Appeal No. 2004-1930 Page 9
Application No. 08/940,544
CD28 . . . cell surface receptors are employed joined to other than
their natural extracellular domain by a transmembrane domain.
Id. at Col. 5, lines 18-32 (emphasis added). Roberts also provides specific
examples of fusion proteins containing CD28 as the cytoplasmic domain. See
Roberts, Fig. 1A, and Col. 16, Example 1.
Roberts also teaches that “[i]n particular, the extracellular domain may
consist of monomeric or dimeric immunoglobulin (Ig) molecules or portions or
modifications thereof.” See Roberts, Col. 8, lines 47-50. Specifically, the patent
teaches that
[b]ecause association of both the heavy and light V domains are
required to generate a functional antigen binding site of high
affinity, in order to generate an Ig chimeric receptor with the
potential to bind antigen, a total of two molecules will typically need
to be introduced into the host cell. Therefore, an alternative and
preferred strategy is to introduce a single molecule bearing a
functional antigen binding site. This avoids the technical difficulties
that may attend the introduction and coordinated expression of
more than one gene construct into host cells. This “single-chain
antibody” (Sab) is created by fusing together the variable domains
of the heavy and light chains using an oligo- or polypeptide linker,
thereby reconstituting an antigen binding site on a single molecule.
Id. at Col. 9, lines 18-31. Thus, we find the disclosure of Roberts anticipates the
fusion protein encoded by the recombinant polynucleotide of claim 1.
Appellants reiterate their arguments with respect to Eshhar. See Appeal
Brief, page 8. In addition, appellants contend that while the
patent asserts that essentially anything with binding function can
serve as the extracellular binding domain, and mentions scFv as a
possibility. However, the patent provides no specific examples of
scFv-containing fusions nor any specific teaching of how to make
such fusions specifically. It also provides no evidence that such
fusions function as asserted, nor any relationship besides binding
function between scFv and the extracellular domains that are
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