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Science 17 January 1986:
Vol. 231. no. 4735, pp. 255 - 258
DOI: 10.1126/science.3484558
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Articles

Science, Vol 231, Issue 4735, 255-258
Copyright © 1986 by American Association for the Advancement of Science

articles

T-cell recognition of Ia molecules selectively altered by a single amino acid substitution

MA Brown, LA Glimcher, EA Nielsen, WE Paul, and RN Germain

T lymphocytes recognize foreign antigen together with allele-specific determinants on membrane-bound class I and class II (Ia) gene products of the major histocompatibility complex. To identify amino acids of class II molecules critical to this recognition process, the genes encoding the beta chains of the I-Ak molecule were cloned from a wild-type B-cell hybridoma and from an immunoselected variant subline showing distinct serological and T-cell stimulatory properties. Nucleotide sequencing and DNA-mediated gene transfer established that a single base transition (G----A) encoding a change from glutamic acid to lysine at position 67 in the I-Ak beta molecule accounted for all the observed phenotypic changes of the variant cells. These results confirm the importance of residues 62 to 78 in the amino terminal domain of I-A beta for class II-restricted T-cell recognition of antigen and demonstrate the ability of a single substitution in this region to alter this recognition event.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Molecular Studies of Antigen Processing and Presentation to T Cells by Class II MHC Molecules.
J.A. Berzofsky, A. Kurata, H. Takahashi, S.J. Brett, and D.J. McKean (1989)
Cold Spring Harb Symp Quant Biol 54, 417-430
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