Institute of Biotechnology, Graiciuno 8, 02241, Vilnius, Lithuania.
Arch Virol. 2010 Feb;155(2):247-50. doi: 10.1007/s00705-009-0561-z. Epub 2009 Nov 29.
Up to now, little is known about hepatitis B virus core protein (HBc) interactions with host-cell proteins, although such interactions might be essential for virus propagation and pathogenicity. In this work, a human liver cDNA library was screened for proteins interacting with HBc. Among several HBc-interacting partners selected, it interacted most strongly with the human protein GIPC1. A common protein interaction domain, PDZ, was identified as the region that is sufficient for the interaction with HBc. The core protein has a putative C-terminal PDZ-interacting motif, and this sequence proved to be important for the interaction with GIPC1.
到目前为止，人们对乙型肝炎病毒核心蛋白 (HBc) 与宿主细胞蛋白的相互作用知之甚少，尽管这种相互作用可能对病毒的增殖和致病性至关重要。在这项工作中，筛选了一个人类肝脏 cDNA 文库，以寻找与 HBc 相互作用的蛋白质。在所选择的几个与 HBc 相互作用的伙伴中，它与人类蛋白 GIPC1 相互作用最强。鉴定出一个常见的蛋白相互作用结构域 PDZ 作为与 HBc 相互作用的区域。核心蛋白具有假定的 C 末端 PDZ 相互作用基序，该序列被证明对与 GIPC1 的相互作用很重要。
