Appeal 2007-1161
Application 09/954,166
2. T-cell receptors are normally comprised of two transmembrane proteins
(e.g., α and β subunits) which form a heterodimer (Specification 4, 8, and
Fig. 1A).
Matsui
3. Matsui describes soluble forms of MHC/protein complexes and T-cell
receptor heterodimers (Matsui, p. 12862, col. 1; Answer 4) which lack the
transmembrane domains responsible for anchoring them to the cell
membrane.
4. The soluble TCR heterodimers bind to soluble peptide/MHC complexes
in a cell free system (Matsui, p. 12862, col. 1).
5. The binding characteristics of soluble TCR heterodimers have been
difficult to study because of their relatively low affinity for the peptide/MHC
complex (Matsui, p. 12862, cols. 1-2; Answer 4).
6. To address this problem, Matsui uses an instrument for detecting protein-
protein interactions in which specific binding between the soluble TCR
heterodimer and peptide/MHC complex is detected by an optical
phenomenon known as surface plasmon resonance (Matsui, p. 12862, col.
2).
Dal Porto
7. According to Dal Porto, “[s]oluble class I MHC-like molecules have been
used to study T-cell responses” (Dal Porto, p. 6671, col. 2).
8. “Previously, soluble monovalent class I molecules have not effectively
inhibited T-cell responses in vitro or in vivo” (Dal Porto, p. 6671, col. 2).
9. Dal Porto describes the production of a genetically engineered divalent
class I MHC molecule which effectively inhibited lysis of target cells by T-
4
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