Appeal No. 2004-1736 Page 5
Application No. 09/243,008
cite the declaration of Dr. Brian Seed, which attests to the fact that the three
amino acids do not signal, but rather anchor the chimera into the cell membrane,
and that signaling is mediated by the transmembrane domain. Appellants
conclude that “[a]s [the] specification provides a working example of a chimeric
receptor that signals through a transmembrane (and not an intracellular) domain,
precisely as specified by the present amended claims, the specification and the
claims, prior to the present amendments, clearly included these features; no sub-
genus has been created.” Id. at 11.
The portion of the specification that appellants cite to states:
To identify the minimal ζ sequences necessary for cytolysis,
a series of deletion mutants were prepared in which successively
more of the ζ intracellular domain was removed from the carboxyl
terminus (Fig. 8A). Most of the intracellular domain of zeta could
be removed with little consequence for cytolytic potential; the full
length chimera CD16:ζ was essentially equal in efficiency to the
chimera deleted to residue 65, CD16:ζAsp66* (Fig. 8B). A
substantial decrease in cytotoxicity was observed on deletion to ζ
residue 59 (chimera CD16:ζGlu60*), and further deletion to residue
50 resulted in slightly less activity. However, complete loss of
activity was not observed even when the intracellular domain was
reduced to a three residue transmembrane anchor (Fig. 8B).
Specification, page 48, lines 20-33.
Appellants also rely on original claim 44 to support that it is the
transmembrane domain is capable of signaling target destruction. See Appeal
Brief, page 9. Original claim 44 recites:
A cell expressing a proteinaceous membrane-bound chimeric
receptor, said receptor comprising (a) an extracellular portion which
is capable of specifically recognizing and binding a target cell or a
target infective agent, and (b) a transmembrane portion derived
from a T cell receptor, a B cell receptor, or an Fc receptor which is
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