T 0358/22 (HER2 Antibody Compositions/GENENTEC) 23-01-2025
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Composition comprising antibody that binds to domain II of HER2 and acidic variants thereof
Hexal AG
Dr. H. Ulrich Dörries
Pohlman, Sandra M.
Dr. Reddy's Laboratories Limited
Hoffmann Eitle
I. The patent proprietor (appellant) filed an appeal against the opposition division's decision to revoke European patent EP 2 238 172. The patent was opposed by five parties, opponents 1 to 5. Opponents 2 and 5 subsequently withdrew their oppositions and ceased to be a party to the proceedings.
II. In the appeal proceedings, opponents 1, 3 and 4 are respondents I, III and IV, respectively.
III. In its decision the opposition division held that the subject-matter of at least claim 1 of the main request lacked novelty over the disclosure in document D1
It further held that
- the main request met the requirements of Rule 80 EPC,
- the main request met the requirements of Article 123(2) EPC,
- that the invention was patentable under Article 52(1) EPC.
It also admitted documents D88, D92 and D93 to the proceedings.
Auxiliary request 1 was held admissible under Rule 80 EPC and was also held to meet the requirements of Article 84 EPC for clarity. Furthermore the claimed subject-matter of the auxiliary request was held to meet the requirements of Articles 123(2) and 123(3) EPC. However, the subject-matter of claim 1 was held to lack novelty over the disclosure in document D1 for the same reasons as claim 1 of the main request.
IV. The appellant submitted a statement of grounds of appeal together with document D96 and also re-submitted set of claims of a main request and an auxiliary request 1. The main request and auxiliary request 1 are the same as the main request and auxiliary request 1 that were dealt with by the opposition division in the decision under appeal.
V. Only respondents I and III filed replies to the patent proprietor's statement of grounds of appeal. Respondent IV made no substantive submissions in the appeal proceedings.
VI. The patent proprietor also filed a letter dated 11 May 2023 in which it replied to the respondents' submissions and summarised its submissions.
Claims
VII. Claim 1 of the main request reads:
"1. A pharmaceutical formulation comprising a composition comprising a main species HER2 antibody that comprises light chain and heavy chain amino acid sequences in SEQ ID NOs. 15 and 16 respectively and binds to domain II of HER2, and acidic variants of that main species antibody, in a pharmaceutically acceptable carrier, wherein the main species HER2 antibody is the antibody amino acid sequence structure in the composition which is the quantitatively predominant antibody molecule in the composition and the main species HER2 antibody and the acidic variants are all intact antibodies, wherein the acidic variants include a disulfide reduced variant, a non-reducible variant, glycated variant, deamidated variant, and sialylated variant".
Documents
VIII. The following documents are referred to in this decision.
D1: WO 2006/033700
D13: Hunt G. and Nashabeh W., 1999, "Capillary electrophoresis sodium dodecyl sulfate nongel sieving analysis of a therapeutic recombinant monoclonal antibody: A biotechnology perspective", Anal. Chem., 71(13), 2390-2397.
D95: Ma S. and Nashabeh W., 2001, "Analysis of protein therapeutics by capillary electrophoresis", Chromatographia Suppl., 53, S-75-S-89.
The bibliographic data for other documents mentioned by document number in this decision are not given here because these documents played no role in the board's considerations.
IX. Oral proceedings before the board were held as scheduled. The appellant and respondent I attended the hearing, while respondents III and IV had informed the board in writing what they would not attend.
X. The submissions of the appellant relevant to the decision under appeal are summarised as follows.
Main request - claim 1
Novelty (Article 54 EPC)
Document D1 did not disclose the claimed pharmaceutical formulation. In particular, it did not disclose a pharmaceutical formulation comprising a disulfide reduced variant of pertuzumab, either in the figures (especially Figure 11B) or in the description (when contemplating 'intact' antibodies). This meant that D1 did not disclose a pharmaceutical composition comprising a disulfide reduced variant of pertuzumab, or a composition comprising a disulfide reduced variant that is also an acidic variant. Already for this reason, the subject matter of claim 1 and all dependent claims was novel over the disclosure in document D1.
D1 description page 9
Respondent I had argued that the definition of 'intact' antibody at page 9 of D1 was an explicit, literal disclosure of a disulfide reduced variant consisting of one heavy chain and one light chain (HL or half antibody). However, this passage was not a disclosure of particular antibodies at all but merely a definition of what was to be understood by 'intact antibody'. It explained that intact antibodies were antibodies that comprised the constant domains as well as the variable domains. Similarly, the definition on page 9 of D1, which states that an 'intact' antibody comprises a heavy and a light chain, did not necessarily imply that it consisted solely of one heavy and one light chain.
