Intracellular transport of hepatitis B virus

• Published in: World journal of gastroenterology : WJG Vol. 13; no. 1; pp. 39 - 47
• Main Authors: Kann, Michael, Schmitz, Andre, Rabe, Birgit
• Format: Journal Article
• Language: English
• Published: United States CNRS-REGER (UMR 5097), Université Bordeaux 2, 146 rue Léo Saignat, F-33076 Bordeaux Cedex, France%Institute of Medical Virology, Frankfurter Str. 107, D-35392 Giessen, Germany 07.01.2007; Baishideng Publishing Group Co. Limited; Baishideng Publishing Group Co., Limited
• Subjects: Active Transport, Cell Nucleus; Active Transport, Cell Nucleus - physiology; alpha Karyopherins; alpha Karyopherins - physiology; beta Karyopherins; beta Karyopherins - physiology; Biological Transport; Biological Transport - physiology; Capsid; Capsid - physiology; Cell Nucleus; Cell Nucleus - metabolism; DNA, Viral; DNA, Viral - metabolism; Hepatitis B virus; Hepatitis B virus - metabolism; Hepatitis B virus - pathogenicity; Hepatocytes; Hepatocytes - metabolism; Hepatocytes - pathology; Hepatocytes - virology; Humans; Life Sciences; Microbiology and Parasitology; Microtubules; Microtubules - physiology; Nuclear Localization Signals; Nuclear Localization Signals - physiology; Nuclear Pore; Topic Highlight; 乙型病毒肝炎; 细胞内运输; Intracellular transport; Nuclear pore; Hepatitis B virus; Capsid; Microtubules
• ISSN: 1007-9327; 2219-2840
• DOI: 10.3748/wjg.v13.i1.39

For genome mulUplication hepadnaviruses use the transcriptional machinery of the cell that is found within the nucleus. Thus the viral genome has to be transported through the cytoplasm and nuclear pore. The intracytosolic translocation is facilitated by the viral capsid that surrounds the genome and that interacts with cellular microtubules. The subsequent passage through the nuclear pore complexes （NPC） is mediated by the nuclear transport receptors importin α andβ. Importin α binds to the C-terminus of the capsid protein that comprises a nuclear localization signal （NLS）. The exposure of the NLS is regulated and depends upon genome maturation and/or phosphorylation of the capsid protein. As for other karyophilic cargos using this pathway importin α interacts with importin β that facilitates docking of the import complex to the NPC and the passage through the pore. Being a unique strategy, the import of the viral capsid is incomplete in that it becomes arrested inside the nuclear basket, which is a cage-like structure on the karyoplasmic face of the NPC. Presumably only this compartment provides the factors that are required for capsid disassembly and genome release that is restricted to those capsids comprising a mature viral DNA genome.