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Crystal structures and KIR3DL1 recognition of three immunodominant viral peptides complexed to HLA-B*2705

Guillame B E Stewart-Jones1, Kati di Gleria, Simon Kollnberger

  • 1The Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, Oxford, UK.

European Journal of Immunology
|January 20, 2005
PubMed

Insights

We determined the crystal structures of HLA-B*2705 complexes with viral peptides from EBV, influenza, and HIV. These structures reveal how HLA-B*2705 presents peptides, influencing T cell responses and immune evasion in HIV infection.

Area of Science:

  • Immunology
  • Structural Biology
  • Virology

Background:

  • HLA-B*2705 is crucial for presenting viral peptides to T cells, impacting HIV progression.
  • Understanding HLA-B*2705-peptide interactions is key to T cell recognition and immune responses.

Purpose of the Study:

  • To elucidate the structural basis of HLA-B*2705 presenting immunodominant viral peptides.
  • To investigate the role of peptide conformation and specific residues in T cell and KIR3DL1 recognition.

Main Methods:

  • X-ray crystallography to solve the structures of three HLA-B*2705-peptide complexes.
  • Analysis of peptide binding and interactions within the HLA-B*2705 B-pocket.
  • Assessment of tetrameric complex binding to the killer-Ig-like receptor (KIR)3DL1.

Main Results:

  • Crystal structures of HLA-B*2705 with EBV, influenza, and HIV peptides were determined.
  • A key arginine anchor in the HIV peptide explains immune escape upon mutation.
  • HLA-B*2705 presents peptides in diverse conformations, with exposed residues influencing interactions.
  • HIV and influenza peptide complexes bound KIR3DL1, unlike the EBV peptide complex, which could be altered by mutation.

Conclusions:

  • HLA-B*2705 exhibits varied peptide presentation, influencing immune recognition.
  • Structural insights explain HIV immune escape mechanisms related to peptide binding.
  • Peptide features and HLA-B*2705 conformation dictate KIR3DL1 interactions, offering potential therapeutic targets.

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