D1 Figure 11B
Contrary to the respondents' arguments, Figure 11B of D1, a non-reduced CE-SDS electropherogram (non-reduced capillary electrophoresis-sodium dodecyl sulfate analysis), did not contain sufficient information for the skilled person to derive the presence of such a variant. Firstly, the skilled person would not have forensically examined Figure 11B in the way suggested. Instead, the skilled person would have relied on the conclusions expressed in D1 by the authors themselves. These had concluded that there was "no evidence of significant product fragments" (see page 48, bottom), which contradicted the respondents' interpretation that Figure 11B disclosed a disulfide reduced variant.
The small peak to the left of the main peak in Figure 11B, relied upon by the respondents, did not have the characteristic fingerprint of a disulfide reduced monoclonal antibody, as additional peaks expected for such a variant were absent.
The conclusion concerning the results in Fig. 11, made by of the authors of D1 themselves was that the pertuzumab samples did contain non-glycosylated heavy chain because there is a small bump to the left of the heavy chain peak which was labelled as such in Fig. 11A. Fig. 11B was an experiment designed to determine whether or not disulfide variants were present and the conclusion reached was that the pertuzumab samples did not contain such disulfide variants. The skilled person considering Figure 11A and the authors' conclusion that pertuzumab contains non-glycosylated heavy chains was therefore primed to regard the tiny bump to the left of the intact antibody peak in Figure 11B as attributable to non-glycosylated heavy chain.
The respondents argued that documents such as D13 supported the interpretation that the small peak in Figure 11B of D1 corresponded to a disulfide reduced variant. They contended that D13 showed that very small non-reduced CE-SDS analysis peaks could be attributed to the presence of disulfide reduced antibodies and therefore, a similar peak in D1 Figure 11B should be interpreted in the same way.
This was not correct. Firstly, D13, provided information not available to the skilled person reading D1 on its own. Any conclusion reached by interpreting D1 using D13 meant that the information was not directly and unambiguously disclosed in D1. The skilled person reading D1 in isolation would not have understood the additional peaks in Fig. 11B to be indicative of a disulfide reduced variant, as D1 itself stated there was "no evidence of significant product fragments".
Secondly, alternative explanations existed for the small peak in Figure 11B. Specifically, it could have been attributed to either:
- a non-glycosylated intact antibody, as Figure 11A of D1 confirmed the presence of non-glycosylated heavy chains in pertuzumab samples; or
- an artifact arising from the CE-SDS sample preparation process, which was known to induce disulfide reduction (as documented in D74, D13, and D15).
An explanation for the tiny bump in Figure 11B that would have come to the mind of the skilled reader was that it was attributable to a non-glycosylated intact antibody (LHHL - two heavy and two light chains).
Furthermore, the skilled person knew that non-reduced CE-SDS (the method used to generate Figure 11B of D1) was subject to artifact. The skilled person reading D1 would have considered the presence of an artifact as a plausible explanation for the results presented in Fig 11B.
Even if the small bump in Figure 11B of D1 had been considered significant enough to warrant serious contemplation by the skilled person, they had several equally plausible explanations for it. It might have been dismissed as attributable to a non-glycosylated intact antibody.
Inevitable result
The respondents has also argued that a pertuzumab formulation as defined in claim 1 was inevitably produced by the generic process disclosed in D1. This "inevitability" type of attack was based on the argument that all five of the claimed variants are always and unavoidably produced by the type of generic recombinant methods mentioned in D1 itself.
This argument was not correct because D1 only described generic cell culture methods for producing pertuzumab and did not provide details of specific culture conditions that would necessarily lead to the formation of a disulfide reduced variant.
Decision T 1990/18 confirmed this approach. It distinguished between a specific chemical reaction inevitably producing a particular product and a more general biological process where multiple outcomes were possible. In fact the production of disulfide reduced variants depended on specific factors such as scale of cell culture, time in harvested cell culture fluid, harvesting conditions, dissolved oxygen levels, and the presence of certain metal ions, none of which were disclosed in D1.
Furthermore, decision T 12/81, which established the concept of inevitability in prior art disclosures, related to a defined chemical reaction with specific reagents and conditions. Such reasoning was inappropriate in the context of recombinant protein production.
