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HLA-B polymorphism affects interactions with multiple endoplasmic reticulum proteins.

H R Turnquist1, H J Thomas, K R Prilliman

  • 1Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha 68198-6805, USA.

European Journal of Immunology
|November 9, 2000
PubMed
Summary
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Amino acid substitutions at position 116 significantly impact HLA class I molecule interactions with TAP, tapasin, and calreticulin. Specific subtypes, like HLA-B*1510, show strong association, while others, like HLA-B*1518, show minimal binding.

Area of Science:

  • Immunology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • The assembly of HLA class I molecules with the peptide-loading complex, including TAP (Transporter associated with antigen processing), tapasin, and calreticulin, is crucial for immune surveillance.
  • Amino acid residues within the HLA class I peptide-binding groove and surrounding regions can influence these interactions.

Purpose of the Study:

  • To investigate how specific amino acid substitutions at position 116 of HLA-B molecules affect their association with TAP and other components of the peptide-loading complex.
  • To compare the interaction profiles of a site-directed mutant and natural HLA-B subtypes with varying residues at position 116.

Main Methods:

  • Site-directed mutagenesis of HLA-B*0702 to create a Y116D mutant.
  • Co-immunoprecipitation assays to assess the association of HLA-B variants with TAP, tapasin, and calreticulin.

Related Experiment Videos

  • Flow cytometry to evaluate the surface expression of HLA class I molecules.

    • Main Results:

    • The HLA-B*0702 (Y116D) mutant exhibited enhanced association with TAP, tapasin, and calreticulin compared to wild-type HLA-B7.
    • Natural HLA-B15 subtypes displayed differential interactions: HLA-B*1510 (Tyrosine at 116) showed strong association, while HLA-B*1518 and HLA-B*1501 (Serine at 116) showed minimal association.
    • HLA-B15 subtypes with low intracellular assembly complex association had higher surface expression of the open heavy chain.

    Conclusions:

    • Position 116 is critical for the association of HLA-B molecules with the TAP complex and associated proteins.
    • Amino acid identity at position 116 dictates the strength of interaction with the entire peptide-loading complex.
    • Reduced intracellular assembly complex interaction may lead to increased surface stability of HLA class I molecules.