DETAILED ACTION
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 .
Election/Restrictions
Applicant’s election without traverse of Group I, comprising claims 1-8, 18-20 and 26, in the reply filed on 12/01/2025 is acknowledged.
However, the Applicant elected the following species with traverse.
Fluorescent protein polypeptide, in claim 3.
Heavy-chain variable domain (VHH), in claim 4.
Barley, in claim 19.
The Examiner duly acknowledges the honest mistake in the previous Office action, dated 10/1/2025, by wrongly referring claim 5 (page 6, line 7), instead of claim 4, while asking for election of the species (a) for Group I. It should have been claim 4, as rightly pointed out by the Applicant.
Applicant's election with traverse of the species in the reply filed on 10/1/2025 is also acknowledged. The traversal is on the ground that different species in the claims “should not represent serious search and/or examination burden” (response, page 13, para 4 and 7). This is not found persuasive. The species are independent or distinct because they have specific characteristics and/or specific structures (as gene and/or protein sequences) which require different search strategies and search queries.
The requirement is still deemed proper and is therefore made FINAL.
Claim Status
Claims 1-28 are pending.
Claims 9-17, 21-25 and 27-28 are withdrawn from examination as being part of non-elected groups.
Claims 1-8, 18-20 and 26 are being examined.
Claim Rejections - 35 USC § 112(b)
Claim 20 is 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.
It is not clear if the method comprises:
introducing a genetic alteration to the plant cell comprising a first nucleic acid sequence encoding a heterologous first subunit polypeptide comprising an affinity polypeptide; and/or
(a) introducing a genetic alteration to the plant cell comprising a second nucleic acid sequence encoding a heterologous second subunit polypeptide optionally comprising a tag polypeptide; or (b) comprising genetically modifying the plant cell by transforming the plant cell with one or more gene editing components that target a first endogenous nuclear genome sequence encoding the first subunit polypeptide, wherein the first subunit polypeptide is genetically modified to comprise the affinity polypeptide; and/or
(a) genetically modifying the plant cell by transforming the plant cell with one or more gene editing components that target a second endogenous nuclear genome sequence encoding the second subunit polypeptide, wherein the endogenous second subunit polypeptide is genetically modified to comprise a tag polypeptide.
OR
introducing a genetic alteration to the plant cell comprising a first nucleic acid sequence encoding a heterologous first subunit polypeptide comprising an affinity polypeptide; and/or
introducing a genetic alteration to the plant cell comprising a second nucleic acid sequence encoding a heterologous second subunit polypeptide optionally comprising a tag polypeptide; or
comprising genetically modifying the plant cell by transforming the plant cell with one or more gene editing components that target a first endogenous nuclear genome sequence encoding the first subunit polypeptide, wherein the first subunit polypeptide is genetically modified to comprise the affinity polypeptide; and/or
genetically modifying the plant cell by transforming the plant cell with one or more gene editing components that target a second endogenous nuclear genome sequence encoding the second subunit polypeptide, wherein the endogenous second subunit polypeptide is genetically modified to comprise a tag polypeptide.
It is unclear how the Examiner should interpret all the alternatives because all the different alternatives are connected by “and/or” or “or”, and separated by semicolons “;” Nonetheless, the Examiner examines the claim 20, as interpreted that any one of the recited alternatives would satisfy the claim limitation.
The Examiner suggests to amend the claim to make the claim limitations clearer.
Claim Rejections - 35 USC § 102(a)(1)
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 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)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(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.
Claims 1-3, 5-7, 18-20 and 26 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Broghammer et al. (Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding, 2012, PNAS, 109:13859-13864).
Broghammer et al. teaches that lotus (Lotus japonicus) (as recited in claim 19) Nod Factor Receptor 5 (NFR5) and Nod Factor Receptor 1 (NFR1) bind Nod factor directly and play an important role in root nodule symbiosis leading towards nitrogen fixation in a plant (Abstract). It also teaches genetically modified cells (as recited in claims 1, 18, and 26) and the method of making (as recited in claim 20) such cells where full length NFR1 and NFR5 are expressed in tobacco and Arabidopsis cells (which are eukaryotic and plant cells, as recited in claims 5-6) as GFP/YFP fusion proteins (page 13860, left column, para 3, line 15-16; page 13863, right column, last 2 lines; Supporting Information, page 1, para 1). All the NFR proteins including NFR1 and NFR5 are known to be a transmembrane protein (page 13859, right column, para 1, line 11-13) and forms a transmembrane (protein) receptor complex (page 13859, right column, para 1, line 19-20). The NFR1 and NFR5 heterocomplex, which is an oligomer with high affinity for each other formed by affinity polypeptides within the NFR1 and NFR5 proteins, is capable of initiating or activating transmembrane (TM) signal transduction process (page 13859, right column, para 2, line 6-7).
