摘要
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.
For genome multiplication hepadnaviruses use the tran-scriptional 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 intracy-tosolic translocation is facilitated by the viral capsid that surrounds the genome and that interacts with cellular microtubules.The subsequent passage through the nu-clear pore complexes(NPC) is mediated by the nuclear transport receptors importin α and β.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 oth-er karyophilic cargos using this pathway importin α inter-acts 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 karyoplas-mic face of the NPC.Presumably only this compartment provides the factors that are required for capsid disas-sembly and genome release that is restricted to those capsids comprising a mature viral DNA genome.
基金
SupportedbytheDeutscheForschungsgemeinschaft(DFG
SFB535TPB5,DFGKA1193/5-2andGraduiertenkolleg"BiochemievonNukleoproteinkomplexen"),bytheEuropeanCommunity(‘Combinedimmuneandgenetherapyforchronichepatitis’5thcallforQualityofLifeandManagementofLivingResources,KeyAction2,Controlofinfectiousdiseases)andtheCanadianIn-stituteofHealthResearchandtheNaturalSciencesandEngineer-ingResearchCouncilofCanada