DETAILED ACTION
This Office Action is in response to Applicant’s Amendment and Remarks filed on 30 July 2026 in which claims 19 and 25 were amended to change the scope and breadth of the claims.
Claims 19-36 are pending in the current application. Claims 33-36 remain withdrawn as being drawn to a non-elected invention. Claims 19-32 are examined on the merits herein.
The Declaration of Dr. Emeline Richard, submitted by Applicant on 27 March 2026 under 37 CFR §1.132 are acknowledged and will be further discussed below.
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Withdrawn Objections & Rejections
Applicant’s amendment, filed 30 July 2026, with respect to the objection to the Drawings, has been fully considered and is persuasive because the Specification has been amended to clearly describe each reference character. The objection is hereby withdrawn.
Applicant’s amendment, filed 30 July 2026, with respect to the objection of claims 19-32 for minor informalities, has been fully considered and is persuasive because the claims have been amended as suggested. The objection is hereby withdrawn.
Applicant’s amendment, filed 30 July 2026, with respect to the rejection of claim 25 under 35 U.S.C. § 112, second paragraph, for indefiniteness, has been fully considered and is persuasive because the claim has been amended to be an independent claim. The claim as amended more specifically claims the subject matter disclosed and supported in Applicant’s Specification. The rejection is hereby withdrawn.
Allowable Subject Matter
Claim 25 is allowed. There is no prior art reference teaching the claimed compound. Furthermore, it is non-obvious over Samain et al. (of record), because the results presented in Table 3 of the Specification demonstrate the claimed compound is significantly and unexpectedly better at binding to hemagglutinin for inhibiting influenza than the closest prior art compound ER84.
New Rejections
The following are new ground(s) or modified rejections necessitated by Applicant's amendment, filed on 30 July 2026, where the limitations in pending claim 19, the independent claim, as amended now have been changed. Therefore, rejections from the previous Office Action, dated 20 May 2026, have been modified and are listed below.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 19, 23, 24 and 26-32 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
The recitation “wherein at least one galactose is linked at one of the extremities of the main chain” in claim 19 (emphasis added) lacks antecedent basis. This limitation renders the claim and dependent claims 23, 24, 26-32 herein indefinite.
According to the Specification “R1 is composed of a chain of one or more monosaccharides that are linked in a row, which defines the “main chain” of R1” (see p.8-9, bridging para).
Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
Since the sialoside of Formula (I) could arguably describe “[GlcNAcβ1-4]n-GlcNAc” as a main chain, it is unclear what main chain is referenced in the recitation “wherein at least one galactose is linked at one of the extremities of the main chain”.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 22 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
The recitation “wherein in R1, the one or more galactose is(are) linked at one of the extremities of the main chain of the glycan structure” fails to further limit the subject matter of the claim upon which it depends, because this limitation is already recited in independent claim 19.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Response to Arguments
Applicant's arguments filed 30 July 2026 with respect to the rejections under 35 U.S.C. §103, have been fully considered but they are not persuasive.
Applicant has pointed to the Specification, Examples 7-13, Table 3, and the Declaration of Dr. Richard filed 27 March 2026 as evidence “the compounds of the invention advantageously enable the inhibition of hemagglutination and possess remarkable therapeutic properties”. Applicant has pointed to multiple data points showing ER15, ER101 and ER100 have significantly higher activity than ER84, which represents the closest prior art compound. Applicant has also pointed to J. Yan et al. (Chin. J. Chem., 2023, cited in IDS submitted 30 July 2026).
The above arguments are not found persuasive, because the results are not commensurate in scope with the present claims. See MPEP 716.02(d) “Whether the unexpected results are the result of unexpectedly improved results or a property not taught by the prior art, the "objective evidence of nonobviousness must be commensurate in scope with the claims which the evidence is offered to support." In other words, the showing of unexpected results must be reviewed to see if the results occur over the entire claimed range.”. Also see MPEP 716.02(d)(I), “The nonobviousness of a broader claimed range can be supported by evidence based on unexpected results from testing a narrower range if one of ordinary skill in the art would be able to determine a trend in the exemplified data which would allow the artisan to reasonably extend the probative value thereof.”.
