International Immunology, Vol. 11, No. 12, 1897-1906,
December 1999
© 1999 Japanese Society for Immunology
Definition and transfer of a serological epitope specific for peptide-empty forms of MHC class I
Department of Genetics, Washington University School of Medicine, St Louis, MO 63110, USA
1 Department of Newborn Medicine, Children's Hospital, St Louis, MO 63110, USA
2 Department of Biochemistry and Biophysics, Texas A & M University, College Station, TX 77843, USA
Correspondence to: T. H. Hansen
Nascent class I molecules have been hypothesized to undergo a conformational change when they bind peptide based on the observation that most available antibodies only detect peptide-loaded class I. Furthermore recent evidence suggests that this peptide-facilitated conformational change induces the release of class I from association with transporter associated with antigen processing (TAP)/tapasin and other endoplasmic reticulum proteins facilitating class I assembly. To learn more about the structure of peptide-empty class I, we have studied mAb 64-3-7 that is specific for peptide-empty forms of Ld. We show here that mAb 64-3-7 detects a linear stretch of amino acids including principally residues 48Q and 50P. Furthermore, we demonstrate that the 64-3-7 epitope can be transferred to other class I molecules with limited mutagenesis. Interestingly, in the folded class I molecule residues 48 and 50 are on a loop connecting a ß strand (under the bound peptide) with the 
1 helix (rising above the ligand binding site). Thus it is attractive to propose that this loop is a hinge region. Importantly, the three-dimensional structure of this loop is strikingly conserved among class I molecules. Thus our findings suggest that all class I molecules undergo a similar conformational change in the loop around residues 48 and 50 when they associate with peptide.
Keywords: H chain conformation, peptide binding
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