Comparative Structural Effects of HIV-1 Gag and Nucleocapsid Proteins in Binding to and Unwinding of the Viral RNA Packaging Signal

Biochemistry ◽  
2012 ◽  
Vol 51 (15) ◽  
pp. 3162-3169 ◽  
Author(s):  
Neil M. Bell ◽  
Julia C. Kenyon ◽  
Shankar Balasubramanian ◽  
Andrew M. L. Lever
Keyword(s):  
Viral Rna ◽  
Structural Effects ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Nucleocapsid Proteins ◽  
Rna Packaging Signal ◽  
Hiv 1

Stem-loop SL4 of the HIV-1 Ψ RNA packaging signal exhibits weak affinity for the nucleocapsid protein. structural studies and implications for genome recognition

2001 ◽  
Vol 314 (5) ◽  
pp. 961-970 ◽  
Author(s):  
Gaya K. Amarasinghe ◽  
Jing Zhou ◽  
Matthew Miskimon ◽  
Kalola J. Chancellor ◽  
Jasmine A. McDonald ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Structural Studies ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Stem Loop ◽  
Genome Recognition ◽  
Rna Packaging Signal ◽  
Hiv 1

scholarly journals Structure of the HIV-1 RNA packaging signal

Science ◽  
2015 ◽  
Vol 348 (6237) ◽  
pp. 917-921 ◽  
Author(s):  
S. C. Keane ◽  
X. Heng ◽  
K. Lu ◽  
S. Kharytonchyk ◽  
V. Ramakrishnan ◽  
...  
Keyword(s):  
Rna Packaging ◽  
Packaging Signal ◽  
Rna Packaging Signal ◽  
Hiv 1

Inhibition of HIV-1 by a Peptide Ligand of the Genomic RNA Packaging Signal Ψ

ChemMedChem ◽  
2008 ◽  
Vol 3 (5) ◽  
pp. 749-755 ◽  
Author(s):  
Julia Dietz ◽  
Joachim Koch ◽  
Ajit Kaur ◽  
Chinnappan Raja ◽  
Stefan Stein ◽  
...  
Keyword(s):  
Peptide Ligand ◽  
Genomic Rna ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Rna Packaging Signal ◽  
Hiv 1

NMR structure of stem-loop SL2 of the HIV-1 Ψ RNA packaging signal reveals a novel A-U-A base-triple platform 1 1Edited by I. Tinoco

2000 ◽  
Vol 299 (1) ◽  
pp. 145-156 ◽  
Author(s):  
Gaya K Amarasinghe ◽  
Roberto N De Guzman ◽  
Ryan B Turner ◽  
Michael F Summers
Keyword(s):  
Nmr Structure ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Stem Loop ◽  
Rna Packaging Signal ◽  
Hiv 1

NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the Ψ-RNA packaging signal. implications for genome recognition 1 1Edited by P. Wright

2000 ◽  
Vol 301 (2) ◽  
pp. 491-511 ◽  
Author(s):  
Gaya K Amarasinghe ◽  
Roberto N De Guzman ◽  
Ryan B Turner ◽  
Kalola J Chancellor ◽  
Zeng Rong Wu ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Nmr Structure ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Stem Loop ◽  
Genome Recognition ◽  
Rna Packaging Signal ◽  
Hiv 1

scholarly journals Influence of gag and RRE Sequences on HIV-1 RNA Packaging Signal Structure and Function

2018 ◽  
Vol 430 (14) ◽  
pp. 2066-2079 ◽  
Author(s):  
Siarhei Kharytonchyk ◽  
Joshua D. Brown ◽  
Krista Stilger ◽  
Saif Yasin ◽  
Aishwarya S. Iyer ◽  
...  
Keyword(s):  
Structure And Function ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Signal Structure ◽  
And Function ◽  
Rna Packaging Signal ◽  
Hiv 1

scholarly journals Nonreciprocal Packaging of Human Immunodeficiency Virus Type 1 and Type 2 RNA: a Possible Role for the p2 Domain of Gag in RNA Encapsidation

1998 ◽  
Vol 72 (7) ◽  
pp. 5877-5885 ◽  
Author(s):  
Jane F. Kaye ◽  
Andrew M. L. Lever
Keyword(s):  
Human Immunodeficiency Virus ◽  
Helper Virus ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Nucleocapsid Proteins ◽  
Gag Protein ◽  
Immunodeficiency Virus ◽  
Hiv 1 ◽  
Chimeric Viruses

