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Phosphorylation of hepatitis B virus Cp at Ser87 facilitates core assembly

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dc.contributor.authorKang, Hee Yong-
dc.contributor.authorLee, Seungkeun-
dc.contributor.authorPark, Sung Gyoo-
dc.contributor.authorYu, Jaehoon-
dc.contributor.authorKim, Youngsoo-
dc.contributor.authorJung, Guhung-
dc.date.accessioned2010-01-19T14:16:31Z-
dc.date.available2010-01-19T14:16:31Z-
dc.date.issued2006-06-03-
dc.identifier.citationBiochem J. 2006 Sep 1;398(2):311-7.en
dc.identifier.issn1470-8728 (Electronic)-
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16740137-
dc.identifier.urihttp://hdl.handle.net/10371/38232-
dc.description.abstractProtein-protein interactions can be regulated by protein modifications such as phosphorylation. Some of the phosphorylation sites (Ser155, Ser162 and Ser170) of HBV (hepatitis B virus) Cp have been discovered and these sites are implicated in the regulation of viral genome encapsidation, capsid localization and nucleocapsid maturation. In the present report, the dimeric form of HBV Cp was phosphorylated by PKA (protein kinase A), but not by protein kinase C in vitro, and the phosphorylation of dimeric Cp facilitated HBV core assembly. Matrix-assisted laser-desorption ionization-time-of-flight analysis revealed that the HBV Cp was phosphorylated at Ser87 by PKA. This was further confirmed using a mutant HBV Cp with S87G mutation. The S87G mutation inhibited the phosphorylation and, as a result, the in vitro HBV core assembly was not facilitated by PKA. In addition, when either pCMV/FLAG-Core(WT) or pCMV/FLAG-Core(S87G) was transfected into HepG2 cells, few mutant Cps (S87G) assembled into capsids compared with the wild-type (WT) Cps, although the same level of total Cps was expressed in both cases. In conclusion, PKA facilitates HBV core assembly through phosphorylation of the HBV Cp at Ser87.en
dc.language.isoenen
dc.publisherPortland Pressen
dc.subjectAmino Acid Sequenceen
dc.subjectCapsid Proteins/chemistry/genetics/*metabolism/ultrastructureen
dc.subjectCell Line, Tumoren
dc.subjectCyclic AMP-Dependent Protein Kinases/metabolismen
dc.subjectHepatitis B virus/*chemistry/classification/*metabolism/ultrastructureen
dc.subjectHumansen
dc.subjectKineticsen
dc.subjectMicroscopy, Electron, Transmissionen
dc.subjectMolecular Sequence Dataen
dc.subjectPhosphorylationen
dc.subjectProtein Bindingen
dc.subjectSerine/genetics/*metabolismen
dc.subjectSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen
dc.subjectSurface Plasmon Resonanceen
dc.subject*Virus Assemblyen
dc.titlePhosphorylation of hepatitis B virus Cp at Ser87 facilitates core assemblyen
dc.typeArticleen
dc.contributor.AlternativeAuthor강희용-
dc.contributor.AlternativeAuthor이승근-
dc.contributor.AlternativeAuthor박성규-
dc.contributor.AlternativeAuthor유재훈-
dc.contributor.AlternativeAuthor김영수-
dc.contributor.AlternativeAuthor정구홍-
dc.identifier.doi10.1042/BJ20060347-
Appears in Collections:
College of Medicine/School of Medicine (의과대학/대학원)Molecular and Genomic Medicine (분자유전체의학전공)Journal Papers (저널논문_분자유전체의학전공)
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