DETAILED ACTION
Notice of Pre-AIA or AIA Status
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claim Status
2. The amendment filed January 19, 2023 have been entered. Claims 1-38 are cancelled. Claims 39-58 are under consideration.
Election/Restrictions
3. Applicant’s election without traverse of Group I in the reply filed on June 25, 2026 is acknowledged. Claims 47 and 49-58 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected claims, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on June 25, 2026.
Information Disclosure Statement
4. The information disclosure statement (IDS) submitted on August 12, 2024 and June 25, 2026 was filed. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
5. Claims 39-46 are rejected under 35 U.S.C. 101 because the claimed invention is not directed to patent eligible subject matter. Based upon an analysis with respect to the claim as a whole, claims 39-46 are determined to be directed to natural products and do not recite something “significantly different” than the natural product. Natural products are “judicial exemptions”. The rationale for this determination is explained below:
Claims 39-46 are drawn to an antigenic OspA polypeptide comprising an outer surface protein A (OspA) serotype 1 polypeptide of Borrelia, wherein the OspA serotype 1 polypeptide of Borrelia does not comprise the sequence of SEQ ID NO: 77 and comprises a modification to reduce or eliminate glycosylation.
Sterba et al., (Microbial Cell Biology. J of Bacteriology. April 1, 2008. Vol 190. Issue 7. Pages 2619-2623). The presence of glycoproteins in Borrelia burgdorferi. Sterba et al., did not find any evidence for glycosylation of the major outer membrane proteins OspA and OspB or the structural flagellar proteins FlaB and FlaA. Surprisingly, Sterba et al., were unable to demonstrate N-linked glycosylation by both indirect staining and detailed structural analysis. However, several other proteins from membrane preparations were stained as glycoproteins and were labeled by lectins. Thus, the OspA is not “markedly different” in structure than naturally occurring OspA. Therefore, all of the ingredients are therefore not markedly different from their counterparts found in nature. These claims fail to satisfy the non-naturally occurring requirement. Furthermore, there is no structural difference because of the mere aggregation of natural occurring OspA a composition; the composition does not change the structure of the naturally occurring OspA.
Additionally, the product claims as a whole do not recite something significantly different from the judicial exceptions because the additional components do not impose meaningful limits on the claim scope therefore substantially all practical applications of the judicial exception are covered. Furthermore, the additional elements in dependent claims for the inclusion of a pharmaceutically acceptable carrier are recited at a high level of generality, and/or are well-understood, purely conventional and routine in the field, and/or are merely appended to the judicial exception without a significant change in the structure of the judicial exception itself as evidenced by the prior art recited within the rejections.
If the applicant chooses to amend the instant claims, the examiner recommends that applicant consider the U.S. Supreme Court ruling that the additional steps should consist of more than well-understood, routine, conventional activity already engaged in by the scientific community. Such putative additional steps, when viewed as a whole, might add nothing significant beyond the sum of their parts taken separately. The Court has made clear that to transform an unpatentable law of nature into a patent-eligible application of such a law, one must do more than simply state the law of nature while adding the words "apply it." Essentially, appending conventional steps, specified at a high level of generality, to laws of nature, natural phenomena, and abstract ideas cannot make those laws, phenomena, and ideas patent-eligible.
The unpatentability of laws of nature was confirmed by the U.S. Supreme Court in Mayo Collaborative Services v. Prometheus Laboratories, Inc., No. 10-1150 (March 20, 2012). The unpatentability of natural products was confirmed by the U.S. Supreme Court in Association for Molecular Pathology v. Myriad Genetics, Inc., 569 U. S. (June 13, 2013). Also see the December 4, 2014 and May 4, 2016 Guidance for Determining Subject Matter Eligibility of Claims Reciting or Involving Laws of Nature, Natural Phenomena, & Natural Products (the Guidance).
Based upon consideration of all of the relevant factors with respect to the claim as a whole, the claims are held to claim a law of nature and natural products and are therefore rejected as ineligible subject matter under 35 U.S.C. 101.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
6. Claim 48 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a method of eliciting an immune response to Borrelia a subject against Lyme Disease comprising administering the antigenic OspA polypeptide to a subject, does not reasonably provide enablement for a method of protecting a subject against Lyme Disease comprising administering the antigenic OspA polypeptide of claim 39 to a subject. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims. This is a scope of enablement rejection.
