T cell epitope "hotspots" on the HIV Type 1 gp120 envelope protein overlap with tryptic fragments displayed by mass spectrometry

AIDS Res Hum Retroviruses. 2005 Feb;21(2):165-70. doi: 10.1089/aid.2005.21.165.

Abstract

Our previous work has shown that immunodominant T-helper cell epitopes cluster within distinct fragments on a single face of the HIV envelope gp120 protein. We show in this report that the general positions of immunodominant epitopes are shared by T cells derived from BALB/c, C57BL/6, and CB6F1 mice, yet the precise peptides recognized by the responding T cell populations may differ. In addition, we find that gp120 peptides displayed by tryptic digestion and mass spectrometry of a purified HIV envelope protein share location with peptides defined as immunodominant T cell targets. Results are consistent with the suggestion that gp120 peptide location influences antigen processing, which, in turn, influences the specificity of immunodominant T cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • AIDS Vaccines / immunology
  • Amino Acid Sequence
  • Animals
  • Epitopes, T-Lymphocyte*
  • HIV Envelope Protein gp120 / immunology*
  • Immunodominant Epitopes*
  • Mass Spectrometry
  • Mice
  • Mice, Inbred BALB C
  • Mice, Inbred C57BL
  • Molecular Sequence Data
  • Peptide Fragments / immunology*
  • Trypsin / pharmacology

Substances

  • AIDS Vaccines
  • Epitopes, T-Lymphocyte
  • HIV Envelope Protein gp120
  • Immunodominant Epitopes
  • Peptide Fragments
  • Trypsin