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J. Exp. Med.,
Volume 187, Number 3, February 2, 1998 319-327
By
From the * Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York 10029; the Superantigens are defined as proteins that activate a large number of T cells through interaction
with the V Howard Hughes Medical Institute, The Rockefeller University, New York 10021; the § Howard
Hughes Medical Institute, Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York
10029; and the Immunology Program, Graduate School of Medical Sciences, and the Department of
Medicine, Cornell University Medical College, New York 10021
region of the T cell antigen receptor (TCR). Here we demonstrate that the superantigen produced by Mycoplasma arthritidis (MAM), unlike six bacterial superantigens tested, interacts not only with the V region but also with the CDR3 (third complementarity-determining region) of TCR-. Although MAM shares typical features with other superantigens, direct interaction with CDR3- is a feature of nominal peptide antigens situated in the antigen
groove of major histocompatibility complex (MHC) molecules rather than superantigens. During peptide recognition, V and V
domains of the TCR form contacts with MHC and the
complex is stabilized by CDR3-peptide interactions. Similarly, recognition of MAM is V-dependent and is apparently stabilized by direct contacts with the CDR3- region. Thus,
MAM represents a new type of ligand for TCR, distinct from both conventional peptide antigens and other known superantigens.
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