Amgen Inc. v. F. Hoffmann-LaRoche LTD et al

Filing 752

MOTION for Leave to File Reply in Further Support of Defendants' Motion for Summary Judgment that Claim 1 of U.S. Patent No. 5,995,422 is Invalid for Indefiniteness and Lack of Written Description and Defendants' Opposition to Amgen's Alternative Motion to Strike by F. Hoffmann-LaRoche LTD, Roche Diagnostics GmbH, Hoffmann LaRoche Inc.. (Attachments: #1 Exhibit Proposed Reply in Further Support of Defendants' Motion for Summary Judgment that Claim 1 of U.S. Patent No. 5,995,422 is Invalid for Indefiniteness and Lack of Written Description and Defendants' Opposition to Amgen's Alternative Motion to Strike#2 Exhibit Decl. of Jennifer Moore in Support of Proposed Reply in Further Support of Defendants' Motion for SJ that Claim 1 of the '422 Patent is Invalid for Indefiniteness and Lack of Written Description and Defendants' Opp. to Amgen's Alternative Motion to Strike#3 Exhibit A to Declaration of Jennifer Moore#4 Exhibit B to Declaration of Jennifer Moore#5 Exhibit C to Declaration of Jennifer Moore#6 Exhibit D to Declaration of Jennifer Moore#7 Exhibit E to Declaration of Jennifer Moore#8 Exhibit F to Declaration of Jennifer Moore#9 Exhibit G to Declaration of Jennifer Moore)(Toms, Keith)

Case 1:05-cv-12237-WGY

Document 752-9

Filed 07/16/2007

EXH Page 1 of 3 IBIT

F

IN THE UNITED STATES DISTRICT COURT FOR THE DISTRICT OF MASSACHUSETTS
AMGEN, INC.,
Plaintiff,
v.

Civil Action No. 05-cv-12237 WGY

F. HOFFMANN-LA ROCHE, LTD., ROCHE DIAGNOSTICS GMBH, and HOFFMANN-LA ROCHE, INC.
Defendants.

CONTAINS RESTRICTED ACCESS BLAIIND CONFIDENTIAL INFORMATION

SUBJECT TO PROTECTIVE ORDER

NON-INFRINGEMENT EXPERT REPORT OF RICHARD A. FLA VELL, PH.D.

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134. In addition, host cells of

the asserted process claims all specify the use of

"mammalian

host cells" or "vertebrate cells" for the production of a "glycosylated erythropoietin polypeptide"

or "erythropoietin." It is possible to use non-mammalian, non-vertebrate host cells to produce
the products of

the claimed process, however. For example, Hamilton et ai. describe the creation

of yeast cells that express and secrete glycoproteins having human-like glycosylation patterns. J7

Thcse yeast cells could be transformed or transfected with a DNA sequence encoding human
erythropoietin to produce a glycosylated erythropoietin polypeptide according to the claims.

Importantly, these cells were capable of expressing and secreting a polypeptide with terminal
sialic acids intact.176 In fact, using human erythropoietin as an example of "heavily glycosylated

175 Hamilton, S.R., et al. (2006) Science, 313: 144 i -43.
176id. The authors refer to this last step as the "the most complex step of

human N-glycosylation."

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protein," the authors showed that biologically active human erythropoietin could be expressed in

17 These results demonstrate commercial viability because the work was done with
yeast cells.

several authors affiliated with Glyco-Fi, Inc. a biotechnology company now a wholly-owned

subsidiary of Merck. Because yeast cells are neither vertebrate nor mammalian and, the
limitations of the claimed process would not be met and would not infringe.

17 I d.

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