Journal
EMBO JOURNAL
Volume 22, Issue 23, Pages 6245-6255Publisher
WILEY
DOI: 10.1093/emboj/cdg614
Keywords
adenovirus; assembly; hexon; nucleo-cytoplasmic transport; protein VI
Categories
Funding
- NATIONAL EYE INSTITUTE [R01EY011431] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL054352] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM041955] Funding Source: NIH RePORTER
- NEI NIH HHS [EY11431, R01 EY011431] Funding Source: Medline
- NHLBI NIH HHS [HL54352, R01 HL054352] Funding Source: Medline
- NIGMS NIH HHS [GM41955, R01 GM041955] Funding Source: Medline
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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.
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