Open AccessInhibition of protein kinase C phosphorylation of hepatitis B virus capsids inhibits virion formation and causes intracellular capsid accumulation
Author(s) -
Wittkop Linda,
Schwarz Alexandra,
Cassany Aurelia,
GrünBernhard Stefanie,
Delaleau Mildred,
Rabe Birgit,
Cazenave Christian,
Gerlich Wolfram,
Glebe Dieter,
Kann Michael
Publication year - 2010
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/j.1462-5822.2010.01444.x
Subject(s) - capsid , biology , kinase , phosphorylation , protein kinase a , virology , duck hepatitis b virus , viral replication , microbiology and biotechnology , viral life cycle , hepatitis b virus , protein phosphorylation , virus , hepadnaviridae
Summary Capsids of hepatitis B virus and other hepadnaviruses contain a cellular protein kinase, which phosphorylates the capsid protein. Some phosphorylation sites are shown to be essential for distinct steps of viral replication as pregenome packaging or plus strand DNA synthesis. Although different protein kinases have been reported to phosphorylate the capsid protein, varying experimental approaches do not allow direct comparison. Furthermore, the activity of a specific protein kinase has not yet been correlated to steps in the hepadnaviral life cycle. In this study we show that capsids from various sources encapsidate active protein kinase Cα, irrespective of hepatitis B virus genotype and host cell. Treatment of a virion expressing cell line with a pseudosubstrate inhibitor showed that inhibition of protein kinase C phosphorylation did not affect genome maturation but resulted in capsid accumulation and inhibited virion release to the medium. Our results imply that different protein kinases have distinct functions within the hepadnaviral life cycle.