Factors to be considered in determining whether a disclosure meets the enablement requirement of 35 USC 112, first paragraph, have been described by the court in In re Wands, 8 USPQ2d 1400 (CAFC 1988),page 1404.
Enablement is considered in view of the Wands factors (MPEP 2164.01 (A)). These include: nature of the invention, breadth of the claims, guidance of the specification, the existence of working examples, state of the art, predictability of the art and the amount of experimentation necessary. In re Fisher, 427 F.2d 833,839, 166 USPQ 18, 24 (CCPA 1970) states, "The amount of guidance or direction needed to enable the invention is inversely related to the amount of knowledge in the state of the art as well as the predictability in the art." "The "amount of guidance or direction" refers to that information in the application, as originally filed, that teaches exactly how to make or use the invention. The more that is known in the prior art about the nature of the invention, how to make, and how to use the invention, and the more predictablethe art is, the less information needs to be explicitly stated in the specification. In contrast, if little is known in the prior art about the nature of the invention and the art is unpredictable, the specification would need more detail as to how to make and use the invention in order to be enabling" (MPEP 2164.03). The MPEP further states that physiological activity can be considered inherently unpredictable. Thus, Applicant assumes a certain burden in establishing that inventions involving physiological activity are enabled. All of the Wands factors have been considered with regard to the instant claims, with the most relevant factors discussed below.
Nature of the invention: The nature of the invention is a method of protecting a subject against Lyme Disease comprising administering the antigenic OspA polypeptide of claim 39 to a subject; wherein the relative level of skill of those in the art is deemed to be high.
Breadth of the claims: The claims are broadly drawn to a method of protecting a subject against Lyme Disease. Thus, the claim encompasses a “protective immune response” refers to an immune response that protects any type of subject from Lyme infection e.g., prevents infection or prevents the development of disease associated with infection.
Guidance of the specification/The existence of working examples: The specification teaches any one or more of the antigenic polypeptides, or compositions described herein are provided for use in producing a protective immune response to future infection with Borrelia within any type of subject [para 260]. There is no teaching within the specification for a single vaccine which protects humans, dogs, horses and/or cattle against Lyme disease. There is no teaching within the specification for of multiple different vaccines which protects humans, dogs, horses and/or At best, the specification at paragraph [0024] describes an OspA-Ferritin nanoparticle composition which elicits an immune response in a canine. There are no protocols provided which demonstrate that the OspA polypeptide would be effective in protective immunization, nor are their protocols detailing the amount of OspA needed to mount a sufficient protective immune response. There is no teaching as to what the most effective route of administration for the claimed OspA. There is merely a general suggestion of the compositions that do not apply directly to the instant invention. There are no working examples of the claimed polypeptides provides protective immunity to a mammalian host. Thus, the scope of the scope of the claims is extremely broad compared to the guidance and exemplification provided in the specification. The scope of the claims must bear a reasonable correlation with the scope of enablement. See In re Fisher, 166 USPQ 19 24 (CCPA 1970).
State of the art: The state of the prior art is such that it is well established in the art that there is no vaccine for Lyme disease currently available for humans. The only one ever marketed in the United States, called LYMErix, was pulled from the market in 2002. There is currently no approved or commercially available Lyme disease vaccine for cattle. Because a specific livestock vaccine does not exist, managing ticks in pastures relies on external prevention strategies. Lyme disease products on the market, such as Nobivac Lyme or RECOMBITEK Lyme, are exclusively approved and formulated for dogs. There is no single vaccine product for the different Lyme disease effected subjects. There is no teaching of preventing the tick induced infection or prevents the development of Lyme disease caused by Borrelia harbored within Ixodes scapularis associated with infection. Thus, the state of the art recognized that it would be highly unpredictable with regard to the method of protecting a subject against Lyme Disease comprising administering the antigenic OspA polypeptide of claim 39 to a subject.