Remittal (Article 111(1) EPC and Article 11 RPBA)
If as requested, the board overturned the decision of the opposition division, then the case should be remitted to the opposition division for further prosecution based on the main request.
There were special reasons for remittal in the present circumstances, namely that the decision under appeal only dealt with the formal requirements of claim requests (Rule 80, Article 123(2) EPC) and novelty. The remaining substantive issues of sufficiency and inventive step were not discussed at all in the first instance proceedings.
XI. The respondents' arguments relevant to the decision are summarised as follows.
Main request - claim 1
Novelty (Article 54 EPC)
As correctly set out in the decision under appeal, the claimed pharmaceutical formulation lacked novelty over the disclosure in D1. In particular, it disclosed formulations comprising a disulfide reduced variant of pertuzumab for three main reasons:
1) document D1 contained an explicit disclosure of a half-antibody (one heavy and one light chain - HL) on page 9, lines 7 to 11. This paragraph read: "An 'intact antibody' is one which comprises an antigen-binding variable region as well as a light chain constant domain (CL) and heavy chain constant domains, CH1, CH2 and CH3. The constant domains may be native sequence constant domains (e.g. human native sequence constant domains) or amino acid sequence variants thereof. Preferably, the intact antibody has one or more effector functions, and comprises an oligosaccharide structure attached to one or two heavy chains thereof". This taught that a half-antibody (HL) was the minimum entity of an "intact" pertuzumab. The HL fragment was a disulfide reduced variant because the disulfide bridges between the two heavy chains were broken.
2) there was experimental data in D1 (Fig. 11B) confirming the presence of small amounts of 'intact' antibody variants (HHL, HL) in all recombinantly produced monoclonal Pertuzumab compositions analysed.
All electropherograms of Fig. 11B showed the commonly known characteristic fingerprint of these well-known size variants (HHL, HL etc.) that migrate in front of the 'native' (HHLL) antibody. D1 therefore directly and unambiguously disclosed that the recombinantly produced pertuzumab compositions comprised such size variants, including the prominently visible HHL fragment, which was a disulfide reduced variant. The original characteristic peak assignment consistent with common general knowledge (as evidenced in D13 or D95) matched that in Fig. 11B in D1 and confirmed that such variants were present in the disclosed compositions.
3) document D1 disclosed standard recombinant production methods for Pertuzumab using CHO cells. Disulfide reduced variants were inevitably formed during recombinant production. It was demonstrated by experimental data (e.g. in D92, D3, D26 to D28, D88) that disulfide reduced variants were inevitably formed in such conditions. No counter evidence had been provided by the appellant to challenge this technical fact. The spike-in data in the patent clearly demonstrated that disulfide reduced variants are formed in the chemical environment of the cell culture medium due to degradation events.
D92 was evidence that the majority of these disulfide reduced variants were formed during the incubation in standard cell culture medium, as demonstrated by the much smaller amount of these variants found in the starting material. Therefore, the experimental data of D92 provided clear and conclusive proof that disulfide reduced variants, especially the HHL variant, were automatically formed during incubation in standard cell culture medium as acidic variants.
The respondents had provided conclusive proof of lack of novelty. Since the Patentee failed to submit counter experiments refuting the inevitable formation of disulfide reduced variants, the burden of proof had shifted, and the claim could not be considered novel.
Remittal (Article 111(1) EPC and Article 11 RPBA)
There were compelling reasons not to remit the case to the opposition division for further prosecution, should the board, despite the arguments and evidence presented by the respondents, arrive at the conclusion that either the subject-matter of the main request or the auxiliary request met the requirements of Article 54 EPC. This was because it was evident that the requirements of Article 56 EPC were not met in view of the same technical facts and considerations that had been carefully worked-up by the opposition division and discussed by the parties in conjunction with the novelty assessment. The appellant should not benefit from the fact that the question of inventive step had not arisen at the oral proceedings before the opposition division because of a finding of lack of novelty. The same considerations applied to objections raised by the respondents under Article 83 EPC. Moreover, the remaining objections in the case could be dealt with without undue burden for either the board or the parties. Finally, other considerations such as the patent term spoke against remittal,
Requests
XII. The appellant requested that the decision under appeal be set aside and the case be remitted to the opposition division for discussion of the remaining requirements of the EPC based on the claims of the main request, as submitted with the statement of grounds of appeal.
Alternatively, the case be should remitted to the opposition division based on the set of claims of auxiliary request 1, as submitted with the statement of grounds of appeal. Further alternatively the appellant requested that the patent be maintained on the basis of the claims of the main request or auxiliary request 1.
