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J. Exp. Med.,
Volume 189, Number 8, April 19, 1999 1265-1274
By
From the Department of Molecular and Cellular Biology, Harvard University, Cambridge,
Massachusetts 02138
Molecular interactions with the extracellular domains of class I major histocompatibility complex proteins are major determinants of immune recognition that have been extensively studied
both physically and biochemically. However, no immunological function has yet been placed
on the transmembrane or cytoplasmic amino acid sequences of these proteins despite strict conservation of unique features within each class I major histocompatibility complex locus. Here
we report that lysis by a subset of natural killer (NK) cells inhibited by target cell expression
of human histocompatibility leukocyte antigen (HLA)-Cw6 or -Cw7 was not inhibited by expression of chimeric proteins consisting of the extracellular domains of HLA-C and the
COOH-terminal portion of HLA-G. Assays using transfectants expressing a variety of HLA-Cw6 mutants identified the transmembrane sequence and, in particular, cysteine at position
309 as necessary for inhibition of 68% (25/37) of NK cell lines and 23% (33/145) of NK clones
tested. Moreover, these NK clones inhibited by target cell expression of HLA-Cw6 and dependent upon the transmembrane sequence were found not to express or to only dimly express
NK inhibitory receptors (NKIR1) that are EB6/HP3E4-positive. Furthermore, assays using
monoclonal antibody blocking suggest that an NK receptor other than NKIR1 or CD94 is responsible for recognition dependent upon the transmembrane sequence of HLA-Cw6.
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