Relative Skill of Those in the Art: One of ordinary skill in the art could not predictably extrapolate the teachings in the specification, limited to a vaccine for inducing a protective immunological response in a canine host, the composition comprising the OspA polypeptide as broadly as claimed. In view of the lack of support in the art and specification for an effective and protective vaccine, it would require undue experimentation on the part of the skilled artisan to make and use the claimed vaccine composition; therefore the full scope of the claims is not enabled.
Thus, the scope of the scope of the claims is extremely broad compared to the guidance and exemplification provided in the specification and the specification fails to teach such. The specification fails to show a single challenge experiment. Therefore the scope of enablement does not embrace a method of protection as instantly claimed. Moreover, there is no teaching as to the general vaccination guidelines or the production of a protective immune response.
The specification does not enable the genus because where the results are unpredictable, the disclosure of a single species usually does not provide an adequate basis to support generic claims. In re Soll, 97 F.2d 623, 624, 38 USPQ 189, 191 (CCPA 1938). In cases involving unpredictable factors, such as most chemical reactions and physiological activity, more may be required. In re Fisher, 427 F.2d 833, 839, 166 USPQ 18, 24 (CCPA 1970) (contrasting mechanical and electrical elements with chemical reactions and physiological activity). See also In re Wright, 999 F.2d 1557, 1562, 27 USPQ2d 1510, 1513 (Fed. Cir. 1993); In re Vaeck, 947 F.2d 488, 496, 20 USPQ2d 1438, 1445 (Fed. Cir. 1991). This is because it is not obvious from the disclosure of one particular species, what other species will work. See MPEP 2164.03. One of skill in the art would neither expect nor predict the appropriate functioning of the protection method as broadly as is claimed. Without such guidance, the changes which can be made in polypeptides structure and still function as a vaccine is unpredictable and the experimentation left to those skilled in the art is unnecessarily and improperly extensive and undue. See Amgen, Inc. v. Chugai Pharmaceutical Co. Ltd., 927 F, 2d 1200, 18 USPQ 1016 (Fed. Cir. 1991) at 18 USPQ 1026 1027 and Ex parte Forman, 230 USPQ 546 (BPAI 1986).
In view of the lack of the predictability of the art to which the invention pertains as evidenced by the prior art; the lack of guidance and direction provided by applicant, and the absence of working examples, undue experimentation would be required to practice the claimed vaccine with a reasonable expectation of success, absent a specific and detailed description in applicant’s specification of how to effectively inducing a protective immune response in any type of host, commensurate in scope with the claimed invention.
Claim Rejections - 35 USC § 112
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.
7. Claims 39 and 48 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.
Claim 39 is drawn to an antigenic OspA polypeptide comprising an outer surface protein A (OspA) serotype 1 polypeptide of Borrelia, wherein the OspA serotype 1 polypeptide of Borrelia does not comprise the sequence of SEQ ID NO: 77 and comprises a modification to reduce or eliminate glycosylation. However, the claim does not include language for how to determine the metes and bounds to determine the reduction of glycosylation. The claim does not recite any comparison language. Therefore, clarification of the claim is required to overcome the rejection.
Additionally, claim 48 does not recite administering an therapeutically effective amount of the antigenic OspA. Therefore, the metes and bounds are unclear regarding the amount of the antigenic OspA being administered.
Claim Rejections - 35 USC § 102
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 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 the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
8. Claims 39-41 and 43-46 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Huang et al., (WO 2009126816 published 2009-04-09; priority to April 9, 2008).
The claims 39-46 are drawn to an antigenic OspA polypeptide comprising an outer surface protein A (OspA) serotype 1 polypeptide of Borrelia, wherein the OspA serotype 1 polypeptide of Borrelia does not comprise the sequence of SEQ ID NO: 77 and comprises a modification to reduce or eliminate glycosylation.
