Journal
VIROLOGY
Volume 330, Issue 2, Pages 481-486Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2004.10.011
Keywords
human immunodeficiency virus type 1; Tat; heparan sulfate proteoglycans; long terminal repeat
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Funding
- NHLBI NIH HHS [HL56984, HL58884] Funding Source: Medline
- NIAID NIH HHS [AI46149, AI41899] Funding Source: Medline
- NINDS NIH HHS [NS27405, NS44513] Funding Source: Medline
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Cell surface heparan sulfate proteoglycans (HSPGs) mediate internalization of HIV-1 Tat. Herein, we report that human WiDr cells, which express perlecan but no other HSPGs, can internalize I-125-labeled Tat with minimal lysosomal degradation. Pre-treatment of cells with heparitinase almost completely abolished I-125-Tat surface binding, while the use of an HIV-1 long terminal repeat (LTR) promoter-reporter construct demonstrated that transactivation was potently blocked by pretreatment of cells with heparitinase, indicating an essential role for perlecan in the biologic effects of Tat. We conclude that the perlecan mediates Tat uptake and is required for HIV-1 LTR-directed transactivation in this human cell type. (C) 2004 Elsevier Inc. All rights reserved.
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