified for the first time, which indicate that MERS-CoV might use the host acetylation machinery to regulate its enzyme activity and to achieve optimal replication. Upstream factors were predicted, which might facilitate further analysis of the regulatory mechanism of MERS-CoV replication.
Persistent Identifierhttp://hdl.handle.net/10722/287921
ISSN
2019 Impact Factor: 4.87
2015 SCImago Journal Rankings: 3.213
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorZhu, L-
dc.contributor.authorFung, SY-
dc.contributor.authorXie, G-
dc.contributor.authorWONG, LYR-
dc.contributor.authorJin, DY-
dc.contributor.authorCai, Z-
dc.date.accessioned2020-10-05T12:05:11Z-
dc.date.available2020-10-05T12:05:11Z-
dc.date.issued2020-
dc.identifier.citationMolecular & Cellular Proteomics, 2020, v. 19 n. 8, p. 1303-1309-
dc.identifier.issn1535-9476-
dc.identifier.urihttp://hdl.handle.net/10722/287921-
dc.description.abstractMERS is a life-threatening disease and MERS-CoV has the potential to cause the next pandemic. Protein acetylation is known to play a crucial role in host response to viral infection. Acetylation of viral proteins encoded by other RNA viruses have been reported to affect viral replication. It is therefore of interest to see whether MERS-CoV proteins are also acetylated. Viral proteins obtained from infected cells were trypsin-digested into peptides. Acetylated peptides were enriched by immunoprecipitation and subject to nano-LC-Orbitrap analysis. Bioinformatic analysis was performed to assess the conservation level of identified acetylation sites and to predict the upstream regulatory factors. A total of 12 acetylation sites were identified from 7 peptides, which all belong to the replicase polyprotein pp1ab. All identified acetylation sites were found to be highly conserved across MERS-CoV sequences in NCBI database. Upstream factors, including deacetylases of the SIRT1 and HDAC families as well as acetyltransferases of the TIP60 family, were predicted to be responsible for regulating the acetylation events identified. Western blotting confirms that acetylation events indeed occur on pp1ab protein by expressing NSP4 in HEK293 cells. Acetylation events on MERS-CoV viral protein pp1ab were identified for the first time, which indicate that MERS-CoV might use the host acetylation machinery to regulate its enzyme activity and to achieve optimal replication. Upstream factors were predicted, which might facilitate further analysis of the regulatory mechanism of MERS-CoV replication.-
dc.languageeng-
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.mcponline.org/-
dc.relation.ispartofMolecular & Cellular Proteomics-
dc.rightsMolecular & Cellular Proteomics. Copyright © American Society for Biochemistry and Molecular Biology, Inc.-
dc.rightsThis research was originally published in the [Journal Name]. Author(s). Title. Journal Name. Year; Vol:pp-pp. © the American Society for Biochemistry and Molecular Biology or © the Author(s).-
dc.subjectAcetylation-
dc.subjectpost-translational modifications-
dc.subjectviruses-
dc.subjectimmunoaffinity-
dc.subjectbioinformatics-
dc.titleIdentification of lysine acetylation sites on MERS-CoV replicase pp1ab-
dc.typeArticle-
dc.identifier.emailFung, SY: kittyfsy@connect.hku.hk-
dc.identifier.emailJin, DY: dyjin@hku.hk-
dc.identifier.authorityJin, DY=rp00452-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1074/mcp.RA119.001897-
dc.identifier.pmid32424026-
dc.identifier.scopuseid_2-s2.0-85089127199-
dc.identifier.scopuseid_2-s2.0-85089127199-
dc.identifier.hkuros315277-
dc.identifier.volume19-
dc.identifier.issue8-
dc.identifier.spage1303-
dc.identifier.epage1309-
dc.identifier.isiWOS:000561114000004-
dc.publisher.placeUnited States-
dc.identifier.issnl1535-9476-

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