Identification of a novel cell attachment domain in the HIV-1 Tat protein and its 90-kDa cell surface binding protein.

Journal Article (Journal Article)

The HIV-1 transactivator protein Tat is essential for viral gene expression and replication. Tat is taken up by cells and transactivates the HIV-LTR promoter in the cell nucleus. The present studies show that cells adhere to both synthetic and recombinant Tat, and, using synthetic peptides, we localize the binding site to a region spanning amino acid residues 49-57 (peptide Tat49-57). Tat49-57 also inhibited cell attachment to solid phase full-length Tat peptide and to recombinant Tat protein. Using Tat peptide affinity chromatography, we identified a 90-kDa cell surface protein that binds to Tat. The 90-kDa protein could be eluted from the Tat column using the Tat49-57 peptide. A 90-kDa cell surface Tat binding protein was also identified by coprecipitation with Tat after incubation with radiolabeled cell membrane preparations. Co-precipitation of the 90-kDa protein was inhibited by competition with a Tat49-65 peptide, but not with Tat55-86. Our findings suggest that cellular attachment to Tat is mediated through a 90-kDa cell surface protein that binds to a Tat domain between amino acids 49 and 57.

Full Text

Duke Authors

Cited Authors

  • Weeks, BS; Desai, K; Loewenstein, PM; Klotman, ME; Klotman, PE; Green, M; Kleinman, HK

Published Date

  • March 5, 1993

Published In

Volume / Issue

  • 268 / 7

Start / End Page

  • 5279 - 5284

PubMed ID

  • 8444901

International Standard Serial Number (ISSN)

  • 0021-9258


  • eng

Conference Location

  • United States