Yan et al. teach “Among 10 α2,6-sialylated chitooligosaccharides 19-26, 35 and 36, generally, the inhibition rate increases with increased chain length. The inhibition rate decreased with elongated LacNAc unit, as sialylated chitooligosaccharides 19-23 with one LacNAc unit showed better inhibition rate than the corresponding sialylated chitooligosaccharides 24-26, 35 and 36 with two LacNAc units…Compared to ribavirin, all obtained oligosaccharides containing single sialic acid unit displayed lower inhabitation rate to influenza virus (0-40.1% vs 98.3%) due to lack of the cluster glycoside effect (glycoconjugates typically and strongly combine to target proteins through their high-density sugar units). These results indicate that both sialic acid linkage and the glycan chain length play essential roles in the recognition and binding with vir09 influenza virus”.
The compound of claim 19 is drawn towards where R1 is a glycan structure comprising one or more galactose (Gal), wherein at least one galactose is linked at one of the extremities of the main chain” allows for a structure of any length, with any saccharide present, provided there is “at least one galactose linked at one of the extremities of the main chain”.
However, Yan et al. demonstrate any significant difference in HA binding between α-2,6 and α-2,3 disappears between compounds 24 and 24 versus compounds 32 and 33. Furthermore, there is no data showing compounds where R1 is larger than 3 monosaccharides in length, comprising anything other than galactose and LacNAc are effective in binding HA, let alone significantly better than the prior art compound. The compounds prepared having binding to HA, only contain galactose, or LacNAc moieties for R1.
Furthermore, there isn’t any data for compounds where n=5-8.
Thus, the claims are not commensurate in scope with the data, and there is insufficient evidence to ascertain a trend in the data for the claimed ranges. The rejections are hereby maintained.
Maintained Rejections
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 19-24 are rejected under 35 U.S.C. 103 as being unpatentable over Samain (US Patent No. 8,507,227, cited in previous Office Action).
Samain teaches a sialylated tetrasaccharide: Neu5Acα-3Galβ-4GlcNAcβGlcNAc (col.3:12-20). Samain also teach a heptasaccharide prepared by sialylating a chitooligosaccharide: Neu5Ac-3Galβ-4[GlcNAcβ-4]4GlcNAc (col.20:9-24). The sialylated tetrasaccharide and heptasaccharide are positional isomers of the present compound of Formula (I), with the differences highlighted in bold. While the tetra-/hepta-saccharide contain a terminal 2,3-linked Neu5Ac, the present claims contain a terminal 2,6-linked Neu5Ac. Samain et al. teach an α-2,6-sialyltransferase could be used instead of α-2,3-sialyltransferase (col.7:28-38; also see claim 16).
Samain teaches “N-acetylneuraminic acid (Neu5Ac) is the most common member of the sialic acid family of aminosugars. Neu5Ac is frequently found as a terminal sugar in cell surface complex carbohydrates and plays a major role in many biological processes such as cellular adhesion and binding of toxins and virus (Varki, 1993)” (col.1:21-29).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the terminal Neu5Ac-2,3-linkage with Neu5Ac-2,6-, because they are positional isomers of each other, and Samain et al. expressly teach α-2,6-sialyltransferase could be used instead of α-2,3-sialyltransferase in the design and synthesis of the sialylated oligosaccharides. Thus, one having ordinary skill in the art would have had a reasonable expectation of success in making the positional isomer.
See MPEP 2144.09(II), “Compounds which are position isomers (compounds having the same radicals in physically different positions on the same nucleus) or homologs (compounds differing regularly by the successive addition of the same chemical group, e.g., by -CH2- groups) are generally of sufficiently close structural similarity that there is a presumed expectation that such compounds possess similar properties.”.
Thus, the claimed invention as a whole is prima facie obvious over the combined teaching of the prior art.
Claim(s) 26, 27 and 30-32 are rejected under 35 U.S.C. 103 as being unpatentable over Samain et al. (US Patent No. 8,507,227, cited in previous Office Action) as applied to claims 19-24 above, and further in view of Sasisekharan et al. (US Patent No. 8,815,522, cited in previous Office Action).
Samain et al. teach as discussed above.
Samain et al. do not expressly disclose multivalent sialoside (present claim 26).