Huang et al., teach the production of one or more OspA proteins, used as an oral vaccine to prevent the transmission of Lyme disease, particularly by animal vectors. The recombinantly-produced OspA proteins can be provided in oral and parenteral formulations. The present invention also relates to oral administration of OspA protein(s) to vaccinate against Lyme disease. The OspA proteins may be provided in a dosage form that is suitable for oral administration as a vaccine to prevent an animal from developing Lyme disease after exposure to a source of Borrelia burgdorferi [abstract]. Figure 1 shows the prediction of N-glycosylation sites in the OspA protein sequence. The asparagines predicted to be N-glycosylated are underlined, and the other amino acid residues in the conserved N-glycosylation site (Asn-Xaa-Ser/Thr) are in lower case and italics [para 26]. Figure 2 shows the alignment of native OspA versus mutated and codon-optimized OspA. Original represents the native OspA gene sequence in the Borrelia burgdorferi. Codon-opt represents the OspA gene sequence with codon optimization and mutations at some potential N-glycosylation sites. Amino Acid represents the translated amino acid sequence corresponding to the codon-optimized OspA gene sequence. The underlined amino acid residues are different from their native form by mutation to abrogate the N-glycosylation sites [para 27]. Most OspA proteins include five sites for N-glycosylation. When produced by the methods of the invention, the OspA protein(s) may be glycosylated at all five sites, at any four sites, at any three sites, at any two sites, or at any single glycosylation site. If a variant of OspA having a different number of glycosylation sites is utilized, it may be glycosylated at all or less than all of the glycosylation sites [para 63].
Five potential N-glycosylation sites, at Asparagine (N) residues 20, 71, 190, 202, and 251 were identified in the OspA amino acid sequence (Figure 1). The three C-terminus N-glycosylation sites at N residues 251, 202 and 190 could be more likely to adversely perturb the correct OspA conformation structure, and mutations to abrogate the N-glycosylation at these sites were performed. To abrogate these N-glycosylation sites, the naturally occurring mutations in Borrelia species were extrapolated. At the N-glycosylation sites 251 (NGT) and 190 (NiSK), an Alanine (A) residue occurs at the position of amino acid N residue in Eurasian Lyme disease Borrelia and the position of amino acid Serine (S) residue in β. afzelii, respectively, and thus the substitute of N or S to A at these two N-glycosylation sites was carried out. Considering the structure similarity between N-glycosylation sites 190 and 202, A was substituted for the Threonine (T) at the N-glycosylation site 202 (NDT) [para 97]. Therefore, Huang et al., teach the instantly rejected claims.
Sequence Alignment with instant SEQ ID NO:83
ID AXR53712 standard; protein; 257 AA.
AC AXR53712;
XX
DT 26-NOV-2009 (first entry)
XX
DE Variant OspA protein.
KW OspA; lyme disease; outer surface protein A; plant; protein production;
KW seed; transgenic plant; vaccine, general.
XX
OS Borrelia burgdorferi.
OS Chimeric.
OS Synthetic.
OS Unidentified.
XX
CC PN WO2009126816-A1.
CC PD 15-OCT-2009.
CC PF 09-APR-2009; 2009WO-US040083.
XX
PR 09-APR-2008; 2008US-0071032P.
CC PA (VENT-) VENTRIA BIOSCIENCE.
XX
CC PI Huang N, Nandi S, Petersen LR, Zhang D;
XX
DR WPI; 2009-P83150/73.
DR N-PSDB; AXR53710, AXR53711.
XX
CC PT New transgenic monocot seed that expresses outer surface protein (Osp)A,
CC PT useful for vaccinating an animal against Lyme disease and breaking a Lyme
CC PT disease cycle.
XX
CC PS Example; Fig 2; 53pp; English.
XX
CC The present invention relates to a new transgenic monocot seed that
CC expresses outer surface protein A (OspA), useful for vaccinating an
CC animal against Lyme disease and breaking a Lyme disease cycle. Also
CC claimed are: a method of producing OspA in plant seeds; a method for
CC vaccinating an animal against Lyme disease. The transgenic monocot seed
CC and methods are useful for producing OspA in plant seeds, producing at
CC least one OspA, vaccinating an animal against Lyme disease, and breaking
CC a Lyme disease cycle. The present sequence represents the mutated and
CC codon optimized OspA protein used in the plasmid constructs for rice
CC transformation as described in an example of the invention.
