Dr. Youle’s testimony:
In its preliminary motions 3 and 5, Glaxo does not point us to any particular portion of
Dr. Youle’s testimony. Accordingly, as noted above, we do not find Glaxo’s arguments that rely
upon Dr. Youle’s testimony to be persuasive. At any rate, when we review Dr. Youle’s
testimony, we do not find that it shows that the Cabilly applications fail to provide written
description for antibodies that are glycosylated by CHO cells.
At the outset we wish to note that it is not clear to us from Glaxo’s arguments if it is
Glaxo’s position that a CHO cell would not be expected to glycosylate an antibody it expresses.
For example, on the one hand, Glaxo states that “[a]s clearly documented in Youle Declaration 1
[Exhibit 2012], glycosylation of antibodies by CHO cells is not inherent” (Paper 51 at 14). On
the other hand, Glaxo states that “[it] is possible to control and inhibit the glycosylation of an
antibody expressed by a CHO cell” (Paper 49 at 11-12), “even if a CHO cell usually inherently
expresses a glycosylated antibody, the glycosylation could be removed before attempting to use
the antibody for treatment”, and that “GWI does not dispute that the antibody of Cabilly’s
claims 56-60 could have been glycosylated, [since] [t]he claims recite an antibody expressed by
CHO cells” (Paper 156 at 5- 6). Dr. Youle’s testimony does not help us clarify Glaxo’s position.
Dr. Youle testified that, in view of Cabilly’s statement that glycosylation can be
“undesirable”, he “would be reluctant to attempt to use eukaryotic organisms [such as CHO
cells] to express recombinant antibodies in order to avoid possible undesirable effects of
glycosylation on antibody production” (FF 51). Moreover, 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 (FF 51). Thus, a portion of Dr. Youle’s testimony
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