{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T06:39:05Z","timestamp":1790750345009,"version":"4.1.0"},"reference-count":41,"publisher":"Microbiology Society","issue":"3","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2006,3,1]]},"abstract":"The replicase polyproteins, pp1a and pp1ab, of porcine Transmissible gastroenteritis virus<\/jats:italic> (TGEV) have been predicted to be cleaved by viral proteases into 16 non-structural proteins (nsp). Here, enzymic activities residing in the amino-proximal region of nsp3, the largest TGEV replicase processing product, were characterized. It was shown, by in vitro<\/jats:italic> translation experiments and protein sequencing, that the papain-like protease 1, PL1pro<\/jats:sup>, but not a mutant derivative containing a substitution of the presumed active-site nucleophile, Cys1093<\/jats:sup>, cleaves the nsp2|nsp3 site at 879<\/jats:sup>Gly|Gly880<\/jats:sup>. By using an antiserum raised against the pp1a\/pp1ab residues 526\u2013713, the upstream processing product, nsp2, was identified as an 85\u2005kDa protein in TGEV-infected cells. Furthermore, PL1pro<\/jats:sup> was confirmed to be flanked at its C terminus by a domain (called X) that mediates ADP-ribose 1\u2033-phosphatase activity. Expression and characterization of a range of bacterially expressed forms of this enzyme suggest that the active X domain comprises pp1a\/pp1ab residues Asp1320<\/jats:sup>\u2013Ser1486<\/jats:sup>.<\/jats:p>","DOI":"10.1099\/vir.0.81596-0","type":"journal-article","created":{"date-parts":[[2006,2,13]],"date-time":"2006-02-13T21:58:34Z","timestamp":1139867914000},"page":"651-656","source":"Crossref","is-referenced-by-count":47,"title":["Identification of protease and ADP-ribose 1\u2033-monophosphatase activities associated with transmissible gastroenteritis virus non-structural protein 3"],"prefix":"10.1099","volume":"87","author":[{"given":"\u00c1kos","family":"Putics","sequence":"first","affiliation":[{"name":"Institute of Virology and Immunology, University of W\u00fcrzburg, Versbacher Stra\u00dfe 7, 97078 W\u00fcrzburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander E.","family":"Gorbalenya","sequence":"additional","affiliation":[{"name":"Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Leiden, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"Ziebuhr","sequence":"additional","affiliation":[{"name":"Institute of Virology and Immunology, University of W\u00fcrzburg, Versbacher Stra\u00dfe 7, 97078 W\u00fcrzburg, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"12683","DOI":"10.1128\/JVI.78.22.12683-12688.2004","article-title":"The nucleoprotein is required for efficient coronavirus genome replication","volume":"78","author":"Almaz\u00e1n","year":"2004","journal-title":"J Virol"},{"key":"R2","doi-asserted-by":"crossref","first-page":"3213","DOI":"10.1093\/emboj\/cdf327","article-title":"Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra \u03b1 -helical domain","volume":"21","author":"Anand","year":"2002","journal-title":"EMBO J"},{"key":"R3","doi-asserted-by":"crossref","first-page":"1763","DOI":"10.1126\/science.1085658","article-title":"Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs","volume":"300","author":"Anand","year":"2003","journal-title":"Science"},{"key":"R4","doi-asserted-by":"crossref","first-page":"12218","DOI":"10.1128\/JVI.78.22.12218-12224.2004","article-title":"The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor","volume":"78","author":"Bhardwaj","year":"2004","journal-title":"J Virol"},{"key":"R5","doi-asserted-by":"crossref","first-page":"900","DOI":"10.1128\/JVI.71.2.900-909.1997","article-title":"Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59","volume":"71","author":"Bonilla","year":"1997","journal-title":"J Virol"},{"key":"R6","doi-asserted-by":"crossref","first-page":"3779","DOI":"10.1002\/j.1460-2075.1987.tb02713.x","article-title":"An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV","volume":"6","author":"Brierley","year":"1987","journal-title":"EMBO J"},{"key":"R7","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1006\/viro.1994.1567","article-title":"Determinants of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus","volume":"204","author":"Dong","year":"1994","journal-title":"Virology"},{"key":"R8","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.virusres.2005.07.005","article-title":"The complete sequence of the bovine torovirus genome","volume":"115","author":"Draker","year":"2006","journal-title":"Virus Res"},{"key":"R9","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1006\/viro.1995.1004","article-title":"Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus","volume":"206","author":"Eleouet","year":"1995","journal-title":"Virology"},{"key":"R10","doi-asserted-by":"crossref","first-page":"13211","DOI":"10.1074\/jbc.272.20.13211","article-title":"Cloning