Class I MHC alpha 3 domain can function as an independent structural unit to bind CD8 alpha.
Publication/Presentation Date
3-1-1995
Abstract
Functional interactions between CD8-dependent cytotoxic T cells and their targets require physical contact between CD8 and a non-polymorphic determinant on the alpha 3 domain of the class I MHC molecule. We developed a cell-free assay to directly monitor this molecular interaction, specifically excluding the participation of other cellular proteins and lipids. This assay employed a soluble CD8 derivative and a plate-bound HLA-A2.1 derivative, alpha 3/MalE, in which the alpha 3 domain has been expressed independently of its neighboring polypeptide domains on the native class I MHC molecule and beta 2-microglobulin (beta 2-m). These proteins were produced using eukaryotic and prokaryotic expression systems, respectively. Our data demonstrated specific, saturable binding between soluble CD8 alpha (sCD8 alpha) and alpha 3/MalE, and the Kd of this interaction was determined to be 4.5 x 10(-7) M. Monoclonal antibodies (mAb) directed against either CD8 or the alpha 3 domain of class I MHC inhibited binding; mAb directed against other sites on class I MHC and beta 2-m did not. Our data suggest that the interaction between CD8 alpha and the alpha 3 domain of class I MHC does not require the participation of neighboring class I sequences or beta 2-m.
Volume
32
Issue
4
First Page
267
Last Page
275
ISSN
0161-5890
Published In/Presented At
Fayen, J., Huang, J. H., Meyerson, H., Zhang, D., Getty, R., Greenspan, N., & Tykocinski, M. (1995). Class I MHC alpha 3 domain can function as an independent structural unit to bind CD8 alpha. Molecular immunology, 32(4), 267–275. https://doi.org/10.1016/0161-5890(94)00149-u
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
7723772
Department(s)
Administration and Leadership
Document Type
Article