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 .
DETAILED OFFICE ACTION
This Office Action is in response to the papers filed on 27 September 2024.
CLAIMS UNDER EXAMINATION
Claims 23-25 and 27-32 are pending and have been examined on their merits.
PRIORITY
Provisional Application 62/719,272, filed on 17 August 2018, is acknowledged.
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.
Claim 29 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement.
The claims contain subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 29 comprises a step of washing blood. The specification filed on 05 April 2024 provides support for washing red blood cells (erythrocytes) ([00114] [00116] [00118] [00120]). It does not provide support for washing blood.
A consideration of the four corners of the specification does not provide support for the claimed limitation.
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 23-25 and 27-32 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.
Regarding claim 23: step (b) recites incubating the blood or erythrocytes “…for a period of time sufficient to allow “the enzymes”…”. There is a lack of antecedent basis for “the enzymes”. It is unclear if the claim is referring to the proteins recited in step (a), or other enzymes. The meted and bounds of the claimed method are unclear. Appropriate correction is required. All dependent claims are included in this rejection.
Claim 29 recites washing to remove the crowding agent. There is a lack of antecedent basis in the base claim for a crowding agent. The metes and bounds of the claim are unclear. Appropriate correction is required.
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.
Claims 23-25 and 30-32 are rejected under 35 U.S.C. 103 as being unpatentable over Haruko et al. (Development of H-specificity in A Substance by A-Decomposing Enzyme from Clostridium tertium A. proc. Japan Acad., 44 1968) in view of Earl et al. (The Broad Institute Genome Sequencing Platform 2014) as evidenced by the National Cancer Institute (definition of “red blood cell”), NCBI (Flavonifractor plautii Taxonomy) and GenCor (UNIPROT A0A096D861_FLAPL and UNIPROT A0A096B2Z8_FLAPL; see Office Action appendix).
Haruko et al. investigate A-decomposing enzymes from Clostridium tertium (see page 264, second paragraph). The art teaches enzymes that have the activity to destroy the A activity and to enhance the H activity in A substance (page 264, second paragraph). The art applies enzyme fractions to either “A substance or A red cells” (page 264, last paragraph). It is well known in the art that “red cells” are also called erythrocytes (definition by National Cancer Institute). Haruko teaches the enzyme in Fraction 4 destroys A activity, but H activity was not enhanced (page 264, last paragraph). Fraction 4 enzyme acts as deacetylase on N-acetylgalactosaminyl residue, a determinant of the A -specificity (see page 265, second paragraph). The enzymes in Fraction 31-34 enhance H activity and destroy A activity (same cited section).
Haruko teaches “when A substance or A red cells were first incubated with Fr. 4 deacetylase, and then with Fraction 31-34 enzyme, galactosamine was liberated with enhancement of the H activity. This indicates that the Fr. 31-34 enzyme preparation principally contains galactosaminidase and deacetylase” (first paragraph of page 266).
The art teaches “When the deacetylase contained in the A-decomposing enzyme is solely applied to A substance of A red cells, the A activity is destroyed without the H activity being enhanced. When, however, the galactosaminidase is acted together with the deacetylase, the H activity in A-substance is enhanced because if there is fucose in it… which has the capacity to exert H-specific action, H-specificity is developed by liberation of N-acetyl group and galactosamine which has inhibited it” (see page 267, second paragraph).
Haruko treats erythrocytes with enzymes from Clostridium tertium to cleave A-substance (A-antigen).Haruko teaches a galacosaminidase. Haruko also teaches a “deacetylase” which deacetylates a N-acetylgalactosaminyl residue. As evidenced by UniProt, N-acetylgalactosamine-6-phosphate deacetylase catalyzes the deacetylation of N-acetyl-D-galactosamine 6-phosphate to D-galactosamine 6-phosphate”. Examiner notes “GalNac” is N-Acetylgalactosamine. Therefore Haruko teaches a GalNacdeacetylase.
Claim 23 recites at least one of the galactosaminidase or GalNac deacetylase are derived from Flavonifractor plautii. This is a product by process limitation.
The deficiency of Haruko is that it does not teach at least one the enzymes is derived from Flavonifractor plautii. As evidenced by NCBI, “Flavonifractor plautii” is previously known as “Clostridium orbiscindens”
As evidenced by GenCor (see Office Action appendix), Earl et al. teach both enzymes can be derived from Flavonifractor plautii (Clostridium orbiscindens).
