Structure of SL4 RNA from the HIV-1 Packaging Signal†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (48) ◽  
pp. 14518-14529 ◽  
Author(s):  
Deborah J. Kerwood ◽  
Michael J. Cavaluzzi ◽  
Philip N. Borer
Keyword(s):  
Packaging Signal ◽  
Hiv 1

Structure and Stability of Wild-type and Mutant RNA Internal Loops from the SL-1 Domain of the HIV-1 Packaging Signal

2002 ◽  
Vol 322 (3) ◽  
pp. 543-557 ◽  
Author(s):  
Jane Greatorex ◽  
José Gallego ◽  
Gabriele Varani ◽  
Andrew Lever
Keyword(s):  
Wild Type ◽  
Packaging Signal ◽  
Structure And Stability ◽  
Internal Loops ◽  
Hiv 1

Identification of Peptide Ligands for Target RNA Structures Derived from the HIV-1 Packaging Signal ψ by Screening Phage-Displayed Peptide Libraries

ChemBioChem ◽  
2003 ◽  
Vol 4 (10) ◽  
pp. 1093-1097 ◽  
Author(s):  
Anette Pustowka ◽  
Julia Dietz ◽  
Jan Ferner ◽  
Michael Baumann ◽  
Margot Landersz ◽  
...  
Keyword(s):  
Peptide Ligands ◽  
Peptide Libraries ◽  
Rna Structures ◽  
Packaging Signal ◽  
Target Rna ◽  
Hiv 1

ANTIVIRAL ACTIVITY OF STERIC-BLOCK OLIGONUCLEOTIDES TARGETING THE HIV-1 TRANS-ACTIVATION RESPONSE AND PACKAGING SIGNAL STEM-LOOP RNAS

2005 ◽  
Vol 24 (5-7) ◽  
pp. 393-396 ◽  
Author(s):  
Douglas Brown ◽  
Andrey A. Arzumanov ◽  
John J. Turner ◽  
Dmitry A. Stetsenko ◽  
Andrew M. L. Lever ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Packaging Signal ◽  
Stem Loop ◽  
Activation Response ◽  
Hiv 1

The major HIV-1 packaging signal is an extended bulged stem loop whose structure is altered on interaction with the gag polyprotein

2000 ◽  
Vol 301 (5) ◽  
pp. 1315
Author(s):  
Amanda Zeffman ◽  
Stuart Hassard ◽  
Gabriele Varani ◽  
Andrew Lever
Keyword(s):  
Packaging Signal ◽  
Stem Loop ◽  
Gag Polyprotein ◽  
Hiv 1

scholarly journals Nucleolin and the Packaging Signal, ψ, Promote the Budding of Human Immunodeficiency Virus Type-1 (HIV-1)

2004 ◽  
Vol 48 (2) ◽  
pp. 111-118 ◽  
Author(s):  
Tomonori Ueno ◽  
Kenzo Tokunaga ◽  
Hirofumi Sawa ◽  
Masae Maeda ◽  
Joe Chiba ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Packaging Signal ◽  
Immunodeficiency Virus ◽  
Hiv 1

scholarly journals Author response: Dissection of specific binding of HIV-1 Gag to the 'packaging signal' in viral RNA

2017 ◽  
Author(s):  
Mauricio Comas-Garcia ◽  
Siddhartha AK Datta ◽  
Laura Baker ◽  
Rajat Varma ◽  
Prabhakar R Gudla ◽  
...  
Keyword(s):  
Specific Binding ◽  
Viral Rna ◽  
Author Response ◽  
Packaging Signal ◽  
Hiv 1

scholarly journals Identification of the initial nucleocapsid recognition element in the HIV-1 RNA packaging signal

2020 ◽  
Vol 117 (30) ◽  
pp. 17737-17746 ◽  
Author(s):  
Pengfei Ding ◽  
Siarhei Kharytonchyk ◽  
Alexis Waller ◽  
Ugonna Mbaekwe ◽  
Sapna Basappa ◽  
...  
Keyword(s):  
Binding Sites ◽  
Virus Assembly ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Nmr Studies ◽  
Recognition Element ◽  
High Affinity ◽  
Molecule Inhibitor ◽  
Encapsidation Signal ◽  
Hiv 1

Selective packaging of the HIV-1 genome during virus assembly is mediated by interactions between the dimeric 5ʹ-leader of the unspliced viral RNA and the nucleocapsid (NC) domains of a small number of assembling viral Gag polyproteins. Here, we show that the dimeric 5′-leader contains more than two dozen NC binding sites with affinities ranging from 40 nM to 1.4 μM, and that all high-affinity sites (Kd≲ 400 nM) reside within a ∼150-nt region of the leader sufficient to promote RNA packaging (core encapsidation signal, ΨCES). The four initial binding sites with highest affinity reside near two symmetrically equivalent three-way junction structures. Unlike the other high-affinity sites, which bind NC with exothermic energetics, binding to these sites occurs endothermically due to concomitant unwinding of a weakly base-paired [UUUU]:[GGAG] helical element. Mutations that stabilize base pairing within this element eliminate NC binding to this site and severely impair RNA packaging into virus-like particles. NMR studies reveal that a recently discovered small-molecule inhibitor of HIV-1 RNA packaging that appears to function by stabilizing the structure of the leader binds directly to the [UUUU]:[GGAG] helix. Our findings suggest a sequential NC binding mechanism for Gag-genome assembly and identify a potential RNA Achilles’ heel to which HIV therapeutics may be targeted.

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