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Two polymorphisms facilitate differences in plasticity between two chicken major histocompatibility complex class I

Alistair Bailey1, Andy van Hateren1, Tim Elliott1

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Major histocompatibility complex class I (MHC I) molecules present peptides to T-cells. Differences in chicken BF2 MHC I plasticity, influenced by specific polymorphisms, affect peptide selection and tapasin interaction, impacting immune response.

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Area of Science:

  • Immunology
  • Structural Biology
  • Computational Biology

Background:

  • Major histocompatibility complex class I (MHC I) molecules present intracellular peptides to cytotoxic T-cells.
  • Tapasin acts as a co-factor, assisting MHC I in selecting high-affinity peptides.
  • Chicken MHC I (BF2) exhibits unique co-evolution with tapasin, differing from mammalian systems.

Purpose of the Study:

  • To investigate if primary sequence polymorphisms in chicken BF2 MHC I explain functional differences in tapasin interaction and peptide selection.
  • To demonstrate the utility of complementary computational modeling approaches for understanding complex experimental data in molecular immunology.

Main Methods:

  • Mechanistic molecular dynamics simulations were employed to analyze protein plasticity.
  • Statistical coupling analysis was used to identify functionally relevant polymorphisms based on primary sequence.
  • Comparative analysis of BF2*15∶01 and BF2*19∶01 haplotypes.

Main Results:

  • Two specific polymorphisms between BF2*15∶01 and BF2*19∶01 were identified as key drivers of differential protein plasticity.
  • BF2*15∶01 exhibits greater intrinsic plasticity than BF2*19∶01, exploring a wider range of conformations without peptide.
  • A functionally significant protein sector connecting the peptide-binding site and the α3 domain (a putative tapasin-binding site) was identified, containing two polymorphic residues.

Conclusions:

  • Differences in MHC I protein plasticity, encoded by primary sequence polymorphisms, correlate with experimentally observed functional variations.
  • Tapasin may allosterically modulate MHC I plasticity to catalyze peptide selection, providing a mechanistic link between sequence, structure, and function.