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A Novel Enzyme-Linked Immunosorbent Assay for Screening HIV-1 Fusion Inhibitors Targeting HIV-1 Gp41 Core Structure.
- Source :
- Journal of Biomolecular Screening; 04/01/2011, Vol. 16 Issue 2, p221-229, 9p
- Publication Year :
- 2011
-
Abstract
- The gp41 subunit of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein mediates the fusion of viral and host cell membranes. As the HIV-1 enters the host cells, the 2 helical regions, HR1 and HR2, in the ectodomain of gp41 can form a 6-helix bundle, which brings the viral and target cell membranes to close proximity and serves as an attractive target for developing HIV-1 fusion inhibitors. Now, there are several cell- and molecule-based assays to identify potential HIV-1 fusion inhibitors targeting gp41. However, these assays cannot be used universally because they are time-consuming, inconvenient, and expensive. In the present study, the authors expressed and purified GST-HR121 and C43-30a proteins that were derived from the HIV-1 gp41 ectodomain region. GST-HR121 has a function similar to the HR1 peptide of gp41, whereas C43-30a is an HR2-derived peptide that added 50 amino acid residues (aa) in the N-terminal of C43. Further research found they could interact with each other, and a potential HIV-1 fusion inhibitor could inhibit this interaction. On the basis of this fact, a novel, rapid, and economic enzyme-linked immunosorbent assay was established, which can be developed for high-throughput screening of HIV-1 fusion inhibitors. (Journal of Biomolecular Screening 2011;16:221-229) [ABSTRACT FROM PUBLISHER]
Details
- Language :
- English
- ISSN :
- 10870571
- Volume :
- 16
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- Journal of Biomolecular Screening
- Publication Type :
- Academic Journal
- Accession number :
- 58645650
- Full Text :
- https://doi.org/10.1177/1087057110393333