37. Glaxo argues that “it is possible that an antibody expressed by a CHO cell might
not be glycosylated” and “[t]herefore even if the antibody was expressed in a CHO cell, it does
not necessarily follow that the antibody would be glycosylated” (Paper 49 at 11-12 and Paper 51
at 21-22).
38. Cabilly argues that the Cabilly applications disclose antibodies expressed by CHO
cells and that the Cabilly applications disclose that those antibodies would be glycosylated
(Paper 106 at 5).
39. The examples provided by the Cabilly applications are directed to the expression
of antibodies by E.coli cells (Exh. 2103 at 30-53).
40. Evidence pointed out to us indicates that an E.coli cell will not ordinarily
glycosylate a protein it expresses (Exh. 2012 at ¶17).
41. The Cabilly applications indicate that a mammalian cell would be expected to
produce antibodies that are glycosylated. For example, the Cabilly applications state that:
Heavy chain from mammalian cells is expected to be slightly heavier than E.coli
material due to glycosylation in the former (Exh. 2103 and Exh. 2102 at
45:26-28)
and that
Third, both hybridomas and B cells inevitably produce certain antibodies in
glycosylated form (Melchers, F., Biochemistry, 10: 653 (1971)) which, under
some circumstances, may be undesirable (Exh. 2103 and Exh. 2102 at 4:18-21).
42. The only specific mention of CHO cells found in the Cabilly applications is as
follows (Exh. 2103 and Exh. 2102 at 18: 8-10):
Examples of such useful host cells [for expressing antibodies] are VERO and
HeLa cells, Chinese hamster ovary (CHO) cell lines, and WI38, BHK, COS-7 and
MDCK cell lines.
-13-
Page: Previous 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 Next
Last modified: November 3, 2007