Special Issue: Structural and Molecular Biology of HIV

Summers, Michael F.; Karn, Jonathan

doi:10.1016/j.jmb.2011.05.001

Cited by 3 publications

(4 citation statements)

References 19 publications

(8 reference statements)

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“…This view is from the top of the CA-NTD domain and shows the hexagonal arrangement of the Gag lattice. To calculate the theoretical FRET efficiency from this structural model, we selected one of the CA-NTD domain of the hexameric unit [1] (gold surface). The CA-NTD domains of the hexameric units [1], [2] and [3], interacting with the selected CA-NTD, are in magenta.…”

Section: Discussionmentioning

confidence: 99%

“…To calculate the theoretical FRET efficiency from this structural model, we selected one of the CA-NTD domain of the hexameric unit [1] (gold surface). The CA-NTD domains of the hexameric units [1], [2] and [3], interacting with the selected CA-NTD, are in magenta. The other CA-NTD domains located at a distance compatible with FRET are in blue and the CA-NTD domains too far from the domain in gold to provide significant FRET are in gray.…”

Section: Discussionmentioning

confidence: 99%

“…During and/or soon after assembly, Gag molecules undergo maturation by the viral protease generating the MAp17, CAp24, NCp7 and p6 proteins found in infectious mature virions [1,2]. A generally accepted model for HIV-1 assembly stipulates that the genomic RNA acts as a scaffolding platform onto which Gag molecules bind via NC, then kick-starting assembly [3][4][5][6].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Role of the Nucleocapsid Domain in HIV-1 Gag Oligomerization and Trafficking to the Plasma Membrane: A Fluorescence Lifetime Imaging Microscopy Investigation

Meshri

Dujardin

Godet

et al. 2015

Journal of Molecular Biology

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Role of the Nucleocapsid Domain in HIV-1 Gag Oligomerization and Trafficking to the Plasma Membrane: A Fluorescence Lifetime Imaging Microscopy Investigation

Meshri

Dujardin

Godet

et al. 2015

Journal of Molecular Biology

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“…In HIV-1, Gag contains the C-terminal p6 domain, which is critical for release of viral particles from the plasma membrane (PM). During virus particle assembly, MA serves as the membrane-targeting and binding domain (7)(8)(9), CA facilitates Gag multimerization (10)(11)(12)(13), and NC binds the ⌿ packaging signal in the viral RNA for encapsidation of the viral genome and contributes to the formation of Gag-Gag interactions (1,(14)(15)(16)(17).…”

mentioning

confidence: 99%

Mechanistic Differences between Nucleic Acid Chaperone Activities of the Gag Proteins of Rous Sarcoma Virus and Human Immunodeficiency Virus Type 1 Are Attributed to the MA Domain

Rye-McCurdy

Nadaraia-Hoke

Gudleski-O'Regan

et al. 2014

J Virol

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Host cell tRNAs are recruited for use as primers to initiate reverse transcription in retroviruses. Human immunodeficiency virus type 1 (HIV-1) uses tRNALys3 as the replication primer, whereas Rous sarcoma virus (RSV) uses tRNA Trp . The nucleic acid (NA) chaperone function of the nucleocapsid (NC) domain of HIV-1 Gag is responsible for annealing tRNA Lys3 to the genomic RNA (gRNA) primer binding site (PBS). Compared to HIV-1, little is known about the chaperone activity of RSV Gag. In this work, using purified RSV Gag containing an N-terminal His tag and a deletion of the majority of the protease domain (H6.Gag.3h), gel shift assays were used to monitor the annealing of tRNA Trp to a PBS-containing RSV RNA. Here, we show that similar to HIV-1 Gag lacking the p6 domain (Gag⌬p6), RSV H6.Gag.3h is a more efficient chaperone on a molar basis than NC; however, in contrast to the HIV-1 system, both RSV H6.Gag.3h and NC have comparable annealing rates at protein saturation. The NC domain of RSV H6.Gag.3h is required for annealing, whereas deletion of the matrix (MA) domain, which stimulates the rate of HIV-1 Gag⌬p6 annealing, has little effect on RSV H6.Gag.3h chaperone function. Competition assays confirmed that RSV MA binds inositol phosphates (IPs), but in contrast to HIV-1 Gag⌬p6, IPs do not stimulate RSV H6.Gag.3h chaperone activity unless the MA domain is replaced with HIV-1 MA. We conclude that differences in the MA domains are primarily responsible for mechanistic differences in RSV and HIV-1 Gag NA chaperone function. IMPORTANCEMounting evidence suggests that the Gag polyprotein is responsible for annealing primer tRNAs to the PBS to initiate reverse transcription in retroviruses, but only HIV-1 Gag chaperone activity has been demonstrated in vitro. Understanding RSV Gag's NA chaperone function will allow us to determine whether there is a common mechanism among retroviruses. This report shows for the first time that full-length RSV Gag lacking the protease domain is a highly efficient NA chaperone in vitro, and NC is required for this activity. In contrast to results obtained for HIV-1 Gag, due to the weak nucleic acid binding affinity of the RSV MA domain, inositol phosphates do not regulate RSV Gag-facilitated tRNA annealing despite the fact that they bind to MA. These studies provide insight into the viral regulation of tRNA primer annealing, which is a potential target for antiretroviral therapy.

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Multiple Functions and Disordered Nature of Nucleocapsid Proteins of Retroviruses and Hepadnaviruses

Darlix¹,

Rocquigny²

2020

Viruses and Viral Infections in Developing Countries

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Special Issue: Structural and Molecular Biology of HIV

Cited by 3 publications

References 19 publications

Role of the Nucleocapsid Domain in HIV-1 Gag Oligomerization and Trafficking to the Plasma Membrane: A Fluorescence Lifetime Imaging Microscopy Investigation

Role of the Nucleocapsid Domain in HIV-1 Gag Oligomerization and Trafficking to the Plasma Membrane: A Fluorescence Lifetime Imaging Microscopy Investigation

Mechanistic Differences between Nucleic Acid Chaperone Activities of the Gag Proteins of Rous Sarcoma Virus and Human Immunodeficiency Virus Type 1 Are Attributed to the MA Domain

Multiple Functions and Disordered Nature of Nucleocapsid Proteins of Retroviruses and Hepadnaviruses

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