NDLI: Nucleocapsid Annealing-Mediated Electrophoresis (NAME) assay allows the rapid identification of HIV-1 nucleocapsid inhibitors.

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Nucleocapsid Annealing-Mediated Electrophoresis (NAME) assay allows the rapid identification of HIV-1 nucleocapsid inhibitors.

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Nucleocapsid Annealing-Mediated Electrophoresis (NAME) assay allows the rapid identification of HIV-1 nucleocapsid inhibitors.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sosic, Alice Cappellini, Marta Scalabrin, Matteo Gatto, Barbara
Description	Author Affiliation: Sosic A ( Department of Pharmaceutical and Pharmacological Sciences, University of Padova.); Cappellini M ( Department of Pharmaceutical and Pharmacological Sciences, University of Padova.); Scalabrin M ( The RNA Institute, SUNY Albany.); Gatto B ( Department of Pharmaceutical and Pharmacological Sciences, University of Padova)
Abstract	RNA or DNA folded in stable tridimensional folding are interesting targets in the development of antitumor or antiviral drugs. In the case of HIV-1, viral proteins involved in the regulation of the virus activity recognize several nucleic acids. The nucleocapsid protein NCp7 (NC) is a key protein regulating several processes during virus replication. NC is in fact a chaperone destabilizing the secondary structures of RNA and DNA and facilitating their annealing. The inactivation of NC is a new approach and an interesting target for anti-HIV therapy. The Nucleocapsid Annealing-Mediated Electrophoresis (NAME) assay was developed to identify molecules able to inhibit the melting and annealing of RNA and DNA folded in thermodynamically stable tridimensional conformations, such as hairpin structures of TAR and cTAR elements of HIV, by the nucleocapsid protein of HIV-1. The new assay employs either the recombinant or the synthetic protein, and oligonucleotides without the need of their previous labeling. The analysis of the results is achieved by standard polyacrylamide gel electrophoresis (PAGE) followed by conventional nucleic acid staining. The protocol reported in this work describes how to perform the NAME assay with the full-length protein or its truncated version lacking the basic N-terminal domain, both competent as nucleic acids chaperones, and how to assess the inhibition of NC chaperone activity by a threading intercalator. Moreover, NAME can be performed in two different modes, useful to obtain indications on the putative mechanism of action of the identified NC inhibitors.
File Format	HTM / HTML
e-ISSN	1940087X
DOI	10.3791/52474
Journal	Journal of Visualized Experiments
Issue Number	95
Language	English
Publisher	MyJove Corp.
Publisher Date	2015-01-19
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Physical Sciences Discipline Life Sciences Discipline Medicine Electrophoresis Hiv-1 Chemistry Nucleocapsid Proteins Antagonists & Inhibitors Nucleocapsid Dna, Viral Genetics Metabolism Molecular Chaperones Nucleic Acid Conformation Gag Gene Products, Human Immunodeficiency Virus Research Support, Non-u.s. Gov't Video-audio Media
Content Type	Text
Resource Type	Article

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