Proteins encoded by genes in the MHC are highly polymorphic. For class II proteins the highest level of polymorphism is found in distinct regions of variability, notably in the membrane-distal domains. To investigate the role of such residues in antigen presentation, we have tested cells transfected with wild-type or mutant I-Ak beta chains for their ability to present the NH2-terminal peptide of myelin basic protein to a panel of T cell clones. We were unable to detect a gross effect on peptide binding, in that all of the mutant cell lines presented antigen to at least one of the cloned T cells. However, the results imply that the more NH2-terminal residues, particularly 12 and 14, are involved in peptide interactions. Mutations at these residues presented antigen only at high antigen concentrations. Furthermore, residues of the more COOH-terminal regions appear to determine TCR interactions. Mutations in the predicted alpha-helical regions of the beta chain affected antigen presentation without abolishing peptide binding.
Article|
June 01 1989
The role of polymorphic I-Ak beta chain residues in presentation of a peptide from myelin basic protein.
C B Davis,
C B Davis
Department of Biological Sciences, Stanford University, California 94305.
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J M Buerstedde,
J M Buerstedde
Department of Biological Sciences, Stanford University, California 94305.
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D J McKean,
D J McKean
Department of Biological Sciences, Stanford University, California 94305.
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P P Jones,
P P Jones
Department of Biological Sciences, Stanford University, California 94305.
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H O McDevitt,
H O McDevitt
Department of Biological Sciences, Stanford University, California 94305.
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D C Wraith
D C Wraith
Department of Biological Sciences, Stanford University, California 94305.
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C B Davis
Department of Biological Sciences, Stanford University, California 94305.
J M Buerstedde
Department of Biological Sciences, Stanford University, California 94305.
D J McKean
Department of Biological Sciences, Stanford University, California 94305.
P P Jones
Department of Biological Sciences, Stanford University, California 94305.
H O McDevitt
Department of Biological Sciences, Stanford University, California 94305.
D C Wraith
Department of Biological Sciences, Stanford University, California 94305.
Online ISSN: 1540-9538
Print ISSN: 0022-1007
J Exp Med (1989) 169 (6): 2239–2244.
Citation
C B Davis, J M Buerstedde, D J McKean, P P Jones, H O McDevitt, D C Wraith; The role of polymorphic I-Ak beta chain residues in presentation of a peptide from myelin basic protein.. J Exp Med 1 June 1989; 169 (6): 2239–2244. doi: https://doi.org/10.1084/jem.169.6.2239
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