ABSTRACT The ability of human immunodeficiency virus types 1 (HIV-1) and 2 (HIV-2) to cross-package each other’s RNA was investigated by cotransfecting helper virus constructs with vectors derived from both viruses from which the gag and pol sequences had been removed. HIV-1 was able to package both HIV-1 and HIV-2 vector RNA. The unspliced HIV-1 vector RNA was packaged preferentially over spliced RNA; however, unspliced and spliced HIV-2 vector RNA were packaged in proportion to their cytoplasmic concentrations. The HIV-2 helper virus was unable to package the HIV-1 vector RNA, indicating a nonreciprocal RNA packaging relationship between these two lentiviruses. Chimeric proviruses based on HIV-2 were constructed to identify the regions of the HIV-1 Gag protein conferring RNA-packaging specificity for the HIV-1 packaging signal. Two chimeric viruses were constructed in which domains within the HIV-2 gag gene were replaced by the corresponding domains in HIV-1, and the ability of the chimeric proviruses to encapsidate an HIV-1-based vector was studied. Wild-type HIV-2 was unable to package the HIV-1-based vector; however, replacement of the HIV-2 nucleocapsid by that of HIV-1 generated a virus with normal protein processing which could package the HIV-1-based vector. The chimeric viruses retained the ability to package HIV-2 genomic RNA, providing further evidence for a lack of reciprocity in RNA-packaging ability between the HIV-1 and HIV-2 nucleocapsid proteins. Inclusion of the p2 domain of HIV-1 Gag in the chimera significantly enhanced packaging.

scholarly journals Cooperation of an RNA Packaging Signal and a Viral Envelope Protein in Coronavirus RNA Packaging

2001 ◽  
Vol 75 (19) ◽  
pp. 9059-9067 ◽  
Author(s):  
Krishna Narayanan ◽  
Shinji Makino
Keyword(s):  
Envelope Protein ◽  
Viral Envelope ◽  
Viral Rna ◽  
M Protein ◽  
Viral Envelope Protein ◽  
Rna Packaging ◽  
Packaging Signal ◽  
N Protein ◽  
Ribonucleoprotein Complexes ◽  
Rna Packaging Signal

ABSTRACT Murine coronavirus mouse hepatitis virus (MHV) produces a genome-length mRNA, mRNA 1, and six or seven species of subgenomic mRNAs in infected cells. Among these mRNAs, only mRNA 1 is efficiently packaged into MHV particles. MHV N protein binds to all MHV mRNAs, whereas envelope M protein interacts only with mRNA 1. This M protein-mRNA 1 interaction most probably determines the selective packaging of mRNA 1 into MHV particles. A short cis-acting MHV RNA packaging signal is necessary and sufficient for packaging RNA into MHV particles. The present study tested the possibility that the selective M protein-mRNA 1 interaction is due to the packaging signal in mRNA 1. Regardless of the presence or absence of the packaging signal, N protein bound to MHV defective interfering RNAs and intracellularly expressed non-MHV RNA transcripts to form ribonucleoprotein complexes; M protein, however, interacted selectively with RNAs containing the packaging signal. Moreover, only the RNA that interacted selectively with M protein was efficiently packaged into MHV particles. Thus, it was the packaging signal that mediated the selective interaction between M protein and viral RNA to drive the specific packaging of RNA into virus particles. This is the first example for any RNA virus in which a viral envelope protein and a known viral RNA packaging signal have been shown to determine the specificity and selectivity of RNA packaging into virions.

scholarly journals Effects of Gag Mutation and Processing on Retroviral Dimeric RNA Maturation

2006 ◽  
Vol 80 (3) ◽  
pp. 1242-1249 ◽  
Author(s):  
William Fu ◽  
Que Dang ◽  
Kunio Nagashima ◽  
Eric O. Freed ◽  
Vinay K. Pathak ◽  
...  
Keyword(s):  
Viral Protein ◽  
Leukemia Virus ◽  
Viral Rna ◽  
Host Cells ◽  
Protein Cleavage ◽  
Rna Packaging ◽  
Virus Rna ◽  
Rna Dimer ◽  
Rna Maturation ◽  
Hiv 1

ABSTRACT After their release from host cells, most retroviral particles undergo a maturation process, which includes viral protein cleavage, core condensation, and increased stability of the viral RNA dimer. Inactivating the viral protease prevents protein cleavage; the resulting virions lack condensed cores and contain fragile RNA dimers. Therefore, protein cleavage is linked to virion morphological change and increased stability of the RNA dimer. However, it is unclear whether protein cleavage is sufficient for mediating virus RNA maturation. We have observed a novel phenotype in a murine leukemia virus capsid mutant, which has normal virion production, viral protein cleavage, and RNA packaging. However, this mutant also has immature virion morphology and contains a fragile RNA dimer, which is reminiscent of protease-deficient mutants. To our knowledge, this mutant provides the first evidence that Gag cleavage alone is not sufficient to promote RNA dimer maturation. To extend our study further, we examined a well-defined human immunodeficiency virus type 1 (HIV-1) Gag mutant that lacks a functional PTAP motif and produces immature virions without major defects in viral protein cleavage. We found that the viral RNA dimer in the PTAP mutant is more fragile and unstable compared with those from wild-type HIV-1. Based on the results of experiments using two different Gag mutants from two distinct retroviruses, we conclude that Gag cleavage is not sufficient for promoting RNA dimer maturation, and we propose that there is a link between the maturation of virion morphology and the viral RNA dimer.

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