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Peptide binding to the class Ib molecule, Qa-1b

Z Kurepa1, J Forman

  • 1Department of Microbiology, University of Texas Southwestern Medical Center, Dallas 75235, USA.

Journal of Immunology (Baltimore, Md. : 1950)
|April 1, 1997
PubMed
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We analyzed how a Qdm peptide interacts with the Qa-1b molecule. Specific binding was observed, with high affinity and a slow dissociation rate, suggesting Qdm peptide occupies many Qa-1b molecules.

Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • The interaction between peptides and Major Histocompatibility Complex (MHC) molecules is crucial for immune responses.
  • Class Ib MHC molecules, like Qa-1b, present peptides and play roles in immune surveillance.
  • Understanding peptide-MHC interactions provides insights into immune regulation and disease.

Purpose of the Study:

  • To characterize the binding kinetics and affinity of a nonameric peptide (Qdm) to the class Ib molecule Qa-1b.
  • To identify key residues within the Qdm peptide that are essential for Qa-1b binding.
  • To determine the implications of Qdm peptide binding for Qa-1b occupancy on cells.

Main Methods:

  • Direct binding assays using radiolabeled Qdm peptide on Qa-1b expressing cells.

Related Experiment Videos

  • Kinetic analysis to determine on- and off-rates of peptide binding.
  • Site-directed mutagenesis of Qdm peptide residues to alanine or glycine to assess binding.
  • Competitive binding experiments using unlabeled Qdm and control peptides to confirm specificity.

    • Main Results:

    • Specific binding of iodinated Qdm peptide to Qa-1b expressing cells was demonstrated.
    • Binding affinity (Kd) was calculated to be between 0.2 and 1.1 x 10(-10) M, indicating high affinity.
    • The dissociation half-life (t1/2) was approximately 10 hours, suggesting slow dissociation.
    • Substitution of Leucine at position 9 significantly reduced binding, while mutations at positions 2 and 5 had a lesser effect. Simultaneous mutations at positions 2 and 9 abrogated binding.

    Conclusions:

    • The Qdm peptide binds to Qa-1b with high affinity and slow dissociation kinetics.
    • The binding characteristics of Qdm peptide suggest it can occupy a significant proportion of Qa-1b molecules.
    • Residues at positions 2 and 9 of the Qdm peptide are critical for high-affinity binding to Qa-1b.