Importin-alpha promotes passage through the nuclear pore complex of human immunodeficiency virus type 1 Vpr.

Abstract:

:Viral protein R (Vpr) of human immunodeficiency virus type 1 has potent karyophilic properties, but details of the mechanism by which it enters the nucleus remain to be clarified. We reported previously that two regions, located between residues 17 and 34 (alphaH1) and between residues 46 and 74 (alphaH2), are indispensable for the nuclear localization of Vpr. Here, we reveal that a chimeric protein composed of the nuclear localization signal of Vpr, glutathione S-transferase, and green fluorescent protein was localized at the nuclear envelope and then entered the nucleus upon addition of importin-alpha. An in vitro transport assay using a series of derivatives of importin-alpha demonstrated that the carboxyl terminus was required for this nuclear import process. We also showed that Vpr interacts with importin-alpha through alphaH1 and alphaH2; only the interaction via alphaH1 is indispensable for the nuclear entry of Vpr. These observations indicate that importin-alpha functions as a mediator for the nuclear entry of Vpr.

journal_name

J Virol

journal_title

Journal of virology

authors

Kamata M,Nitahara-Kasahara Y,Miyamoto Y,Yoneda Y,Aida Y

doi

10.1128/JVI.79.6.3557-3564.2005

subject

Has Abstract

pub_date

2005-03-01 00:00:00

pages

3557-64

issue

6

eissn

0022-538X

issn

1098-5514

pii

79/6/3557

journal_volume

79

pub_type

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