2012
DOI: 10.1074/jbc.m112.384354
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The Molecular Basis for Modulation of Human Vγ9Vδ2 T Cell Responses by CD277/Butyrophilin-3 (BTN3A)-specific Antibodies

Abstract: Background: Phosphoisoprenoid stimulation of V␥9V␦2 T cells can be modulated by anti-BTNA3 antibodies. Results: Agonist and antagonist antibodies associate differently with BTN3A structurally and biophysically. Conclusion: Differential binding of antibodies to BTN3A modulates its oligomerization on the cell surface. Significance: Defining how ␥␦ T cells recognize antigen is critical for understanding their functions in the immune response.

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Cited by 154 publications
(230 citation statements)
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“…To identify those human chromosome(s) mandatory for PAg presentation, hybrid cells were cloned and tested for induction of reporter cell stimulation in the presence of 1 nM HMBPP. PCR karyotyping showed that loss of human chromosomes 2,3,7,8,9,10,11,13,17,18,20,21, and X had no effect on PAg-mediated activation of the reporter cells, while cells without Chr6 failed to induce activation of the reporter cells in the presence of HMBPP or zoledronate. For reasons so far unknown, 2 of 6 of the Chr6-bearing hybridoma cell lines stimulate the reporter cells in the presence of HMBPP and zoledronate but not in the presence of 2 mM sec-butylamine.…”
Section: Resultsmentioning
confidence: 99%
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“…To identify those human chromosome(s) mandatory for PAg presentation, hybrid cells were cloned and tested for induction of reporter cell stimulation in the presence of 1 nM HMBPP. PCR karyotyping showed that loss of human chromosomes 2,3,7,8,9,10,11,13,17,18,20,21, and X had no effect on PAg-mediated activation of the reporter cells, while cells without Chr6 failed to induce activation of the reporter cells in the presence of HMBPP or zoledronate. For reasons so far unknown, 2 of 6 of the Chr6-bearing hybridoma cell lines stimulate the reporter cells in the presence of HMBPP and zoledronate but not in the presence of 2 mM sec-butylamine.…”
Section: Resultsmentioning
confidence: 99%
“…Given that BTN3A1 protein loaded with PAg in a cell-free system binds to recombinant Vγ9Vδ2 TCRs [12], we would predict that the missing Chr6-encoded gene(s) relate to cellular functions such as PAg loading of the BTN3A1 molecule or control of its cellsurface distribution or cellular compartmentalization, for which the PAg-binding intracellular B30.2 domain of BTN3A1 might be crucial [8][9][10][11][12]. The colocalization of BTN3 with genes associated with antigen-presenting function might be by coincidence, but is clearly reminiscent of what is seen for peptide-presenting MHC molecules [15].…”
Section: Discussionmentioning
confidence: 99%
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“…22,23 This intracellular binding induced extracellular conformational changes of BTN3A, similar to those observed with 20.1 mAb and resulting Vg9Vd2 T cell activation. 24 Together, these data open new perspectives in Vg9Vd2 T cells-based immunotherapies, with BTN3A appearing as an interesting target to regulate their functions. In this study, we decided to investigate how BTN3A molecules might contribute to AML cells clearance through Vg9Vd2 T cells-based immunotherapy.…”
Section: Introductionmentioning
confidence: 99%