Structure-function analysis of Ia molecules: in-phase insertion mutagenesis of the amino-terminal domain of the Eβk polypeptide chain

Najet Rebaï, François Letourneur, Nilabh Shastri, Sylvie Marchetto, Michel Pierres, Bernard Malissen

Research output: Contribution to journalArticlepeer-review

Abstract

To identify which segments of the β1 domain of the Eβk polypeptide control T cell recognition of antigen, Eβ genes were constructed with in-phase insertion mutations. Five independent mutants, with insertions mapping to positions 24, 50 and 93 of the Eβk polypeptide, were obtained. Cell lines expressing these mutated genes were analysed by microfluorometry using a panel of 20 anti-Ek monoclonal antibodies. None of the tested in-phase insertions has resulted in the loss of antibody binding sites. In striking contrast, mutations at position 93 and at a lesser level 50 were indicative of a crucial role of the corresponding regions in T-cell recognition, because they led to significant or complete loss of antigen-presenting function with all but one of the T hybridomas tested. These data are discussed with regard to a model of the foreign antigen binding site fo Ia molecules.

Original languageEnglish (US)
Pages (from-to)927-935
Number of pages9
JournalBiochimie
Volume70
Issue number7
DOIs
StatePublished - Jul 1988
Externally publishedYes

Keywords

  • Ia molecule
  • T-cell recognition
  • gene transfer
  • in-phase insertion mutation

ASJC Scopus subject areas

  • Biochemistry

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