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Comment
. 2014 Mar;11(2):117-9.
doi: 10.1038/cmi.2013.50. Epub 2013 Oct 7.

Critical role of butyrophilin 3A1 in presenting prenyl pyrophosphate antigens to human γδ T cells

Dieter Kabelitz
Comment

Critical role of butyrophilin 3A1 in presenting prenyl pyrophosphate antigens to human γδ T cells

Dieter Kabelitz. Cell Mol Immunol. 2014 Mar.
No abstract available

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Figures

Figure 1
Figure 1
Role of BTN3A1 in phosphoantigen presentation. (a) BTN3A1 consists of two Ig-like extracellular domains (IgV, IgC), a transmembrane region and an intracellular B30.2 domain. (b) Multimerization of BTN3A1 by agonistic anti-CD277 mAb 20.1 decreases lateral motility and induces a 19-Å rotational shift, which might somehow contribute to γδ T-cell activation. (c) As shown by Vavassori et al., the extracellular IgV domain of BTN3A1 can directly bind HMBPP and IPP, associated with conformational changes and direct interaction with the Vγ9Vδ2 TCR. The role of the intracellular B30.2 domain (if any) in this setting has not been determined. (d) It remains presently unclear how endogenously generated phosphoantigens (e.g., IPP accumulating in response to n-BP treatment) are ‘presented' by BTN3A1. Intracellular IPP might directly bind to B30.2 and thereby, change the conformation of extracellular IgV domain. Alternatively, intracellular IPP might be secreted and then bind directly to BTN3A1 on the same or neighboring cells. HMBPP, (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate; IPP, isopentenyl pyrophosphate; mAb, monoclonal antibody;n-BP, aminobisphosphonate; TCR, T-cell receptor. ▴, HMBPP or IPP phosphoantigens; formula image, anti-CD277 mAb 20.1.
See this image and copyright information in PMC

Comment on

References

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