The appellant further requested that document D96 be admitted into the proceedings.
XIII. Respondent I requested that the appeal be dismissed and that the case not be remitted to the opposition division for further prosecution but that the board itself decide on the further grounds of opposition under Article 100(a) EPC in conjunction with Article 56 EPC and Article 100(b) EPC, should it come to the conclusion that either the main request or auxiliary request 1 met the requirements of Article 123 (2) EPC and Article 54 EPC.
XIV. Respondent III requested in writing that the appeal be dismissed.
XV. Respondent IV made no requests in the appeal proceedings.
Oral proceedings in the absence of a party duly summoned (Rule 115(2) EPC)
1. Respondents III and IV had indicated that they would not be attending the oral proceedings, which were held in their absence. Respondent III was treated as relying only on its written case (Rule 15(3) RPBA).
Main request - claim 1
Novelty (Article 54 EPC)
2. The claim is directed to a pharmaceutical formulation defined by the presence of a "main species" HER2 antibody that comprises the light chain and heavy chain amino acid sequences in SEQ ID NOs. 15 and 16, respectively and binds to domain II of HER2 and also a number of acidic variants, which are stated to be "intact antibodies" and include "a disulfide reduced variant, a non-reducible variant, glycated variant, deamidated variant, and sialylated variant".
3. According to the paragraph [0025] of the patent, the expression "main species antibody" "refers to the antibody amino acid sequence structure in a composition which is the quantitatively predominant antibody molecule in the composition. The main species antibody is one comprising the light chain and heavy chain amino acid sequences in SEQ ID Nos. 15 and 16 (pertuzumab)".
4. In the decision under appeal, the opposition division held that the disclosure in document D1 anticipated the claimed subject-matter because it disclosed:
a) a process for the preparation of pertuzumab, involving the culture in batch of recombinant CHO cells;
b) that a pertuzumab preparation according to D1 contained not only unmodified pertuzumab, but also a number of charged variants;
c) among these, sialylated, glycated, deaminated, disulfide reduced and nonreducible variants
could be directly and unambiguously identified in the antibody preparations disclosed. The aforementioned variants were acidic and the antibody preparation was suitable for medical use.
5. It is noted that document D1 can only anticipate the claimed subject-matter if it discloses, directly and unambiguously, either explicitly or implicitly, a pharmaceutical formulation containing all of the acidic variants recited in claim 1 of the main request. In this decision, the board will focus on whether or not document D1 discloses a pertuzumab preparation comprising disulfide reduced variants.
6. The figure below, taken from respondent I's reply to the statement of grounds of appeal, illustrates the different disulfide reduced IgG1 variants that can be identified based on non-reduced capillary electrophoresis with sodium dodecyl sulfate (non-reduced CE-SDS) analysis by indicating (1) the reduced disulfide bond, and (2) the resulting fragments. H stands for heavy chain, L stands for light chain.
FORMULA/TABLE/GRAPHIC
7. According to the decision under appeal, disulfide reduced variants of pertuzumab are directly and unambiguously disclosed in D1. In particular, the HHL variant was disclosed: "it is apparent that the small peak to the left of the main antibody peak [in Fig. 11B of D1] corresponds to the HHL disulfide reduced variants present in the pertuzumab composition of D1" (point 5.40).
8. The respondents agreed with the opposition division's conclusion and put forward three main lines of argument as to why document D1 discloses compositions comprising disulfide reduced variants (see point XI. above).
9. The first was that disulfide reduced variants are directly disclosed on page 9, in the paragraph defining an intact antibody. In the respondents' view, the fact that this paragraph mentions that an intact antibody can be a 'half-antibody', i.e. one in which the interchain disulfide bridges are not correctly formed but instead are reduced, is a direct disclosure that the monoclonal pertuzumab composition may comprise a disulfide reduced pertuzumab variant.
10. The board is not persuaded by this argument because the paragraph in question is not a disclosure of a particular composition comprising a 'half-antibody' disulfide reduced variant, but is merely a definition of an "intact antibody" for the purposes of D1. The paragraph cannot in itself be seen as a disclosure of any composition and in particular not one as defined in the claim.
11. The second line of argument put forward by the respondents was that disulfide reduced variants were detected in all pertuzumab compositions that were characterized in the examples of D1, using the same analytical assay that is used in the patent in suit for detecting disulfide reduced variants based on their difference in size, i.e. non-reduced CE-SDS. In particular in Fig. 11B there were several small peaks in front of the native antibody, including a considerable peak that migrates at the characteristic position of the HHL fragment. The variously sized variants that are formed because the reduction of interchain disulfide bridges resulted in a characteristic "fingerprint" in non-reduced CE-SDS are shown in textbook D95 (Fig. 7a) and also in D13 (Fig 1).
