Identification of HIV-1 Reverse Transcriptase Inhibitors Using a Scintillation Proximity Assay View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2013

AUTHORS

Bertrand Van Schoubroeck , Marnix Van Loock , Tania Ivens , Pascale Dehertogh , Dirk Jochmans , Géry Dams

ABSTRACT

The human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) converts the viral single-stranded RNA into double-stranded DNA. The inhibition of reverse transcription in the viral life cycle has proven its efficacy as a clinically relevant antiviral target, but the appearance of resistance mutations remains a major cause of treatment failure and stresses the continuous need for new antiviral compounds. In this chapter, we describe an HIV-1 RT scintillation proximity assay (SPA) to identify inhibitors of the RT. The assay uses an RNA/DNA (poly(rA)/oligo(dT)) template/primer bound to SPA beads, which contain scintillant. Reverse transcriptase extends the primer by incorporating [(3)H]dTTP and dTTP, which results in light production by the scintillant in the bead. Compounds that inhibit reverse transcriptase will prevent the incorporation of tritiated dTTP resulting in a reduction of emitted light compared to the untreated controls. More... »

PAGES

19-24

References to SciGraph publications

  • 2001-11. HIV-1 Replication in SOMATIC CELL AND MOLECULAR GENETICS
  • 2005-03-25. Measurement of Radioligand Binding by Scintillation Proximity Assay in RECEPTOR BINDING TECHNIQUES
  • 1989-09. Scintillation proximity assay in NATURE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/978-1-62703-484-5_3

    DOI

    http://dx.doi.org/10.1007/978-1-62703-484-5_3

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1011903595

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/23821257


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