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Chain Junctional Region in Prenyl Pyrophosphate Antigen Recognition by 
T Cells1
Lymphocyte Biology Section, Division of Rheumatology, Immunology, and Allergy, Department of Medicine, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115
Human 
T cells recognize prenyl pyrophosphate Ags and their
analogues in a V2V2 TCR-dependent manner. Few data are available
regarding the TCR structural requirements for recognition of such
prenyl pyrophosphate Ags by T cells. Presently, we made chain
pair switch, chimeric, and site mutant TCRs and transfected them
into TCR- mutant Jurkat T cells to examine the
effects of changing the TCR junctional region sequences on
reactivity to prenyl pyrophosphate Ags. Substitution of the TCR
junctional region (N and J) sequences from an Ag-reactive TCR with
TCR junctional region sequences from an Ag-nonreactive TCR abrogated
reactivity to the prenyl pyrophosphate Ag isopentenyl pyrophosphate and
to its synthetic analogue ethyl pyrophosphate but not to a
mycobacterial supernatant containing a mixture of prenyl pyrophosphate
Ags. Substitution of only the TCR N nucleotide region with that from
this Ag-nonreactive TCR destroyed reactivity to isopentenyl
pyrophosphate and to the mycobacterial supernatant. Substitution of the
entire V2 chain from the Ag-reactive TCR with a V1 chain from an
Ag-nonreactive TCR yielded a prenyl pyrophosphate Ag-nonreactive TCR.
Thus, using TCR mutagenesis and TCR transfectants, we show that
TCR reactivity to prenyl pyrophosphate Ags is dependent upon the
junctional region of the TCR chain and upon pairing of V2 and
V2 TCR chains. These structural requirements of TCR
recognition of prenyl pyrophosphates distinguish this reactivity from
that of protein superantigens and emphasize the importance of the
TCR CDR3 loop and adjacent residues.
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