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Mechanisms and Specificity of HIV Entry into Host Cells pp 203–221Cite as

The Assembly of the HIV-1 Env Glycoprotein into Dimers and Tetramers

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 300))

Abstract

The envelope (env) glycoprotein of human immunodeficiency virus 1 (HIV-1), initially synthesized as a precursor molecule termed gp160, is cleaved into two noncovalently associated subunits prior to delivery to the plasma membrane. We have studied the oligomeric structure of this protein using chemical cross-linking, velocity gradient sedimentation, and SDS-resistance. We find that gp160 forms stable homodimers after synthesis. After cleavage to gp120/gp41 the molecule becomes less stable to detergent solubilization and centrifugation but remains dimeric. Interactions between the 129 amino terminal residues in the ectodomains of adjoining gp41 subunits are both sufficient and necessary for assembly. In addition, tetramers composed of two dimers were also formed. Larger structures were not observed. The tetrameric paramyxovirus F protein, which has structural and functional similarities to the HIV-1 env protein, also forms a dimer of dimers.

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Author information

Authors and Affiliations

  1. Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, 20892, USA

    Robert W. Doms, Patricia L. Earl & Bernard Moss

  2. Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, 20892, USA

    Robert W. Doms

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  1. Robert W. Doms
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  2. Patricia L. Earl
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  3. Bernard Moss
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Editors and Affiliations

  1. University of the Pacific, San Francisco, California, USA

    Nejat Düzgüneş

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© 1991 Plenum Press, New York

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Doms, R.W., Earl, P.L., Moss, B. (1991). The Assembly of the HIV-1 Env Glycoprotein into Dimers and Tetramers. In: Düzgüneş, N. (eds) Mechanisms and Specificity of HIV Entry into Host Cells. Advances in Experimental Medicine and Biology, vol 300. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5976-0_13

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  • DOI: https://doi.org/10.1007/978-1-4684-5976-0_13

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5978-4

  • Online ISBN: 978-1-4684-5976-0

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