Fig. 11B is reproduced here:
FORMULA/TABLE/GRAPHIC
12. The board is not persuaded that document D1 directly and unambiguously discloses compositions containing disulfide reduced pertuzumab variants. The reasons for this are as follows. Firstly, it is established case law that in the assessment of legal issues in the context of novelty, in particular in the context of whether the skilled person would have derived a specific piece of information from a document, it is determined whether or not that document provides a direct and unambiguous disclosure of that information, including any features implicit to a person skilled in the art (see Case Law of the Boards of Appeal of the European Patent Office, 10th edition 2022, in the following "Case Law", I.C.4.1 and also T 1708/18, point 21). In this context, an alleged disclosure can only be considered "implicit" if it is immediately apparent to the skilled person that nothing other than the alleged implicit feature forms part of the subject-matter disclosed (see Case Law I.C.4.3).
13. Turning to the disclosure in document D1 itself, it is noted that nowhere in the document is there a verbatim disclosure of disulfide reduced variants, in particular there is no verbatim disclosure of compositions comprising the HHL antibody fragment. The capillary electrophoresis-sodium dodecyl sulfate with laser-induced fluorescence (CE-SDS-LIF) analysis of pertuzumab samples is described starting on page 48 of D1. Reference is made to electropherograms of process development material with and without reduction (Figs. 11A and 11B) and the only explicit conclusion made is that "No evidence of significant product fragments or other impurities were found in the CE-SDS-LIF analysis of these samples". The skilled person reading this could not conclude that the samples analysed contained the HHL fragment or any other disulfide reduced variant.
14. For the same reason, the concept of implicit disclosure referred to above, is also not met. As recalled by the appellant (referring to T 1239/20, Reasons 2.2;
T 572/21, Reasons 2.1; T 982/20, Reasons 3.4), there can be no implicit disclosure of a feature as long as there is another technically realistic way of interpreting a prior art document. The skilled person, on account of the express disclosure in D1, would have alternative technical explanations in mind for the small peak in Fig. 11B, which could have been attributed to a non-glycosylated intact antibody in view of Fig. 11A, or to an artifact arising from the CE-SDS sample preparation process.
15. The line of argument based on the premise that the skilled person would have compared the electropherogram in Fig. 11B with the commonly known characteristic fingerprint of antibody electropherograms such as those known from documents D13 and D95, and thus realised that D1 unambiguously disclosed recombinantly produced pertuzumab compositions comprising size variants, including the HHL fragment (a disulfide reduced variant), is not convincing either for the following reasons.
16. This line of argument is based on the assumption that D95 and D13 represent common general knowledge of the skilled person. However, this is not the case for the following reasons.
17. D95, published in 2001, is not part of the state of the art for the patent. The skilled person could not have referred to it.
18. Regarding D13, which is part of the state of the art for the patent, the respondents suggest that Fig. 1 shows a characteristic "fingerprint" of a CE-SDS-NGS (Capillary Electrophoresis Sodium Dodecyl Sulfate Nongel Sieving) analysis of non-reduced and reduced preparations of a therapeutic recombinant monoclonal antibody.
Figure 1 of D13 is shown below:
FORMULA/TABLE/GRAPHIC
19. Firstly, D13 itself does not refer to the electropherogram in Fig. 1 as a characteristic "fingerprint" nor suggest it as a standard for comparison. Thus, the board is not persuaded that the pattern shown in Fig. 1 of D13 represents a "fingerprint" that was common general knowledge for the skilled person at the relevant date.
20. Secondly, given that Fig. 11B of D1 essentially only shows a single clearly identifiable peak before the main peak, in contrast to clearly visible secondary peaks in Fig. 1 of D13, it takes rather stretch of the imagination to conclude from this that the skilled person would in Fig. 11B of D1, have immediately recognised the "fingerprint" of Fig. 1 of D13 and drawn conclusions from this.
21. Thirdly, if the skilled person reading D1 has, without any pointers, to consult a second document and in that document refer to a particular Figure (here Fig. 1), again without any pointers, and subsequently has to draw different or additional conclusions about the meaning of a figure in D1, which are not disclosed in D1 itself, this is far from a direct and unambiguous disclosure in D1 and cannot persuade the board that the claimed subject-matter is anticipated by the disclosure in D1.
