Literature DB >> 8888583

Ultrastructure and morphogenesis of human immunodeficiency virus.

M Nakai1, T Goto.   

Abstract

The ultrastructure and morphogenesis of human immunodeficiency virus (HIV) were elucidated by observation with several techniques including immunoelectron microscopy and cryo-microscopy. The virus particle consists of an envelope, a core and matrix. The virus particles were observed extracellularly as having one of three profiles: (1) a centric or an eccentric electron-dense core, (2) rod-shaped electron-dense core, and (3) doughnut-shaped. HIV-1 particles in the hydrated state were observed by high resolution electron cryo-microscopy to be globular, and the lipid membrane was clearly resolved as a bilayer. Many projections around the circumference were seen to be knob-like. The shapes and sizes of the projections, especially head parts, were found to vary in each projection. By isolation with Nonidet P40 and glutaraldehyde, HIV-1 cores were confirmed to consist of p24 protein by immunogold labeling. When the virus enters the cell, two entry modes were found: membrane fusion and endocytosis. No structures resembling virus particles could be seen in the cytoplasm after viral entry. In HIV-1-infected cells, positive reactions by immuno-labeling suggest that HIV-1 Gag may be produced in membrane-bound structures and transported to the cell surface by cytoskeletons. Then a crescent electron-dense layer was first formed underneath the cell membrane. Finally, the virus particle was released from the cell surface. Several cell clones producing defective particles were isolated from MT-4/HIV-1 cells. Among them, doughnut-shaped or teardrop-shaped particles were seen to be produced in the extracellular space. In the doughnut-shaped particles, Gag p17 and p24 proteins faced each other against the inner electron dense ring, suggesting that the inner ring consists of a precursor Gag protein.

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Year:  1996        PMID: 8888583     DOI: 10.1093/oxfordjournals.jmicro.a023441

Source DB:  PubMed          Journal:  J Electron Microsc (Tokyo)        ISSN: 0022-0744


  6 in total

1.  Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

Authors:  Uta K von Schwedler; Kirsten M Stray; Jennifer E Garrus; Wesley I Sundquist
Journal:  J Virol       Date:  2003-05       Impact factor: 5.103

2.  Cryoelectron microscopic examination of human immunodeficiency virus type 1 virions with mutations in the cyclophilin A binding loop.

Authors:  L B Kong; D An; B Ackerson; J Canon; O Rey; I S Chen; P Krogstad; P L Stewart
Journal:  J Virol       Date:  1998-05       Impact factor: 5.103

3.  Replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral protease.

Authors:  Steve C Pettit; Gavin J Henderson; Celia A Schiffer; Ronald Swanstrom
Journal:  J Virol       Date:  2002-10       Impact factor: 5.103

4.  Rev inhibition strongly affects intracellular distribution of human immunodeficiency virus type 1 RNAs.

Authors:  Dusan Cmarko; Stig-Ove Bøe; Catia Scassellati; Anne Marie Szilvay; Svend Davanger; Xiang-Dong Fu; Gunnar Haukenes; Karl-Henning Kalland; Stanislav Fakan
Journal:  J Virol       Date:  2002-10       Impact factor: 5.103

5.  Target cell type-dependent modulation of human immunodeficiency virus type 1 capsid disassembly by cyclophilin A.

Authors:  Yuan Li; Alak Kanti Kar; Joseph Sodroski
Journal:  J Virol       Date:  2009-08-05       Impact factor: 5.103

Review 6.  Cyclophilin A as a target in the treatment of cytomegalovirus infections.

Authors:  Ashwaq A Abdullah; Rasedee Abdullah; Zeenathul A Nazariah; Krishnan N Balakrishnan; Faez Firdaus J Abdullah; Jamilu A Bala; Mohd-Azmi Mohd-Lila
Journal:  Antivir Chem Chemother       Date:  2018 Jan-Dec
  6 in total

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