title: A physical link between the pseudorabies virus capsid and the nuclear egress complex.
abstract: Following their assembly, herpesvirus capsids exit the nucleus by budding at the inner nuclear membrane. Two highly conserved viral proteins are required for this process, pUL31 and pUL34. In this report, we demonstrate that the pUL31 component of the pseudorabies virus nuclear egress complex is a conditional capsid-binding protein that is unmasked in the absence of pUL34. The interaction between pUL31 and capsids was confirmed through fluorescence microscopy and Western blot analysis of purified intranuclear capsids. Three viral proteins were tested for their abilities to mediate the pUL31-capsid interaction: the minor capsid protein pUL25, the portal protein pUL6, and the terminase subunit pUL33. Despite the requirement for each protein in nuclear egress, none of these viral proteins were required for the pUL31-capsid interaction. These findings provide the first formal evidence that a herpesvirus nuclear egress complex interacts with capsids and have implications for how DNA-containing capsids are selectively targeted for nuclear egress.
authors: Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, 303 E. Chicago Ave., Morton 3-603, Chicago, IL 60611, USA.
authors: Mindy
authors: M
authors: Leelawong
authors: Dongsheng
authors: D
authors: Guo
authors: Gregory A
authors: GA
authors: Smith
mesh_terms: D021581:Active Transport, Cell Nucleus; D015153:Blotting, Western; D002213:Capsid / Q000378:metabolism*; D011558:Herpesvirus 1, Suid / Q000502:physiology*; D008856:Microscopy, Fluorescence; D011485:Protein Binding; D025941:Protein Interaction Mapping; D014764:Viral Proteins / Q000378:metabolism*; D057074:Virus Release
chemical_list: D014764:Viral Proteins