PMID: 7518533Aug 1, 1994Paper

Phenotypic mixing between different hepadnavirus nucleocapsid proteins reveals C protein dimerization to be cis preferential

Journal of Virology
C ChangD N Standring

Abstract

Hepadnaviruses encode a single core (C) protein which assembles into a nucleocapsid containing the polymerase (P) protein and pregenomic RNA during viral replication in hepatocytes. We examined the ability of heterologous hepadnavirus C proteins to cross-oligomerize. Using a two-hybrid assay in HepG2 cells, we observed cross-oligomerization among the core proteins from hepatitis B virus (HBV), woodchuck hepatitis virus, and ground squirrel hepatitis virus. When expressed in Xenopus oocytes, in which hepadnavirus C proteins form capsids, the C polypeptides from woodchuck hepatitis virus and ground squirrel hepatitis virus, but not duck hepatitis B virus, can efficiently coassemble with an epitope-tagged HBV core polypeptide to form mixed capsids. However, when two different core mRNAs are coexpressed in oocytes the core monomers show a strong preference for forming homodimers rather than heterodimers. This holds true even for coexpression of two HBV C proteins differing only by an epitope tag, suggesting that core monomers are not free to diffuse and associate with other monomers. Thus, mixed capsids result from aggregation of different species of homodimers.

References

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Citations

Jul 15, 2005·Journal of Virology·Margherita MelegariRobert J Schneider
Sep 11, 2009·The Journal of General Virology·Kilian WeigandHeinz Schaller
Mar 8, 2000·Microbiology and Molecular Biology Reviews : MMBR·C Seeger, W S Mason
Apr 19, 2006·The Journal of Biological Chemistry·Arik Cooper, Yosef Shaul
Apr 1, 1995·Journal of Virology·F von WeizsäckerH E Blum

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