and characterization of the Arabidopsis cyclic phosphodiesterase which hydrolyzes ADP-ribose 1\u2033,2\u2033-cyclic phosphate and nucleoside 2\u2032,3\u2032-cyclic phosphates","volume":"272","author":"Genschik","year":"1997","journal-title":"J Biol Chem"},{"key":"R11","doi-asserted-by":"crossref","first-page":"2207","DOI":"10.1007\/s00705-003-0162-1","article-title":"A comparative sequence analysis to revise the current taxonomy of the family Coronaviridae","volume":"148","author":"Gonz\u00e1lez","year":"2003","journal-title":"Arch Virol"},{"key":"R12","doi-asserted-by":"crossref","first-page":"4847","DOI":"10.1093\/nar\/17.12.4847","article-title":"Coronavirus genome: prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis","volume":"17","author":"Gorbalenya","year":"1989","journal-title":"Nucleic Acids Res"},{"key":"R13","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/0014-5793(91)81034-6","article-title":"Putative papain-related thiol proteases of positive-strand RNA viruses. Identification of rubi- and aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, \u03b1 - and coronaviruses","volume":"288","author":"Gorbalenya","year":"1991","journal-title":"FEBS Lett"},{"key":"R14","doi-asserted-by":"crossref","first-page":"13600","DOI":"10.1128\/JVI.78.24.13600-13612.2004","article-title":"Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity","volume":"78","author":"Harcourt","year":"2004","journal-title":"J Virol"},{"key":"R15","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1099\/0022-1317-83-3-595","article-title":"Conservation of substrate specificities among coronavirus main proteases","volume":"83","author":"Hegyi","year":"2002","journal-title":"J Gen Virol"},{"key":"R16","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1128\/JVI.72.2.910-918.1998","article-title":"Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: identification of a papain-like proteinase and its substrate","volume":"72","author":"Herold","year":"1998","journal-title":"J Virol"},{"key":"R17","doi-asserted-by":"crossref","first-page":"14918","DOI":"10.1074\/jbc.274.21.14918","article-title":"A human RNA viral cysteine proteinase that depends upon a unique Zn2+-binding finger connecting the two domains of a papain-like fold","volume":"274","author":"Herold","year":"1999","journal-title":"J Biol Chem"},{"key":"R18","doi-asserted-by":"crossref","first-page":"7833","DOI":"10.1128\/JVI.78.14.7833-7838.2004","article-title":"Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5\u2032-triphosphatase activities","volume":"78","author":"Ivanov","year":"2004","journal-title":"J Virol"},{"key":"R19","doi-asserted-by":"crossref","first-page":"12694","DOI":"10.1073\/pnas.0403127101","article-title":"Major genetic marker of nidoviruses encodes a replicative endoribonuclease","volume":"101","author":"Ivanov","year":"2004a","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R20","doi-asserted-by":"crossref","first-page":"5619","DOI":"10.1128\/JVI.78.11.5619-5632.2004","article-title":"Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase","volume":"78","author":"Ivanov","year":"2004b","journal-title":"J Virol"},{"key":"R21","doi-asserted-by":"crossref","first-page":"7911","DOI":"10.1128\/JVI.74.17.7911-7921.2000","article-title":"Identification of mouse hepatitis virus papain-like proteinase 2 activity","volume":"74","author":"Kanjanahaluethai","year":"2000","journal-title":"J Virol"},{"key":"R22","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.1038\/sj.emboj.7600664","article-title":"The macro domain is an ADP-ribose binding module","volume":"24","author":"Karras","year":"2005","journal-title":"EMBO J"},{"key":"R23","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1006\/viro.1998.9164","article-title":"Characterization of the two overlapping papain-like proteinase domains encoded in gene 1 of the coronavirus infectious bronchitis virus and determination of the C-terminal cleavage site of an 87-kDa protein","volume":"245","author":"Lim","year":"1998","journal-title":"Virology"},{"key":"R24","doi-asserted-by":"crossref","first-page":"1674","DOI":"10.1128\/JVI.74.4.1674-1685.2000","article-title":"Identification of a novel cleavage activity of the first papain-like proteinase domain encoded by open reading frame 1a of the coronavirus Avian infectious bronchitis virus and characterization of the cleavage products","volume":"74","author":"Lim","year":"2000","journal-title":"J Virol"},{"key":"R25","doi-asserted-by":"crossref","first-page":"3554","DOI":"10.1128\/JVI.69.6.3554-3559.1995","article-title":"Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59","volume":"69","author":"Lu","year":"1995","journal-title":"J