XX
SQ Sequence 257 AA;
Query Match 93.3%; Score 1248; Length 257;
Best Local Similarity 98.8%;
Matches 254; Conservative 1; Mismatches 2; Indels 0; Gaps 0;
Qy 17 CKQNVSSLDEKNSVSVDLPGEMKVLVSKEKNKDGKYDLIATVDKLELKGTSDKNNGSGVL 76
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 CKQNVSSLDEKNSVSVDLPGEMKVLVSKEKNKDGKYDLIATVDKLELKGTSDKNNGSGVL 60
Qy 77 EGVKADKSKVKLTISDDLGQTTLEVFKEDGKTLVSKKVTSKDKSSTEEKFNEKGEVSEKI 136
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 EGVKADKSKVKLTISDDLGQTTLEVFKEDGKTLVSKKVTSKDKSSTEEKFNEKGEVSEKI 120
Qy 137 ITRADGTRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISKSGE 196
|||||||||||||||||||||||||||||||||||||||||||||||||||||||:||||
Db 121 ITRADGTRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNIAKSGE 180
Qy 197 VSVELNDTDSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTKENTITVQQYDSNGTKLE 256
||||||| |||||||||||||||||||||||||||||||||||||||||||||| |||||
Db 181 VSVELNDADSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTKENTITVQQYDSAGTKLE 240
Qy 257 GSAVEITKLDEIKNALK 273
|||||||||||||||||
Db 241 GSAVEITKLDEIKNALK 257
Claim Rejections - 35 USC § 102
9. Claims 39, 42 and 48 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Comstedt et al., (US 20140010835 published 2014-01-09; priority to July 6, 2012).
Comstedt et al., describe a polypeptide comprising a mutant fragment of an outer surface protein A (OspA), a nucleic acid coding the same, a pharmaceutical composition (particularly for use as a medicament of in a method of treating or preventing a Borrelia infection) comprising the polypeptide and/or the nucleic acid, a method of treating or preventing a Borrelia infection and a method of immunizing a subject [abstract]. These truncated forms of OspA proved to be less protective than the full-length OspA protein. Surprisingly, however, it was found in the course of the current invention that the introduction of a disulfide bond in the truncated form (also referred to herein as “mutant OspA fragment” or “mutant fragment”) overcomes this disadvantage. While not being limited to a specific mechanism, it is thought that improved protection is due to increased stability of the OspA fragment, as shown in assays measuring thermal stability [para 19]. The OspA mutant fragment may also comprise further mutations relative to the wild-type. As detailed above, the structure and surface domain of OspA are known in the art. Accordingly, the mutant fragment may comprise further mutations, particularly at sites not on the surface of the protein and/or not involved in the immune response and, therefore not impacting antigenic capacity. These can include one or more amino acid deletion(s), particularly small (e.g., up to 10 amino acids) deletions, one or more amino acid addition(s) (particularly C- or N-terminally), one or more amino acid substitution(s), particularly one or more conservative amino acid substitutions [para 28]. Examples of conservative amino acid substitutions include Asn to Gln and Asp to Glu [para 29]. In a further embodiment of the present invention, the polypeptide of the present invention consists of (i) one or more mutant OspA fragments, optionally joined by linkers, e.g., as defined below and (ii) optionally one or more amino acids heterologous to OspA, particularly a signal sequence and (iii) optionally a posttranslational modification, such as lipidation [para 36]. Therefore Comstedt et al., teach the instantly rejected claims.
Alignment of SEQ ID NO:7
AC BDV37125;
XX
DT 01-JUN-2017 (first entry)
DE Borrelia afzelii OspA serotype 4.
XX
KW OspA protein; Outer surface protein A; antibacterial;
KW borrelia burgdorferi infection; borrelia infection; immune stimulation;
KW prophylactic to disease; protein engineering; protein therapy;
KW therapeutic.
XX
OS Borrelia afzelii K78.
CC PN US2017101446-A1.
CC PD 13-APR-2017.
XX
CC PF 22-SEP-2016; 2016US-00272581.
XX
PR 06-JUL-2012; 2012US-0668627P.
