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Escape of herpesviruses from the nucleus
Author(s) -
Lee ChungPei,
Chen MeiRu
Publication year - 2010
Publication title -
reviews in medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.06
H-Index - 90
eISSN - 1099-1654
pISSN - 1052-9276
DOI - 10.1002/rmv.643
Subject(s) - nuclear lamina , nuclear pore , nucleoporin , inner membrane , lamin , cytoplasm , microbiology and biotechnology , nuclear transport , biology , viral envelope , nuclear membrane , cell nucleus , capsid , nucleus , nuclear protein , virology , genetics , gene , virus , transcription factor , mitochondrion
Abstract The nuclear envelope of eukaryotic cells is composed of double lipid‐bilayer membranes, the membrane‐connected nuclear pore complexes and an underlying nuclear lamina network. The nuclear pore complexes serve as gates for regulating the transport of macromolecules between cytoplasm and nucleus. The nuclear lamina not only provides an intact meshwork for maintaining the nuclear stiffness but also presents a natural barrier against most DNA viruses. Herpesviruses are large DNA viruses associated with multiple human and animal diseases. The complex herpesviral virion contains more than 30 viral proteins. After viral DNA replication, the newly synthesised genome is packaged into the pre‐assembled intranuclear capsid. The nucleocapsid must then transverse through the nuclear envelope to the cytoplasm for the subsequent maturation process. Information regarding how nucleocapsid breaches the rigid nuclear lamina barrier and accesses the inner nuclear membrane for primary envelopment has emerged recently. From the point of view of both viral components and nuclear structure, this review summarises recent advances in the complicated protein–protein interactions and the phosphorylation regulations involved in the nuclear egress of herpesviral nucleocapsids. Copyright © 2010 John Wiley & Sons, Ltd.

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