Dr Youles’ testimony regarding glycosylation:
43. In its preliminary motions 3 and 5, Glaxo points to the testimony of Dr. Richard J.
Youle (Exh. 2012) in support of its arguments regarding the insufficient written description in
the Cabilly applications, but directs us to no specific portion of the testimony.
44. In its reply to Cabilly’s opposition to its preliminary motion 3, Glaxo states that
the entire Youle declaration should be considered but that “since Cabilly suggests that GWI[6]
must point to particular paragraphs, GWI will point to ¶¶ 27, 28, 33-38 of Exhibit 2012 [Dr.
Youle’s declaration]” (Paper 154 at 7-8).
45. From our own review of Dr.Youle’s testimony, we note the following:
a) Dr. Youle testified that: “antibodies expressed by the E. coli cells described in the
Cabilly application[7 ] were not glycosylated, since it is well known that prokaryotic organisms,
such as E.coli and other bacteria, do not produce glycosylated antibodies” (Exh. 2012 at ¶17);
b) Dr. Youle testified that, “[s]ince Cabilly cautions that glycosylated antibodies can
be ‘undesirable’, I would be reluctant to attempt to use eukaryotic organisms to express
recombinant antibodies in order to avoid possible undesirable effects of glycosylation on
antibody production” (Exh. 2012 at ¶ 23);
c) Dr. Youle testified that, in CHO cells expressing antibodies, it would have been
possible to take steps to either inhibit glycosylation or to remove the sugar groups after
glycosylation (Exh. 2012 at ¶¶31-32) ; and
6 We understand “GWI” to be Glaxo.
7 Dr. Youle seems to be referring to the ‘457 application at this point in his
testimony but later in his testimony indicates that his conclusions regarding written description
also apply to the ‘419 application (Exh. 2012 at ¶¶33-34).
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