Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Structural and functional identification of major histocompatibility complex class i-restricted self-peptides as naturally occurring molecular mimics of viral antigens - possible role in cd8(+) t cell-mediated, virus-induced autoimmune disease

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Hudrisier, D.
  • Riond, J.
  • Burlet-Schiltz, O.
  • von Herrath, M. G.
  • Lewicki, H.
  • Monsarrat, B.
  • Oldstone, Michael
  • Gairin, J. E.

publication date

  • June 2001

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Structural similarity (molecular mimicry) between viral epitopes and self-peptides can lead to the induction of autoaggressive CD4(+) as well as CD8(+) T cell responses. Based on the flexibility of T cell receptor/antigen/major histocompatibility complex recognition, it has been proposed that a self-peptide could replace a viral epitope for T cell recognition and therefore participate in pathophysiological processes in which T cells are involved. To address this issue, we used, as a molecular model of viral antigen, the H-2D(b)-restricted immunodominant epitope nucleoprotein (NP)-(396-404) (FQPQNGQFI) of lymphocytic choriomeningitis virus (LCMV). We identified peptide sequences from murine self-proteins that share structural and functional homology with LCMV NP-(396-404) and that bound to H-2D(b) with high affinity. One of these self-peptides, derived from tumor necrosis factor receptor I (FGPSNWHFM, amino acids 302-310), maintained LCMV-specific CD8(+) T cells in an active state as observed both in vitro in cytotoxic assays and in vivo in a model of virus-induced autoimmune diabetes, the rat insulin promoter-LCMV NP transgenic mouse. The natural occurrence and molecular concentration at the surface of H-2(b) spleen cells of tumor necrosis factor receptor I-(302-310) were determined by on-line micro-high pressure liquid chromatography/mass spectrometry and supported its biological relevance.

subject areas

  • Adoptive Transfer
  • Amino Acid Sequence
  • Animals
  • Antigens
  • Antigens, CD4
  • Autoimmune Diseases
  • CD8-Positive T-Lymphocytes
  • Cell Division
  • Cell Line
  • Chromatography, High Pressure Liquid
  • Dose-Response Relationship, Drug
  • Epitopes
  • Humans
  • Inhibitory Concentration 50
  • Insulin
  • Interferon-gamma
  • Major Histocompatibility Complex
  • Mass Spectrometry
  • Mice
  • Mice, Inbred BALB C
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Peptides
  • Promoter Regions, Genetic
  • Protein Binding
  • Rats
  • Spleen
  • Structure-Activity Relationship
  • Time Factors
  • Transplantation
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M008864200

PubMed ID

  • 11278441
scroll to property group menus

Additional Document Info

start page

  • 19396

end page

  • 19403

volume

  • 276

issue

  • 22

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support