Abstract
Human coronavirus 229E gene expression involves proteolytic processing of the gene 1-encoded polyproteins pp1a and pp1ab. In this study, we have detected a 71-kDa polypeptide in virus-infected cells that is released from pp1ab by the virus-encoded 3C-like proteinase and that has been predicted to contain both metal-binding and helicase domains. The polypeptide encompasses amino acids Ala-4996 to Gln-5592 of pp1ab and exhibits nucleic acid-stimulated ATPase activity when expressed as a fusion protein with the Escherichia coli maltose-binding protein. These data provide the first identification of a coronavirus open reading frame 1b-encoded enzymatic activity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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3C Viral Proteases
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism*
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Adenosine Triphosphate / metabolism
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Binding Sites
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Cell Line
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Coronavirus / enzymology*
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Coronavirus / genetics
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Coronavirus 229E, Human*
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Cysteine Endopeptidases / metabolism
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Humans
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Peptides / genetics
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Peptides / metabolism*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Viral Proteins / genetics
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Viral Proteins / metabolism*
Substances
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Peptides
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Recombinant Fusion Proteins
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Viral Proteins
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gene 1 protein, Coronavirus
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Adenosine Triphosphate
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Cysteine Endopeptidases
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3C Viral Proteases
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Adenosine Triphosphatases