Virol"},{"key":"R26","doi-asserted-by":"crossref","first-page":"12721","DOI":"10.1128\/JVI.79.20.12721-12731.2005","article-title":"ADP-ribose-1\u2033-monophosphatase: a conserved coronavirus enzyme that is dispensable for viral replication in tissue culture","volume":"79","author":"Putics","year":"2005","journal-title":"J Virol"},{"key":"R27","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1007\/978-1-4615-1899-0_79","article-title":"Coronaviruses use discontinuous extension for synthesis of subgenome-length negative strands","volume":"380","author":"Sawicki","year":"1995","journal-title":"Adv Exp Med Biol"},{"key":"R28","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1007\/978-1-4615-5331-1_26","article-title":"A new model for coronavirus transcription","volume":"440","author":"Sawicki","year":"1998","journal-title":"Adv Exp Med Biol"},{"key":"R29","doi-asserted-by":"crossref","first-page":"6620","DOI":"10.1128\/JVI.79.11.6620-6630.2005","article-title":"Selective replication of coronavirus genomes that express nucleocapsid protein","volume":"79","author":"Schelle","year":"2005","journal-title":"J Virol"},{"key":"R30","doi-asserted-by":"crossref","first-page":"1056","DOI":"10.1017\/S1355838200000728","article-title":"The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5\u2032-to-3\u2032 polarity","volume":"6","author":"Seybert","year":"2000","journal-title":"RNA"},{"key":"R31","first-page":"95","article-title":"Viral and cellular proteins involved in coronavirus replication","volume":"287","author":"Shi","year":"2005","journal-title":"Curr Top Microbiol Immunol"},{"key":"R32","first-page":"823","article-title":"Coronaviruses, toroviruses, and arteriviruses","volume-title":"In Topley and Wilson's Microbiology and Microbial Infections","author":"Siddell","year":"2005"},{"key":"R33","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1016\/S0022-2836(03)00865-9","article-title":"Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage","volume":"331","author":"Snijder","year":"2003","journal-title":"J Mol Biol"},{"key":"R34","doi-asserted-by":"crossref","first-page":"2305","DOI":"10.1099\/vir.0.19424-0","article-title":"Mechanisms and enzymes involved in SARS coronavirus genome expression","volume":"84","author":"Thiel","year":"2003","journal-title":"J Gen Virol"},{"key":"R35","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1038\/nm1024","article-title":"Identification of a new human coronavirus","volume":"10","author":"van der Hoek","year":"2004","journal-title":"Nat Med"},{"key":"R36","first-page":"57","article-title":"The coronavirus replicase","volume":"287","author":"Ziebuhr","year":"2005","journal-title":"Curr Top Microbiol Immunol"},{"key":"R37","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1128\/JVI.73.1.177-185.1999","article-title":"Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: identification of proteolytic products and cleavage sites common to pp1a and pp1ab","volume":"73","author":"Ziebuhr","year":"1999","journal-title":"J Virol"},{"key":"R38","doi-asserted-by":"crossref","first-page":"4331","DOI":"10.1128\/JVI.69.7.4331-4338.1995","article-title":"Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity","volume":"69","author":"Ziebuhr","year":"1995","journal-title":"J Virol"},{"key":"R39","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1099\/0022-1317-81-4-853","article-title":"Virus-encoded proteinases and proteolytic processing in the Nidovirales","volume":"81","author":"Ziebuhr","year":"2000","journal-title":"J Gen Virol"},{"key":"R40","doi-asserted-by":"crossref","first-page":"33220","DOI":"10.1074\/jbc.M104097200","article-title":"The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond","volume":"276","author":"Ziebuhr","year":"2001","journal-title":"J Biol Chem"},{"key":"R41","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1128\/JVI.78.2.980-994.2004","article-title":"Sequence motifs involved in the regulation of discontinuous coronavirus subgenomic RNA synthesis","volume":"78","author":"Z\u00fa\u00f1iga","year":"2004","journal-title":"J Virol"}],"container-title":["Journal of General Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/jgv\/10.1099\/vir.0.81596-0?crawler=true","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,10,6]],"date-time":"2020-10-06T12:23:22Z","timestamp":1601987002000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/jgv\/10.1099\/vir.0.81596-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,3,1]]},"references-count":41,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2006,3,1]]}},"URL":"https:\/\/doi.org\/10.1099\/vir.0.81596-0","relation":{},"ISSN":["0022-1317","1465-2099"],"issn-type":[{"value":"0022-1317","type":"print"},{"value":"1465-2099","type":"electronic"}],"subject":[],"published":{"date-parts":[[2006,3,1]]}}}