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  • The EMBO Journal (2003) 22, 6245 - 6255
  • doi:10.1093/emboj/cdg614

Switch from capsid protein import to adenovirus assembly by cleavage of nuclear transport signals

Harald Wodrich1, Tinglu Guan1, Gino Cingolani1, Dan Von Seggern2, Glen Nemerow2 and Larry Gerace1

  1. Departments of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA
  2. Departments of Immunology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA

Correspondence to:

Larry Gerace, E-mail: lgerace@scripps.edu

Received 3 June 2003; Accepted 16 October 2003; Revised 24 September 2003

Replication and assembly of adenovirus occurs in the nucleus of infected cells, requiring the nuclear import of all viral structural proteins. In this report we show that nuclear import of the major capsid protein, hexon, is mediated by protein VI, a structural protein located underneath the 12 vertices of the adenoviral capsid. Our data indicate that protein VI shuttles between the nucleus and the cytoplasm and that it links hexon to the nuclear import machinery via an importin alpha/beta-dependent mechanism. Key nuclear import and export signals of protein VI are located in a short C-terminal segment, which is proteolytically removed during virus maturation. The removal of these C-terminal transport signals appears to trigger a functional transition in protein VI, from a role in supporting hexon nuclear import to a structural role in virus assembly.

  • Keywords:

    • adenovirus,
    • assembly,
    • hexon,
    • nucleo-cytoplasmic transport,
    • protein VI