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Tuesday, July 11, 2006 11:37:28 AM
"When I read the decision what I was struck with was the broadness and non-specificness of the patents. As this initial decision is just setting the ground rules, there are lot more twists and turns to come.
My initial impression was TRCA fared much better than INSM- which probably was the case. It appeared from the transcript that TRCA was better prepared than INSM. After having thought about this for most of the day (after being upset and down most of the day), I really feel that this initial decision was a non-event. The real trial is yet to come- nothing was settled here.
In reading the decision, it is quite apparent that the patents were broad as possible and I (not being a lawyer but a physician scientist) can already see many potential weaknesses with the position taken by TRCA. First, the patent for the production of IGF is as broad as can be- including usage of all prokaryotic host (not just E. coli). There are number of very broad application of the process that are mentioned throughout. There were some areas that the judge also had raised some issues for TRCA. The brief summary by Unterberg previously posted also provides some insight. SOme things that bother me about TRCA patent position are 1) the broadness of the patents in regards to production -they cover all prokaryotes (all bacterial hosts), 2) the broadness or nonspecific definition of IGF, fusion protein and etc..., 3) the method they described for IGF production is not unique or novel but a simple standard molecular methodology that is published in any first year college molecular biology textbook- it completely baffles me how this can be considered a patent but what do I know, 4) judge in this case just laid down the groundrules but did not entertain arguments as to why the patents are invalid- I personally see many potential targets for attack by INSM, 5) this case has just started- the trial in November is only the beginning- there will certainly be an appeal- I still believe INSM will prevail in November- I just don't think TRCA can defend the broadness of the patent- INSM will be able to pick and choose and put holes in TRCA defense.
Let's just hope the sales numbers look good and a breakthrough data for MMD od AIDS lipodystrophy data will be presented in the near future.
Good Luck to all longs and hope for better days to come. "
I finally had a chance to research this issue further. I believe the major concern for us all is whether the patent 414 that claims the method for IGF-1 production by TRCA is valid. The key question is "Is the method proposed in Patent 414 a novel method or novel invention for producing IGF-1" by DNA or TRCA. I am very relieved to say that the answer is a resounding "no". Following lies the evidence. I have searched the PUBMED and found over 10 prior publications which have used the identical method to produced IGF- that is utilizing the E.coli as the host and using recombinant DNA approach consisting of fusion protein and a plasmid vector. Following are six papers dating back as early as 1985: (I hope this makes your day). There is no way that TRCA can win the novel method patent- the key issue of this litigation.
1: Francis GL, Ross M, Ballard FJ, Milner SJ, Senn C, McNeil KA, Wallace JC,
King R, Wells JR.
Novel recombinant fusion protein analogues of insulin-like growth factor
(IGF)-I indicate the relative importance of IGF-binding protein and receptor
binding for enhanced biological potency.
J Mol Endocrinol. 1992 Jun;8(3):213-23.
PMID: 1378742 [PubMed - indexed for MEDLINE]
2: King R, Wells JR, Krieg P, Snoswell M, Brazier J, Bagley CJ, Wallace JC,
Ballard FJ, Ross M, Francis GL.
Production and characterization of recombinant insulin-like growth factor-I
(IGF-I) and potent analogues of IGF-I, with Gly or Arg substituted for Glu3,
following their expression in Escherichia coli as fusion proteins.
J Mol Endocrinol. 1992 Feb;8(1):29-41.
PMID: 1311930 [PubMed - indexed for MEDLINE]
3: Nilsson B, Forsberg G, Hartmanis M.
Expression and purification of recombinant insulin-like growth factors from
Escherichia coli.
Methods Enzymol. 1991;198:3-16. No abstract available.
PMID: 1857223 [PubMed - indexed for MEDLINE]
4: Hummel M, Herbst H, Stein H.
Gene synthesis, expression in Escherichia coli and purification of
immunoreactive human insulin-like growth factors I and II. Application of a
modified HPLC separation technique for hydrophobic proteins.
Eur J Biochem. 1989 Apr 1;180(3):555-61.
PMID: 2469575 [PubMed - indexed for MEDLINE]
5: Wong EY, Seetharam R, Kotts CE, Heeren RA, Klein BK, Braford SR, Mathis KJ,
Bishop BF, Siegel NR, Smith CE, et al.
Expression of secreted insulin-like growth factor-1 in Escherichia coli.
Gene. 1988 Sep 7;68(2):193-203.
PMID: 3065142 [PubMed - indexed for MEDLINE]
6: Moks T, Abrahmsen L, Holmgren E, Bilich M, Olsson A, Uhlen M, Pohl G, Sterky
C, Hultberg H, Josephson S, et al.
Expression of human insulin-like growth factor I in bacteria: use of optimized
gene fusion vectors to facilitate protein purification.
Biochemistry. 1987 Aug 25;26(17):5239-44.
PMID: 3676250 [PubMed - indexed for MEDLINE]
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