Abstract
Two alpha-type CK2-activated PKAs (CK2-aPKAIalpha and CK2-aPKAIIalpha) were biochemically characterized in vitro using GST-HBV core fusion protein (GST-Hcore) and GST-Hcore157B as phosphate acceptors. It was found that (i), in the absence of cAMP, these two CK2-aPKAs phosphorylated both Ser-170 and Ser-178 on GST-Hcore and Hcore157B; (ii) this phosphorylation was approx. 4-fold higher than their phosphorylation by cAMP-activated PKAs; and (iii) suramin effectively inhibited the phosphorylation of Hcore157B by CK2-aPKAIIalpha through its direct binding to Hcore157B in vitro. These results suggest that high phosphorylation of HBV-CP by two CK2-aPKAs, in the absence of cAMP, may be involved in the pregenomic RNA (pgRNA) encapsidation and DNA-replication in HBV-infected cells.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antineoplastic Agents / pharmacology
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Casein Kinase II / metabolism*
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Cattle
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Cyclic AMP / metabolism
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Cyclic AMP-Dependent Protein Kinases
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Enzyme Activation
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Genome, Viral / physiology
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Hepatitis B / enzymology
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Hepatitis B virus / metabolism*
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Humans
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Phosphorylation / drug effects
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Protein Processing, Post-Translational / drug effects
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Protein Processing, Post-Translational / physiology*
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Protein Serine-Threonine Kinases / metabolism*
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RNA, Viral / metabolism
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Serine / metabolism
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Suramin / pharmacology
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Viral Core Proteins / metabolism*
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Virus Replication / drug effects
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Virus Replication / physiology
Substances
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Antineoplastic Agents
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RNA, Viral
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Viral Core Proteins
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Serine
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Suramin
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Cyclic AMP
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Casein Kinase II
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Protein Serine-Threonine Kinases
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Cyclic AMP-Dependent Protein Kinases