ArticleThe Journal of experimental medicine1991
Mutations in CD8 that affect interactions with HLA class I and monoclonal anti-CD8 antibodies.
Article in The Journal of experimental medicine, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed, 62 citations in OpenAlex.
- CD8 co-receptor modulates the specificity profile of the 1G4 TCR against NY-ESO-1.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- Structural basis of the CD8 alpha beta/MHC class I interaction: focused recognition orients CD8 beta to a T cell proximal position.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- Familial CD8 deficiency due to a mutation in the CD8 alpha gene.The Journal of clinical investigation · 2001Article
- Molecular analysis of protein interactions mediating the function of the cell surface protein CD8.Immunologic research · 1999Review
- Human CD8 transgene regulation of HLA recognition by murine T cells.The Journal of experimental medicine · 1995Article
- Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the alpha 2 and alpha 3 domains of MHC class I.The Journal of experimental medicine · 1995Article
- Complementarity determining region 1 (CDR1)- and CDR3-analogous regions in CTLA-4 and CD28 determine the binding to B7-1.The Journal of experimental medicine · 1994Article
- The role of charge and multiple faces of the CD8 alpha/alpha homodimer in binding to major histocompatibility complex class I molecules: support for a bivalent model.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- The CD58 (LFA-3) binding site is a localized and highly charged surface area on the AGFCC'C" face of the human CD2 adhesion domain.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- The alpha 3 domain of the Qa-2 molecule is defective for CD8 binding and cytotoxic T lymphocyte activation.The Journal of experimental medicine · 1993Article
- Delineation of an extended surface contact area on human CD4 involved in class II major histocompatibility complex binding.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Mutational analysis of the CD2/CD58 interaction: the binding site for CD58 lies on one face of the first domain of human CD2.The Journal of experimental medicine · 1993Article
- Reconstitution of the subclass-specific expression of CD4 in thymocytes and peripheral T cells of transgenic mice: identification of a human CD4 enhancer.The Journal of experimental medicine · 1993Article
- Structure of CD8 alpha and beta chains of the orangutan: novel patterns of mRNA splicing encoding hingeless polypeptides.Immunogenetics · 1992Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The T cell co-receptor, CD8, binds to the alpha 3 domain of HLA class I (Salter, R.D., R.J. Benjamin, P.K. Wesley, S.E. Buxton, T.P.J. Garrett, C. Clayberger, A.M. Krensky, A.M. Norman, D.R. Littman, and P. Parham. 1990. Nature [Lond.]. 345:41; Connolly, J.M., T.A. Potter, E.M. Wormstall, and T.H. Hansen. 1988. J. Exp. Med. 168:325; and Potter, T.A., T.V. Rajan, R.F. Dick II, and J.A. Bluestone. 1989. Nature [Lond.]. 337:73). To identify regions of CD8 that are important for binding to HLA class I, we performed a mutational analysis of the CD8 molecule in the immunoglobulin (Ig)-like variable domain. Our mutational analysis was based on our finding that using a cell-cell adhesion assay murine CD8 (Lyt-2) did not bind to human class I. Since the interaction of human CD8 with HLA class I is species specific, we substituted nonconservative amino acids from mouse CD8 and analyzed the ability of the mutated CD8 molecules expressed in COS 7 cells to bind HLA class I-bearing B lymphoblastoid cells, UC. Mutants with the greatest effect on binding were located in a portion of the molecule homologous to the first and second hypervariable regions of an antibody combining site. In addition, a panel of 12 anti-CD8 monoclonal antibodies were used to stain the 10 CD8 mutants, and amino acids that affected antibody binding were localized on the crystal structure of the Bence-Jones homodimer, REI. Support for an Ig-like structure of CD8 can be found in the pattern of substitutions affecting antibody binding. This work supports the similar tertiary structure of the CD8 alpha-terminal domain and an Ig variable domain.
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