Correction: Prevention of Vγ9Vδ2 T cell activation by a Vγ9Vδ2 TCR nanobody (Journal of Immunology (2017) 198 (308-317))

Abstract

BTN3A1 and VHH 5E7 were transposed in the column headings of Table II as published. The corrected table is shown below. The authors also wish to correct the text in one paragraph in the Discussion. The paragraph beginning with "Previously, mutagenesis experiments have shown. . ." should read as follows: Previously, mutagenesis experiments have shown that variations in the Vγ9Vd2 TCR CDR3δ2 region, which may differ within and between individuals, determine phosphoantigen/BTN3A1-mediated Vγ9Vδ2 TCR activation. However, no specific sequence was required except for an aliphatic residue at position 97 and restrictions regarding the length of the CDR (10, 75). In accordance, we found multiple interactions in the CDR3δ2 98-103 region for both models of the Vγ9Vδ2 TCR-VHH 5E7 and the Vγ9Vδ2 TCR-BTN3A1 complex, as well as an additional CDR3δ2 Leu 97 interaction in the latter. Of note, mutations in the CDR3δ2 98-103 region of the Vγ9Vδ2 TCR did not abrogate VHH 5E7 binding (Supplemental Fig. 3), suggesting that VHH 5E7 will be widely applicable when considering clinical utility. Additionally, interactions were also predicted for the Vγ9 chain with VHH 5E7 and BTN3A1. Both molecules were found to interact with γ9 Lys 109, a residue previously reported to be involved in Vg9Vd2 TCR activation (76, 77). Considering the relevance of the δ2 chain interactions reported in the current study and previously (10, 78), the γ9 interactions are likely to be primarily relevant for stabilization of the interaction with Vδ2. Additionally, we found residue γ9 Tyr 54 to interact with both BTN3A1 and VHH 5E7, which is in accordance with the suggestion that this residue is involved in contacting the Ag-presenting molecule of the Vγ9Vδ2 TCR (75). (Table Presented).