22. In view of these considerations, the board concludes that Fig. 11B of D1 does not directly and unambiguously disclose a pertuzumab preparation comprising disulfide reduced variants.
23. The final argument put forward by the respondents was that D1 disclosed standard recombinant production methods for Pertuzumab using CHO cells which, when carried out, inevitably lead to compositions containing disulfide reduced variants. In their view, it was consistently demonstrated by experimental data (e.g. in D92, D3, D26 to D28, D88) that disulfide reduced variants were inevitably formed in such conditions. The respondents, having shown that it is more likely than not that disulfide reduced variants are inevitably formed during recombinant production, thus discharged their burden of proof. The allegation is that D1 discloses methods which inevitably lead to a particular product and that this particular product is covered by the claim, i.e. a pertuzumab composition comprising a disulfide reduced variant.
24. It is an established principle in the jurisprudence of the Boards of Appeal that, in the field of chemistry, a product is considered to be disclosed even if it is not cited expressis verbis in a prior art document, if it is the inevitable but undetected result of a process properly defined in the prior art document as to its starting substance and reaction conditions (see
T 12/81, Headnote 1). It is essential in this context that the process, from which the inevitable product should be disclosed, be adequately and credibly described in the prior publication.
25. As regards the applicable standard of proof, the appellant invoked the application of the higher standard of proof beyond reasonable doubt, justified by the inevitability of the facts to be proved, given that the claimed product is not disclosed in the text of the prior art document. The respondents while agreeing on the beyond reasonable doubt standard, at the same time referred to T 1708/18 (Headnote 2) and the balance of probabilities standard indicated for examination of factual issues in the context of novelty. The present board concurs with the view that the practical relevance of the distinction between the two standards is often overestimated (see e.g. T 768/20, Reasons 2.1.2 ) and that both standards are only fulfilled if the deciding body is persuaded that the alleged fact is true, which is not a matter of "just tipping the balance slightly" (see T 545/08, Reasons 8 and
T 1634/17, Reasons 19). In the present circumstances the board is not persuaded that in view of D1 and supplementary experimental evidence provided by the respondents, a pertuzumab composition comprising a disulfide reduced variant is an unavoidable outcome of the expressed disclosure in D1, rather the board finds that there still remains a "grey area" (see T 793/93, Reasons 2.1).
26. The "inevitability" argument, put forward by the respondents, fails under the present circumstances because D1 only discloses production methods in very general terms (see pages 21 to 27), but it does not disclose individualised production methods in a way that could support an allegation that a clearly defined, specific product is inevitably obtained. An argument that such a product would inherently meet the requirements of the claim, for example in that it must comprise disulfide reduced variants, could only succeed if the prior art disclosed a clearly defined process, but that is not the case here. For this reason, since individualised process conditions (such as cell culture and antibody harvesting conditions) are not given in D1, it is not inevitable that a pertuzumab composition comprising a disulfide reduced variant is the result of carrying out the instructions of D1. Accordingly, due to the lack of individualised process conditions in D1 it cannot be said that the experimental data provided by the respondents (e.g. in D92, D3, D26 to D28, D88) exactly correspond to the conditions used to make the pertuzumab compositions in D1.
27. In view of the above considerations, the board concludes that document D1 does not disclose a pharmaceutical formulation as claimed.
Admittance of D96
28. The board admitted document D96 into the proceedings, however a reference to this document was not necessary for the present decision. In view of this no reason needs be given for its admittance.
Remittal (Article 111(1) EPC and Article 11 RPBA)
29. The decision under appeal dealt with objections of lack of novelty under Article 100(a) EPC in combination with Article 54 EPC and objections of lack of novelty against the auxiliary request under Article 54 EPC.
However, it did not deal with objections of lack of inventive step (Article 100(a) EPC and Article 56 EPC) or lack of sufficient disclosure (Article 100(b) EPC). The board does not disregard the respondent I's considerations, with respect to the patent term and the extensive discussion on novelty, however it is also not convinced by the argument that the inventive step assessment would follow straightforwardly from the analysis made for the question of novelty. Thus, considering that under Article 12(2) RPBA, the primary object of the appeal proceedings is to review the decision under appeal in a judicial manner, the board considers that the circumstances of the case represent "special reasons" within the meaning of Article 11 RPBA for remittal.
For these reasons it is decided that:
1. The decision under appeal is set aside.
2. The case is remitted to the opposition division for further prosecution.