Appeal No. 2001-1048
Application No. 08/121,105
sequences of a protein. See Answer, page 4. In addition, the examiner relies on
LaRosa (Answer, page 5) to “teach that the specificity of ligand binding to both IL -8
receptor subtypes is dictated by the heterogeneous NH2 terminal domain.”
From the these teachings the examiner concludes that (id.):
it would have been prima facie [sic] obvious to one of ordinary
skill in the art at the time of the invention to have incorporated
the interleukin 8 receptor 2 molecule as taught by Murphy and
to elicit a [sic] antibodies against the antigenically active
sequences as taught by Lee et al[.] and Geysen. One would
have be[en] motivated to elicit an antibody against these
regions in view that [sic] LaRosa sets forth that the specificity
of ligand binding to both IL-8 receptor subtypes is dictated by
the heterogeneous NH2 terminal domain.
The claimed invention requires, inter alia, that an antibody (1) compete with
IL8 for binding to IL8 receptor 2, and (2) interact with residues of a peptide of the
NH2 terminal extracellular domain of IL8 receptor 2. In this regard, appellants focus
our attention on LaRosa. Appellants explain (Brief, page 8) that LaRosa teaches
two IL8 receptors that bind “IL8 with similar affinity, but differed in their ability to bind
related ligands, MGSA/GRO and NAP-2.” These two receptors are (1) 4ab, now
known as IL8 receptor 2; and (2) F3R, the rabbit homologue of IL8 receptor 1.
According to LaRosa (page 25402, column 2) F3R and 4Ab both bind IL -8 with high
affinity, however, unlike F3R, 4AB IL-8 binding is competed by MGSA/GRO and
NAP-2. As relied upon by the examiner, LaRosa “demonstrate [by switching the
NH2-terminal domains of these two receptors] that the extracellular NH2-terminal
region of these receptor subtypes dictates the different ligand binding specificities.”
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