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ANIMAL VIRUSES

The C-Terminal Half of the Human Immunodeficiency Virus Type 1 Gag Precursor Is Sufficient for Efficient Particle Assembly

Alessandra Borsetti, Åsa Öhagen, Heinrich G. Göttlinger
Alessandra Borsetti
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02215
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Åsa Öhagen
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02215
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Heinrich G. Göttlinger
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02215
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DOI: 10.1128/JVI.72.11.9313-9317.1998
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    Fig. 1.

    Schematic representation of Gag deletion mutants. The domain structure of the Gag polyprotein and the position of the MHR within the CA domain are indicated. Numbers refer to the positions of the deleted amino acids relative to the initiating methionine.

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    Fig. 2.

    Effects of large deletions in CA on particle production. HeLa cells were transfected with wild-type proviral DNA (WT) or with the indicated mutants. (A) The cells were metabolically labeled with [35S]methionine from 48 to 60 h posttransfection, and viral proteins were immunoprecipitated from the cell lysates. (B) Viral particles released during the labeling period were pelleted through 20% sucrose cushions, and the protein profile of the pelleted material was directly analyzed by SDS-PAGE. The positions of specific viral proteins are indicted on the left. The Δ126-285 and Δ126-304 mutants were analyzed in duplicate.

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    Fig. 3.

    Efficient particle production in the absence of up to 50% of Pr55gag. HeLa cells transfected with the indicated proviral constructs were labeled with [35S]methionine, and viral proteins were immunoprecipitated from the cell lysates with patient serum (A). Particles released into the supernatant were pelleted through sucrose and directly analyzed by SDS-PAGE (B). The positions of specific viral proteins are indicated on the left. The positions of migration of molecular mass markers (in kilodaltons) are indicated on the right.

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    Fig. 4.

    Thin-section electron microscopy of HeLa cells transfected with the wild type provirus (A) or with the indicated Gag deletion mutants (B, C). Bars indicate a length of 100 nm.

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The C-Terminal Half of the Human Immunodeficiency Virus Type 1 Gag Precursor Is Sufficient for Efficient Particle Assembly
Alessandra Borsetti, Åsa Öhagen, Heinrich G. Göttlinger
Journal of Virology Nov 1998, 72 (11) 9313-9317; DOI: 10.1128/JVI.72.11.9313-9317.1998

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The C-Terminal Half of the Human Immunodeficiency Virus Type 1 Gag Precursor Is Sufficient for Efficient Particle Assembly
Alessandra Borsetti, Åsa Öhagen, Heinrich G. Göttlinger
Journal of Virology Nov 1998, 72 (11) 9313-9317; DOI: 10.1128/JVI.72.11.9313-9317.1998
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KEYWORDS

Gene Products, gag
HIV-1
Peptide Fragments
Protein Precursors

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