Broghammer et al. describes using split YFP system using NFR1 and NFR5 (page 13859, right column, para 1, line 20-21), where the fluorescent protein polypeptide (as recited in claim 3), YFP, is divided in two halves. One half of the YFP is fused to NFR1 while the other half is fused to NFR5, and these two halves bind directly (as recited in claim 2) due to high affinity to each other. It is known in the art that the split YFP assay (a Bimolecular Fluorescence Complementation, BiFC, assay) relies on the high intrinsic affinity of YFP’s two halves (YN and YC) to spontaneously reassemble into a functional, fluorescent Yellow Fluorescent Protein (YFP) when brought close together by interacting proteins creating a signal that visualizes the protein-protein interaction (PPI) in real-time within living cells. In this context, NFR1 and NFR5 can be used interchangeably to read on to “first subunit polypeptide” and “second subunit polypeptide” (as recited in claims 1-2, 6-7 and 20) of the oligomer they form. All these interactions happen inside a cell, i.e., intracellularly, as recited in claim 1.
It is known in the art that all NFRs including NRF1 and NRF5 comprise lysin motif (LysM) receptor (Broghammer et al., page 13859, left column, para 1, line 7-8), as recited in claim 6.
The Applicant describes, “an affinity polypeptide can be any polypeptide that enables any stable protein-protein dimerization (e.g., two proteins that bind). Protein dimerization by affinity polypeptides can be or can be derived from known dimers, known protein interactions, or proteins that bind in silico” (page 99, para 98, line 1-4). The instant description teaches, “the term “epitope tag” or “affinity tag” or “tag polypeptides” refers to a site on or fused to a target polypeptide to which an affinity polypeptide binds” (examples are excluded) (page 99, para 99, line 1-4). Thus, the two halves of YFP (YC and YN), which are heterologous to both NFR1 and NFR 5, can be described as, and reads on to, “tag polypeptide” as well as “affinity polypeptide”.
Broghammer et al. also teaches expressing NRF1-GFP (page 13860, para 3, line 1-2) and NRF5-GFP (page 13860, para 3, line 7) fusion proteins in genetically modified plant cells. It is implied that these two fusion proteins would directly bind to each other forming an oligomer and activating a TM receptor signaling process, as recited in claim 1.
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Broghammer et al. as applied to rejected claims 1-3, 5-7, 20 and 26 under 35 U.S.C. 102(a)(1) above, and further in view of Rothbauer et al. (A Versatile Nanotrap for Biochemical and Functional Studies with Fluorescent Fusion Proteins, 2008, Molecular & Cellular Proteomics, Molecular & Cellular Proteomics.7:282-9).
Claim 4 depends from claim 1 and is drawn to the genetically modified cell wherein the affinity polypeptide is a heavy-chain variable domain (VHH) and/or a synthetic version of it.
Broghammer et al. describes a genetically modified cell comprising a transmembrane (TM) receptor complex comprising a first subunit polypeptide fused to a heterologous affinity polypeptide and binds to a second subunit polypeptide forming an oligomer and activates TM receptor signaling, as discussed above.
However, Broghammer et al. does not teach any heavy-chain variable domain (VHH) and/or a synthetic version of it.
Rothbauer et al. described developing a specific binder for fluorescent proteins including GFP and YFP (page 283, left column, para 2, line 1-6; page 183, para 3, line 3), which are the most widely used labeling tags in cell biology (page 282, right column, line 12-13), based on a 13-kDa GFP binding fragment derived from a llama single chain antibody (Abstract), which is also referred to as VHH (heavy-chain variable domain) (page 282, right column, line 18-19). These VHHs, which present the smallest intact antigen-binding units, are highly soluble and stable, and can be efficiently produced in heterologous systems (page 282, right column, line 20-24).
The GFP-binding protein (GBP) allows a fast and efficient (one-step) isolation of GFP and YFP fusion proteins and their interacting factors for biochemical analyses including mass spectroscopy and enzyme activity measurements, as GBP recognizes YFP as well (page 284, right column, para 3, line 3-4). Moreover, GBP is also suitable for chromatin immune-precipitations from cells expressing fluorescent DNA-binding proteins including GFP and YFP. Most importantly, GBP can be fused with cellular proteins to ectopically recruit GFP/YFP fusion proteins allowing targeted manipulation of cellular structures and processes in living cells (abstract).
It would have been obvious to an ordinarily skilled artisan to fuse the heavy-chain variable domain, as described by Rothbauer et al., with specific proteins including NFR1 and/or NFR5 for various goals. Such goals would comprise purifying the fused proteins with this small affinity polypeptide, isolate and/or identify the interacting partners of the fused protein(s) in a protein complex while having the useful option to visualize the fused or interacting fluorescent protein(s) like GFP or YFP in-vivo.