Sasisekharan et al. teach the preparation of glycans that bind to influenza hemagglutinin (HA), including multivalent structures (col.1:1-49; col.68:18-34; fig. 18; col.61:47-48). Glycan structures include Neu5Acα2-6-Sug1-Sug2-Sug3 (claim 16). Sasisekharan et al. teach the glycan structures can be fixed to a support, e.g. agarose beads (col.37:48-50; col. 38:41). Dosage forms include inhalants (col.51:11-15; col.52:43-46). Sasisekharan et al. teach “the present invention encompasses the recognition that high affinity binding to long α2-6 glycans, which are extensively expressed in the upper respiratory tissues, is a determinant not only for HA human adaptation, but also for influenza virus transmission in general” (col. 73:24-28).
According to Sasisekharan et al., avian hemagglutinin (HA), H5 HAs show the most diverse binding to Neu5Ac-α-2,3 linkages including sulfated and fucosylated α2-3 (col.61:29-52). The human adapted H1 and H3 HAs bind to long α2-6. Wild type and mutant H5N1 Has is, however, not supported by long α2-6, although it is supported by both α2-3 and short α2-6 classifiers. Figure 15 of Sasisekharan et al. shows human H1 HA has a narrow specificity, while the H3 HA (Mos99) can bind to diverse sialylated glycans. Sasisekharan et al. teach multivalency enabled binding to HA units (fig. 18).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to prepare a multivalent sialoside having Neu5Ac-6Galβ-4[GlcNAcβ-4]4GlcNAc.
In addition to the reasons discussed above, the skilled artisan would have been motivated to substitute Neu5Ac-3Galβ-4[GlcNAcβ-4]4GlcNAc with Neu5Ac-6 to give Neu5Ac-6Galβ-4[GlcNAcβ-4]4GlcNAc, because in the same field of endeavor of preparing sialylated oligosaccharides for binding to cells, bacteria and viruses, Sasisekharan et al. teach Neu5Ac-2,6 terminated oligosaccharides bind to human influenza viruses. Sasisekharan et al. generally teach Neu5Acα2-6-Sug1-Sug2-Sug3, which encompasses the sialyloligosaccharide of Samain et al.
One having ordinary skill in the art would have been motivated to prepare a multivalent glycan, because they generate a higher binding affinity than monovalent antigens. Additionally, converting a monovalent glycan to a multivalent glycan was a known strategy, including for sialyl oligosaccharide based glycans, terminated in Neu5Ac-2,6 residues. The ordinary artisan would have had a reasonable expectation of success because Sasisekharan et al. expressly prepared multivalent sialyl oligosaccharides, for binding to influenza viruses.
Thus, the claimed invention as a whole is prima facie obvious over the combined teaching of the prior art.
Claim(s) 28 and 29 are rejected under 35 U.S.C. 103 as being unpatentable over Samain et al. and Sasisekharan et al. as applied to claims 19-24, 26, 27 and 30-32 above, and further in view of Roy et al. (J. Chem. Soc. Chem. Commun., 1993, pp. 264-265, cited in previous Office Action).
Samain et al. teach as discussed above.
Samain et al. do not expressly disclose a poly-lysine support (present claim 28), or a grafting rate of the sialyl oligosaccharide and support (present claim 29).
Sasisekharan et al. teach as discussed above.
Roy et al. is concerned with the preparation of sialyl oligosaccharides that bind to influenza HA, wherein the sialyl oligosaccharide is bound to a poly-lysine support (title). Roy et al. teach preparing conjugates having 1 molar ratio of sialic acid to 17 free lysine groups, i.e. 4-5 mol% (p.264, fourth and fifth para).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to conjugate a multivalent sialoside having Neu5Ac-6Galβ-4[GlcNAcβ-4]4GlcNAc to poly-lysine, because it is a known support for sialosides, including those used for targeting viral receptors, like influenza HA. While Roy et al. teach grafting 4-5 mol% sialoside per poly-lysine, the ordinary artisan would have routinely optimized the molar ratio of sialoside to support.
See MPEP 2144.05, “Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical.”.
Thus, the claimed invention as a whole is prima facie obvious over the combined teaching of the prior art.
Conclusion
Claim 25 is allowable.
Claims 19-24 and 26-32 are rejected.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/BAHAR CRAIGO/
Primary Examiner
Art Unit 1699
