@inbook{e9e96bac255547e4bdec0509cdab81bc,
title = "HIV-1 capsid stabilization assay",
abstract = "The stability of the HIV-1 core in the cytoplasm is crucial for productive HIV-1 infection. Mutations that stabilize or destabilize the core showed defects in HIV-1 reverse transcription and infection. We developed a novel and simple assay to measure stability of in vitro-assembled HIV-1 CA-NC complexes. This assay allowed us to demonstrate that cytosolic extracts strongly stabilize the HIV-1 core (Fricke et al., J Virol 87:10587-10597, 2013). By using our novel assay, one can measure the ability of different drugs to modulate the stability of in vitro-assembled HIV-1 CA-NC complexes, such as PF74, CAP-1, IXN-053, cyclosporine A, Bi2, and the peptide CAI. We also found that purified CPSF6 (1-321) protein stabilizes in vitro-assembled HIV-1 CA-NC complexes (Fricke et al., J Virol 87:10587-10597, 2013). Here we describe in detail the use of this capsid stability assay. We believe that our assay can be a powerful tool to assess HIV-1 capsid stability in vitro.",
keywords = "Capsid, Core, HIV-1, Stability, Uncoating",
author = "Thomas Fricke and Felipe Diaz-Griffero",
note = "Funding Information: Projects AI087390, AI10282401, R56AI108432, and AI104476 to F.D.-G supported this work. We are grateful to the NIH HIV-1/ AIDS repository for providing reagents such as antibodies and small-molecule inhibitors that were crucial for this work. Publisher Copyright: {\textcopyright} Springer Science+Business Media New York 2016.",
year = "2016",
doi = "10.1007/978-1-4939-3046-3_3",
language = "English (US)",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "39--47",
booktitle = "Methods in Molecular Biology",
}