Products of the Polymerase-Encoding Region of the Coronavirus IBV

Brierley, Ian; Boursnell, M. E. G.; Binns, M. M.; Bilimoria, B.; Rolley, Nicola J.; Brown, T. D. K.; Inglis, Stephen

doi:10.1007/978-1-4684-5823-7_38

Cited by 14 publications

(9 citation statements)

References 15 publications

(9 reference statements)

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“…Several features of the IBV polymerase gene sequence , coupled with the absence of a distinct mRNA for ORF lb, suggested that translation of ORF l b involved ribosomal frameshifting from ORF la, thus synthesizing a large polyprotein containing both l a and l b sequences. Subsequently, a highly efficient (30% frequency) -1 frameshift was demonstrated experimentally in uitro (Brierley et al, 1987;Somogyi et al, 1993) and in uiuo (Brierly et al, 1990). This mechanism has been shown to operate in gene 1 of MHV, HCV-229E, and TGEV as well (Bredenbeek et al, 1990;Lee et al, 1991;Eleouet et al, 1995).…”

Section: Mechanisms Of Translationmentioning

confidence: 95%

The Molecular Biology of Coronaviruses

Lai

Cavanagh

1997

Advances in Virus Research

1,018

1,077

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Section: Mechanisms Of Translationmentioning

confidence: 95%

The Molecular Biology of Coronaviruses

Lai

Cavanagh

1997

Advances in Virus Research

1,018

1,077

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“…Throughout this and our previous report , this protein was referred to as 87 kDa based purely on its migration on linear SDS±PAGE. In an early communication, Brierley et al, (1990) noted that Western blots of IBV-infected chicken kidney cells and Vero cells with antiserum V59 led to the detection of a virus-specific polypeptide of 75 kDa. This 75-kDa protein was subsequently shown to migrate on linear SDS±PAGE at the same position as the 87-kDa product .…”

Section: Deletion Analysis Of the C-terminal Cleavage Site Of The 87-mentioning

confidence: 99%

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

Lim

Liu

1998

Virology

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In a previous report, we showed that proteolytic processing of an 87-kDa mature viral protein from the coronavirus infectious bronchitis virus (IBV) 1a and 1a/1b polyproteins was mediated by two putative overlapping papain-like proteinase domains (PLPDs) encoded within the region from nucleotides 4243 to 5553 of ORF 1a (Liu et al., 1995). In this study, we demonstrate that only the first domain, PLPD-1, is responsible for this cleavage, as deletion of the second domain did not affect the formation of the 87-kDa protein. Site-directed mutagenesis studies further showed that a previously predicted nucleophilic cysteine residue (Cys1274) and a histidine residue (His1437) were essential for the proteinase activity, indicating that they may be important components of the catalytic center of the proteinase. Meanwhile, expression of a series of deletion mutants revealed that the 87-kDa protein was encoded by the 5'-most 2.6 kb of ORF 1a. Deletion and amino acid substitution mutation studies demonstrated that the Gly673-Gly674 dipeptide bond was most likely the cleavage site responsible for releasing the C-terminus of the 87-kDa protein from the 1a and 1a/1b polyproteins.

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“…As described for other viral replicases, the CVL replicases are proteolytically cleaved into smaller active units. A number of cleavage products has recently been detected in coronavirus- (Brierley et al, 1990;Denison et al, 1991Denison et al, , 1992 and arterivirus-infected (Snijder etal., 1992; E. J. Snijder, A. L. M. Wassenaar & W. J. M. Spaan, unpublished) cells. The proteases involved in replicase protein processing are encoded by the ORF la sequence.…”

Section: Conserved Domains In Cvl Replicasesmentioning

confidence: 99%