It would have been obvious to try using galactosaminidase from Flavonifractor plautii in the assay taught by Haruko. One would have been motivated to do so since Haruko uses a galactosaminidase obtained from Clostridium tertium and Earl teaches galactosaminidase can also be obtained from the Clostridium Flavonifractor plautii. Both enzymes catalyze the same reaction. Therefore they are interpreted to have similar properties. KSR B teaches it is rational to substitute one known, equivalent element for another to obtain predictable results. One would have had a reasonable expectation of success since the enzymes catalyze the same reaction. The following is noted from the MPEP 2113:
“[E]ven though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process.” In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985) (citations omitted). MPEP 2113 further indicates that “The Patent Office bears a lesser burden of proof in making out a case of prima facie obviousness for product-by-process claims because of their peculiar nature” than when a product is claimed in the conventional fashion. In re Fessmann, 489 F.2d 742, 744, 180 USPQ 324, 326 (CCPA 1974). Once the examiner provides a rationale tending to show that the claimed product appears to be the same or similar to that of the prior art, although produced by a different process, the burden shifts to applicant to come forward with evidence establishing an unobvious difference between the claimed product and the prior art product. In re Marosi, 710 F.2d 798, 802, 218 USPQ 289, 292 (Fed. Cir. 1983).
Therefore claim 23 is rendered obvious.
As evidenced by GenCor, Earl et al. disclose UNIPROT A0A096D861_FLAPL.
As evidenced by GenCor (Result 1), the sequence reads on Seq ID 2.
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942
752
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As evidenced by GenCor, Earl et al. disclose UNIPROT A0A096B2Z8_FLAPL.
As evidenced by GenCor (Result 1), the sequence reads on SEQ ID 9
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726
428
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Therefore claims 24 and 25 are included in this rejection.
The enzymes taught by Earl anticipate the claimed enzymes. Therefore they would be expected to have the properties recited in claims 30 and 32 when used in the method taught by Haruko. Therefore claims 30 and 32 are included in this rejection.
Haruko teaches the deacetylase acts at an pH optimum of 7.2 (page 265, second column). The galactosaminidase acts at a pH optimum of 6.8 (page 266, first paragraph). Therefore claim 31 is included in this rejection.
Therefore Applicant’s Invention is rendered obvious as claimed.
Claims 27-29 are rejected under 35 U.S.C. 103 as being unpatentable over Haruko in view of Earl as evidenced by GenCor as applied to claim 23 above, and further in view of Goldstein et al. (Enzymatic Conversion of Certain Sub-Type A and AB erythrocytes. Patent 4609627 1986).
Claim 23 is rendered obvious on the grounds set forth above. The teachings of the prior art are reiterated.
Haruko teaches not teach the use of a crowing agent (claims 27-28).
Haruko is silent regarding washing (claim 29)
Goldstein et al. teach a method of treating erythrocytes with a galactosaminidase to remove A-antigen (Abstract). Goldstein teaches the use of either free enzymatic form or disposing the enzyme on a support, such as dextran (hence, a crowding agent) (column 4, lines 51-55). The art teaches the enzyme-soluble support conjugate e.g. enzyme dextran conjugate has the same specificity and ability for removal of the A determinant from the surface of the red cells as the free enzyme preparation and can be reused and stored without loss of activity. The use of such a conjugate is desired since they can be used repeatedly and their use is not characterized by side reactions due to impurities in starting enzyme material as is the case when free enzyme is employed. See column 6, lines 41-65.
Goldstein teaches erythrocytes are washed following enzyme treatment to remove enzyme and adjust the pH to between 7.2-7.4 to re-equilibrate the erythrocytes (see column 5, lines 55-57).
It would have been obvious to use a crowing agent in the method taught by Haruko. One would have been motivated to do so since Haruko treats a method of converting A-erythrocytes using enzymes and Goldstein teaches using a crowding agent in a method of converting A-erythrocytes using enzymes. One would use a crowding agent as an enzyme support, as taught by Goldstein, since it allows the enzymes to be used repeatedly and inhibits side reactions. One would have had a reasonable expectation of success since Goldstein teaches crowing agents can be used when converting erythrocytes. One would have expected similar results since both references using enzymes to convert erythrocytes. Therefore claim 27 is rejected. Goldstein teaches dextran. Therefore claim 28 is included in this rejection.
It would have been obvious to combine the teachings of the prior art by washing erythrocytes. One would have been motivated to do so since Haruko treats a method of converting A-erythrocytes using enzymes and Goldstein teaches washing erythrocytes after being treated with enzyme. One would do so since Goldstein teaches washing removes and enzyme and re-equilibrates the erythrocytes. One would have had a reasonable expectation of success since Goldstein teaches erythrocytes can be washed following enzyme treatment. One would have expected similar results since both references using enzymes to convert erythrocytes. Therefore claim 29 is included in this rejection.
Therefore Applicant’s Invention is rendered obvious as claimed.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NATALIE MOSS whose telephone number is (571) 270-7439. The examiner can normally be reached on Monday-Friday, 8am-5pm EST.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Sharmila Landau can be reached on (571) 272-0614. The fax phone number for the organization where this application or proceeding is assigned is (571) 270-8439.
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/NATALIE M MOSS/ Examiner, Art Unit 1653