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Oligomeric structure of the human immunodeficiency virus type I envelope protein on the virion surface

  1. Author:
    Center, R. J.
    Leapman, R. D.
    Lebowitz, J.
    Arthur, L. O.
    Earl, P. L.
    Moss, B.

  2. Author Address

    NIAID, Viral Dis Lab, NIH, Bldg 4,Room 229,9000 Rockville Pike, Bethesda, MD 20892 USA NIAID, Viral Dis Lab, NIH, Bethesda, MD 20892 USA NIH, Div Bioengn & Phys Sci, Off Res Serv, Bethesda, MD 20892 USA NCI, AIDS Vaccine Program, Sci Applicat Int Corp, Frederick, MD 21702 USA Moss B NIAID, Viral Dis Lab, NIH, Bldg 4,Room 229,9000 Rockville Pike, Bethesda, MD 20892 USA
    1. Year: 2002
  2. Journal: Journal of Virology
    1. 76
    2. 15
    3. Pages: 7863-7867
  4. Type of Article: Article
  1. Abstract:

    The envelope protein (Env) of human immunodeficiency virus type 1 forms homo-oligomers in the endoplasmic reticullum. The oligomeric structure of Env is maintained after cleavage in a Golgi compartment and transport to the surfaces of infected cells, where incorporation into budding virions takes place. Here, we use biophysical techniques to assess the oligomeric valency of virion-associated Env prior to fusion activation. Virion-associated Env oligomers were stabilized by chemical cross-linking prior to detergent extraction and were purified by immunoaffinity chromatography. Gel filtration revealed a single predominant oligomeric species, and sedimentation equilibrium analysis-derived mass values indicated a trimeric structure. Determination of the masses of individual Env molecules by scanning transmission electron microscopy demonstrated that virion-associated Env was trimeric, and a triangular morphology was observed in 20 to 30% of the molecules. These results, which firmly establish the oligomeric structure of human immunodeficiency virus virion-associated Env, parallel those of our previous analysis of the simian immunodeficiency virus Env.

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