Probing the conformation of the human T-lymphotropic virus I envelope protein complex with monoclonal antibodies

J Gen Virol. 1996 Sep;77 ( Pt 9):2025-9. doi: 10.1099/0022-1317-77-9-2025.

Abstract

We are investigating the binding of a series of monoclonal antibodies to native and detergent-treated human T-lymphotropic virus I (HTLV-I) envelope proteins to explore their conformation. A comparison of our data with previously published findings suggests that a central neutralization domain (aa 175-200) is folded such that only short stretches are exposed at the surface of the native envelope protein complex. However, the complete domain becomes accessible after treatment with mild non-ionic detergents, suggesting that envelope subunit interaction may partially obscure this domain. We further provide immunochemical evidence that a region containing a heptad repeat in the extracellular part of the transmembrane protein is folded towards the interior of the HTLV-I envelope complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / immunology
  • Cell Line
  • Epitope Mapping
  • Gene Products, env / chemistry*
  • Gene Products, env / immunology
  • HTLV-I Antigens / chemistry*
  • HTLV-I Antigens / immunology
  • Human T-lymphotropic virus 1 / chemistry*
  • Human T-lymphotropic virus 1 / immunology
  • Humans
  • Molecular Sequence Data
  • Protein Conformation
  • Retroviridae Proteins, Oncogenic / chemistry*
  • Retroviridae Proteins, Oncogenic / immunology
  • Spodoptera / cytology
  • env Gene Products, Human Immunodeficiency Virus

Substances

  • Antibodies, Monoclonal
  • Gene Products, env
  • HTLV-I Antigens
  • Retroviridae Proteins, Oncogenic
  • env Gene Products, Human Immunodeficiency Virus
  • gp21 protein, Human T-lymphotropic virus 1
  • gp46 protein, Human T-cell leukemia virus type I