Inner architecture of human and simian immunodeficiency viruses

Fukui, Takeshi; Imura, Shunro; Goto, Toshiyuki; Nakai, Masuyo

doi:10.1002/jemt.1070250410

Cited by 8 publications

(4 citation statements)

References 32 publications

(30 reference statements)

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“…Isolation and biochemical analysis of the core have been reported for a number of retroviruses (Fukui et al, 1993;Kotov et al, 1999;Accola et al, 2000;Welker et al, 2000;Palmer et al, 1988;Chrystie and Almeida, 1989;Benzair et al, 1986;Roberts and Oroszlan, 1989;Nermut et al, 1972;Lange et al, 1973;Bolognesi et al, 1972Bolognesi et al, , 1973Teramoto et al, 1977;Bader et al, 1970;Stromberg, 1972;Stromberg et al, 1973). A general conclusion from these studies is that the retroviral core appears to be fragile, and inherently unstable, once the viral membrane has been removed.…”

Section: Introductionmentioning

confidence: 85%

“…The cores of lentiviruses such as HIV, SIV, and EIAV are elongated and predominantly conical in shape (Chrystie and Almeida, 1989;Fukui et al, 1993;Roberts and Oroszlan, 1989;Accola et al, 2000;Welker et al, 2000). In contrast, the cores of RSV appear relatively isometric, based on their appearance in the electron microscope.…”

Section: The Appearance Of the Viral Core In Projectionmentioning

confidence: 92%

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The Organization of Mature Rous Sarcoma Virus as Studied by Cryoelectron Microscopy

Kingston

Olson

Vogt

2001

Journal of Structural Biology

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Section: Introductionmentioning

confidence: 85%

Section: The Appearance Of the Viral Core In Projectionmentioning

confidence: 92%

The Organization of Mature Rous Sarcoma Virus as Studied by Cryoelectron Microscopy

Kingston

Olson

Vogt

2001

Journal of Structural Biology

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“…Electron microscopy of protein solutions containing 4 to 10 mg/ml of purified CA protein in 50 mM Tris buffer, pH 8.0, 30 mM NaCl on formvar-carbon grids stained with 2% uranyl acetate revealed large structures similar in morphology to cores isolated from particles assembled in natural infection (Fig. 1; Chrystie and Almeida, 1988;Gelderblom, 1991;Fukui et al, 1993). To prepare dust-free protein solutions for lightscattering measurements, the solutions were filtered through buffer-equilibrated sterile 0.45-m pore-size membrane filters (Millipore, Bedford, MA) into 17-mm-OD light-scattering cells that were rinsed with distilled acetone to ensure dust-free condition before use.…”

Section: Protein Preparationmentioning

confidence: 99%

HIV-1 Capsid Protein Forms Spherical (Immature-Like) and Tubular (Mature-Like) Particles in Vitro: Structure Switching by pH-induced Conformational Changes

Ehrlich

Liu

Scarlata

et al. 2001

Biophysical Journal

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The viral genome and replicative enzymes of the human immunodeficiency virus are encased in a shell consisting of assembled mature capsid protein (CA). The core shell is a stable, effective protective barrier, but is also poised for dissolution on cue to allow transmission of the viral genome into its new host. In this study, static light scattering (SLS) and dynamic light scattering (DLS) were used to examine the entire range of the CA protein response to an environmental cue (pH). The CA protein assembled tubular structures as previously reported but also was capable of assembling spheres, depending on the pH of the protein solution. The switch from formation of one to the other occurred within a very narrow physiological pH range (i.e., pH 7.0 to pH 6.8). Below this range, only dimers were detected. Above this range, the previously described tubular structures were detected. The ability of the CA protein to form a spherical structure that is detectable by DLS but not by electron microscopy indicates that some assemblages are inherently sensitive to perturbation. The dimers in equilibrium with these assemblages exhibited distinct conformations: Dimers in equilibrium with the spherical form exhibited a compact conformation. Dimers in equilibrium with the rod-like form had an extended conformation. Thus, the CA protein possesses the inherent ability to form metastable structures, the morphology of which is regulated by an environmentally-sensitive molecular switch. Such metastable structures may exist as transient intermediates during the assembly and/or disassembly of the virus core.

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“…Despite multiple examples of core, core-like, and/or electron densities resembling cores embedded in the membrane as shown here by particle labeled 6 (also see Fig. 4A), well-defined structures resembling intact nucleocapsids (Fukui et al, 1993) are seldom seen in the cytoplasm of the infected cells. Figure 4B is a very high-resolution image of a mature HIV-1 particle as shown above for particle 5 in Figure 4A.…”

Section: Dmentioning

confidence: 86%

Alterations of lymphocyte membranes during HIV‐1 infection via multiple and simultaneous entry strategies

Fermin¹,

Garry²

2005

Microscopy Res & Technique

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Human immunodeficiency virus type 1 (HIV-1) must bind to and enter lymphocytes to replicate and cause the acquired immunodeficiency syndrome. The association of viral particles with the lymphocyte plasma membrane may vary according to a multitude of unknown variables, including lymphocyte membrane receptor mobilization, lipid raft aggregation, clathrin, caveolin, endosomes, microendosome-mediated penetration or penetration through a hole in the membrane. The time course of this delivery appears to be short. Fusion of the virion membrane and lymphocyte plasma membrane leads to destabilization of the lymphocyte membrane. Five morphological stages of membrane alteration were observed in the infected lymphocytes: (1) swelling, (2) splitting, (3) fusion, (4) breaking, and (5) thinning of the lipid bilayer. These plasma membrane alterations were not contributed by fixation artifacts, because the dimensions and distance between the subunits of the surface glycoprotein (SU, gp120) and the transmembrane glycoprotein (gp41) of the viral particles adjacent to the infected cells and processed at the same time remained unchanged. Destabilization of lipid raft patches in the lymphocyte plasma membrane by unknown variables may facilitate HIV-1 penetration of lymphocyte, and other cell types. This a combined review of the pertinent literature with our data showing that HIV-1 may take advantage of multiple penetration approaches simultaneously in the same cell type (H9) to overwhelm the infected cells. The ultrastructural details of H9 cultured cells infected in vitro with HIV-1 contribute to our understanding of viral particle association with the plasma membrane of infected cells.

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Inner architecture of human and simian immunodeficiency viruses

Cited by 8 publications

References 32 publications

The Organization of Mature Rous Sarcoma Virus as Studied by Cryoelectron Microscopy

The Organization of Mature Rous Sarcoma Virus as Studied by Cryoelectron Microscopy

HIV-1 Capsid Protein Forms Spherical (Immature-Like) and Tubular (Mature-Like) Particles in Vitro: Structure Switching by pH-induced Conformational Changes

Alterations of lymphocyte membranes during HIV‐1 infection via multiple and simultaneous entry strategies

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