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Related Experiment Videos

Mutations in specific I-A(k) alpha(2) and beta(2) domain residues affect surface expression.

M L Lang1, S Yadati, E S Seeley

  • 1Department of Microbiology, Dartmouth Medical School, Lebanon, NH 03756, USA.

International Immunology
|June 6, 2000
PubMed
Summary

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Specific mutations in class II molecules hinder plasma membrane expression and affect antigen presentation. These findings shed light on the complex mechanisms governing Major Histocompatibility Complex class II function.

Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Previous studies showed mutations in class II dimer-of-dimers contact residues affect antigen presentation but not plasma membrane expression.
  • This study investigates class II mutations that *do* inhibit plasma membrane expression.

Purpose of the Study:

  • To examine the effects of specific mutations (H alpha 181D and E beta 170K) in class II molecules on their plasma membrane expression and antigen presentation.
  • To understand the role of these mutations in intracellular trafficking and complex formation.

Main Methods:

  • Site-directed mutagenesis to introduce mutations H alpha 181D and E beta 170K into class II molecules.
  • Analysis of plasma membrane expression using transfectants.
  • Investigation of intracellular transport and localization using hen egg lysozyme (HEL) as a fluid-phase marker.

Related Experiment Videos

  • Assessment of class II compact dimer (CD) formation.
  • Molecular modeling to predict interactions between mutant class II and invariant chain (Ii).

    • Main Results:

    • Molecules with both H alpha 181D and E beta 170K mutations showed low plasma membrane expression, while single mutations had normal expression.
    • Mutant class II molecules were transported to endosomal compartments accessible to HEL.
    • Lysozyme treatment enhanced CD formation, particularly for the double mutant, but this did not correlate with increased surface expression.
    • The joint mutation prevents efficient CD formation in the absence of high peptide concentrations, potentially by affecting invariant chain (Ii) proteolysis or class II stability.
    • At high exogenous peptide concentrations, CD formation occurred, but plasma membrane expression was still inhibited.

    Conclusions:

    • The combined H alpha 181D and E beta 170K mutations impair class II transport to the plasma membrane.
    • These mutations influence invariant chain (Ii) processing and/or the stability of the peptide-loaded class II molecule.
    • Molecular modeling suggests these mutations may directly interact with the invariant chain (Ii), impacting its function.