PR 14-MAR-2013; 2013US-00802991.
PR 08-JUL-2013; 2013WO-EP064403.
PR 05-JAN-2015; 2015US-00412722.
XX
CC PA (ICEL ) VALNEVA AUSTRIA GMBH.
XX
CC PI Comstedt P, Lundberg U, Meinke A, Hanner M, Schueler W, Wizel B;
CC PI Reinisch C, Grohmann B, Schlegl R;
XX
DR WPI; 2017-289277/31.
XX
CC PT New polypeptide comprising mutant fragment of Borrelia outer surface
CC PT protein A, used to treat or prevent Borrelia infection.
XX
CC PS Disclosure; Fig 1; 215pp; English.
XX
CC The present invention relates to a novel mutant fragment of Borrelia
CC outer surface protein A (OspA) useful for treating and preventing
CC Borrelia infection in a subject. The invention further discloses: (1) a
CC nucleic acid molecule encoding a mutant polypeptide fragment of Borrelia
CC OspA; (2) a pharmaceutical composition comprising the polypeptide; (3) a
CC method for treating and preventing Borrelia infection in a subject; and
CC (4) a method for immunizing a subject. Borrelia infection can be due to
CC B. burgdorferi sensu stricto, B. garinii, B. afzelii, B. andersoni, B.
CC bavariensis, B. bissettii, B. valaisiana, B. lusitaniae, B. spielmanii,
CC B. japonica, B. tanukii, B. turdi or B. sinica infection. The present
CC sequence is a Borrelia afzelii OspA serotype 4, which is useful in the
CC method for preparing a pharmaceutical composition comprising for treating
CC and preventing Borrelia infection in a subject.
XX
SQ Sequence 257 AA;
Score 1232; Length 257;
Best Local Similarity 99.6%;
Matches 249; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MDEKNSVSVDLPGEMKVLVSKEKDKDGKYSLMATVDKLELKGTSDKSNGSGTLEGEKSDK 60
:|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 8 LDEKNSVSVDLPGEMKVLVSKEKDKDGKYSLMATVDKLELKGTSDKSNGSGTLEGEKSDK 67
Qy 61 SKAKLTISEDLSKTTFEIFKEDGKTLVSKKVNSKDKSSIEEKFNAKGELSEKTILRANGT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 68 SKAKLTISEDLSKTTFEIFKEDGKTLVSKKVNSKDKSSIEEKFNAKGELSEKTILRANGT 127
Qy 121 RLEYTEIKSDGTGKAKEVLKDFALEGTLAADKTTLKVTEGTVVLSKHIPNSGEITVELND 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 128 RLEYTEIKSDGTGKAKEVLKDFALEGTLAADKTTLKVTEGTVVLSKHIPNSGEITVELND 187
Qy 181 SNSTQATKKTGKWDSNTSTLTISVNSKKTKNIVFTKEDTITVQKYDSAGTNLEGNAVEIK 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 188 SNSTQATKKTGKWDSNTSTLTISVNSKKTKNIVFTKEDTITVQKYDSAGTNLEGNAVEIK 247
Qy 241 TLDELKNALK 250
||||||||||
Db 248 TLDELKNALK 257
Conclusion
10. No claims allowed. However sequences SEQ ID NO: 1, 9, 26, 43, 53, 63 and 76 are free of the prior art.
Pertinent Art
11. The prior art made of record and not relied upon is considered pertinent to applicant’s disclosure. See also US 20140314801 and WO9004411.
Turanek et al., (Molecular Vaccines from Prophylaxis to Therapy - Volume 2, 13 Jun 2013, :561-577) teach Functionalised Nanoliposomes for Construction of Recombinant Vaccines: Lyme Disease as an Example.
Conclusion
12. No claims allowed.
13. Any inquiry concerning this communication or earlier communications from the examiner should be directed to JA-NA A HINES whose telephone number is (571)272-0859. The examiner can normally be reached Monday thru Thursday.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor Peter Paras, can be reached on 571-272-4517. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free).
/JANA A HINES/Primary Examiner, Art Unit 1645
Prosecution Insights