Phosphorylation of Vpr regulates HIV type 1 nuclear import and macrophage infection.

@article{citeulike:3134253, abstract = {Viral protein R (Vpr) of human immunodeficiency virus type 1 (HIV-1) is a small accessory protein that regulates nuclear import of the viral preintegration complex and facilitates infection of nondividing cells, such as macrophages. Studies demonstrated that a fraction of Vpr molecules is phosphorylated in the virions and in HIV-1-infected cells, but the role of phosphorylation in nuclear import activity of Vpr has not been established. We found that Vpr is phosphorylated predominantly on the serine residue in position 79, and mutations affecting Vpr phosphorylation significantly attenuated viral replication in macrophages, but not in activated T lymphocytes or cell lines. The replication defect was mapped by polymerase chain reaction analysis to the step of nuclear import. These results suggest that phosphorylation of Vpr regulates its activity in the nuclear import of the HIV-1 preintegration complex.}, address = {Picower Institute for Medical Research, Manhasset, New York 11030, USA.}, author = {Agostini, I. and Popov, S. and Hao, T. and Li, J. H. and Dubrovsky, L. and Chaika, O. and Chaika, N. and Lewis, R. and Bukrinsky, M. }, citeulike-article-id = {3134253}, doi = {http://dx.doi.org/10.1089/088922202753472856}, issn = {0889-2229}, journal = {AIDS research and human retroviruses}, keywords = {hiv, vpr}, month = {March}, number = {4}, pages = {283--288}, posted-at = {2008-08-18 21:47:47}, priority = {2}, title = {Phosphorylation of Vpr regulates HIV type 1 nuclear import and macrophage infection.}, url = {http://dx.doi.org/10.1089/088922202753472856}, volume = {18}, year = {2002} }

TY - JOUR ID - citeulike:3134253 L3 - citeulike-article-id:3134253 N2 - Viral protein R (Vpr) of human immunodeficiency virus type 1 (HIV-1) is a small accessory protein that regulates nuclear import of the viral preintegration complex and facilitates infection of nondividing cells, such as macrophages. Studies demonstrated that a fraction of Vpr molecules is phosphorylated in the virions and in HIV-1-infected cells, but the role of phosphorylation in nuclear import activity of Vpr has not been established. We found that Vpr is phosphorylated predominantly on the serine residue in position 79, and mutations affecting Vpr phosphorylation significantly attenuated viral replication in macrophages, but not in activated T lymphocytes or cell lines. The replication defect was mapped by polymerase chain reaction analysis to the step of nuclear import. These results suggest that phosphorylation of Vpr regulates its activity in the nuclear import of the HIV-1 preintegration complex. IS - 4 JF - AIDS research and human retroviruses SN - 0889-2229 AD - Picower Institute for Medical Research, Manhasset, New York 11030, USA. EP - 288 TI - Phosphorylation of Vpr regulates HIV type 1 nuclear import and macrophage infection. VL - 18 SP - 283 KW - hiv KW - vpr AU - Agostini, I AU - Popov, S AU - Hao, T AU - Li, JH AU - Dubrovsky, L AU - Chaika, O AU - Chaika, N AU - Lewis, R AU - Bukrinsky, M PY - 2002/03/01/ UR - http://dx.doi.org/10.1089/088922202753472856 ER -