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Journal of Virology, February 2001, p. 2024-2028, Vol. 75, No. 4
Institute for Cancer Research, Fox Chase
Cancer Center, Philadelphia, Pennsylvania 19111
Received 7 September 2000/Accepted 15 November 2000
Hepadnaviruses are enveloped viruses, each with a DNA genome
packaged in an icosahedral nucleocapsid, which is the site of viral DNA
synthesis. In the presence of envelope proteins, DNA-containing nucleocapsids are assembled into virions and secreted, but in the
absence of these proteins, nucleocapsids deliver viral DNA into the
cell nucleus. Presumably, this step is identical to the delivery of
viral DNA during the initiation of an infection. Unfortunately, the
mechanisms triggering the disintegration of subviral core particles and
delivery of viral DNA into the nucleus are not yet understood. We now
report the identification of a sequence motif resembling a serine- or
threonine-proline kinase recognition site in the core protein at a
location that is required for the assembly of core polypeptides into
capsids. Using duck hepatitis B virus, we demonstrated that mutations
at this sequence motif can have profound consequences for RNA
packaging, DNA replication, and core protein stability. Furthermore, we
found a mutant with a conditional phenotype that depended on the cell
type used for virus replication. Our results support the hypothesis
predicting that this motif plays a role in assembly and disassembly of
viral capsids.
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.4.2024-2028.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Does a cdc2 Kinase-Like Recognition Motif on the Core Protein
of Hepadnaviruses Regulate Assembly and Disintegration
of Capsids?
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Corresponding author. Mailing address: Institute for
Cancer Research, Fox Chase Cancer Center, 7701 Burholme Ave.,
Philadelphia, PA 19111. Phone: (215) 728-4312. Fax: (215)
728-4329. E-mail: c_seeger{at}fccc.edu.
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