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, But Not Mouse CD8, Can Be Expressed in the Absence of CD8
as a Homodimer1
*
Department of Laboratory Medicine and Section of Immunobiology, and
Department of Genetics, Yale University School of Medicine, New Haven, CT 06520
The T cell coreceptor CD8 exists on mature T cells as
disulfide-linked homodimers of CD8
polypeptide chains and
heterodimers of CD8- and CD8
-chains. The function of the
CD8-chain for binding to MHC class I and associating with the
tyrosine kinase p56lck was demonstrated with
CD8 homodimers. CD8 functions as a better coreceptor, but
the actual function of CD8 is less clear. Addressing this issue has
been hampered by the apparent inability of CD8 to be expressed
without CD8. This study demonstrates that human, but not mouse,
CD8 can be expressed on the cell surface without CD8 in both
transfected COS-7 cells and murine lymphocytes. By creating chimeric
proteins, we show that the murine Ig domain of CD8 is responsible
for the lack of expression of murine CD8 dimers. In contrast to
CD8, CD8 is unable to bind MHC class I in a cell-cell
adhesion assay. Detection of this form of CD8 should facilitate studies
on the function of the CD8 -chain and indicates that caution should
be used when interpreting studies on CD8 function using chimeric
protein with the murine CD8 Ig domain. In addition, we
demonstrate that the Ig domains of CD8 are also involved in
controlling the ability of CD8 to be expressed. Mutation of B- and
F-strand cysteine residues in CD8 reduced the ability of the protein
to fold properly and, therefore, to be expressed.
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