Nitrogen fixation via nodulation in legume plants where NFR1 and NFR5 proteins play important roles, is of great economic importance. Understating the process and other proteins that interact with NFR1 and/or NFR5 is of great academic and commercial interests.
An ordinarily skilled artisan would have been motivated to fuse the heavy-chain variable domain with NFR1 or NFR5 for various goals. Such goals would include to purify the fused protein with this small affinity polypeptide more efficiently or easily, isolate and/or identify the interacting partners of the fused protein(s) in a protein complex while having the useful option to visualize the fused or interacting fluorescent protein(s) like GFP or YFP in-vivo.
Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Broghammer et al. as applied to reject claims 1-3, 5-7, 20 and 26 under 35 U.S.C. 102(a)(1) above, and further in view of Andedrsen et al. (US 2021/0233608 A1, published on July 29, 2021).
Claim 8 indirectly depends from claim 1 and is drawn to any of the recited SEQ ID NOs encoding NFR1, LYK3, or RLK4; and any of the recited sequences encoding NFR5, NFP, or RLK10. The list of SEQ ID NOs comprise NFR1 encoded by SEQ ID NO: 4 and NFR5 encoded by SEQ ID NO: 5.
Broghammer et al. describes expressing full length cDNA encoding full length NFR1 and NFR5 proteins (page 13860, left column, para 3, line 15-16; page 13863, right column, last 2 lines; Supporting Information, page 1, para 1). Broghammer et al. also describes a genetically modified cell comprising a transmembrane (TM) receptor complex comprising a first subunit polypeptide fused to a heterologous affinity polypeptide that binds to a second subunit polypeptide forming an oligomer and activates TM receptor signaling, as discussed above.
However, Broghammer et al. does not explicitly teach a NFR1 protein encoded by SEQ ID NO: 4 and a NFR5 protein encoded by SEQ ID NO: 5.
Andedrsen et al. teaches a NFR1 protein from lotus (Lotus japonicus) encoded by SEQ ID NO: 70 (page 12, para 0048, line 13) which is having 100% sequence identity to instant SEQ ID NO: 4, as shown below.
RESULT 1
US-17-267-240-70
Filing date in PALM: 2021-02-09
Sequence 70, US/17267240
Publication No. US20210233608A1
GENERAL INFORMATION
APPLICANT: Aarhus Universitet
TITLE OF INVENTION: GENETICALLY ALTERED LYSM RECEPTORS WITH ALTERED AGONIST
TITLE OF INVENTION: SPECIFICITY AND AFFINITY
FILE REFERENCE: 79454-20004.00
CURRENT APPLICATION NUMBER: US/17/267,240
CURRENT FILING DATE: 2021-02-09
PRIOR APPLICATION NUMBER: PCT/EP2019/071705
PRIOR FILING DATE: 2019-08-13
PRIOR APPLICATION NUMBER: US 62/718,282
PRIOR FILING DATE: 2018-08-13
NUMBER OF SEQ ID NOS: 106
SEQ ID NO 70
LENGTH: 623
TYPE: PRT
ORGANISM: Lotus japonicus
Query Match 100.0%; Score 3198; Length 623; Best Local Similarity 100.0%;
Matches 623; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MKLKTGLLLFFILLLGHVCFHVESNCLKGCDLALASYYILPGVFILQNITTFMQSEIVSS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MKLKTGLLLFFILLLGHVCFHVESNCLKGCDLALASYYILPGVFILQNITTFMQSEIVSS 60
Qy 61 NDAITSYNKDKILNDINIQSFQRLNIPFPCDCIGGEFLGHVFEYSASKGDTYETIANLYY 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 NDAITSYNKDKILNDINIQSFQRLNIPFPCDCIGGEFLGHVFEYSASKGDTYETIANLYY 120
Qy 121 ANLTTVDLLKRFNSYDPKNIPVNAKVNVTVNCSCGNSQVSKDYGLFITYPIRPGDTLQDI 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 ANLTTVDLLKRFNSYDPKNIPVNAKVNVTVNCSCGNSQVSKDYGLFITYPIRPGDTLQDI 180
Qy 181 ANQSSLDAGLIQSFNPSVNFSKDSGIAFIPGRYKNGVYVPLYHRTAGLASGAAVGISIAG 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 ANQSSLDAGLIQSFNPSVNFSKDSGIAFIPGRYKNGVYVPLYHRTAGLASGAAVGISIAG 240
Qy 241 TFVLLLLAFCMYVRYQKKEEEKAKLPTDISMALSTQDGNASSSAEYETSGSSGPGTASAT 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 TFVLLLLAFCMYVRYQKKEEEKAKLPTDISMALSTQDGNASSSAEYETSGSSGPGTASAT 300
Qy 301 GLTSIMVAKSMEFSYQELAKATNNFSLDNKIGQGGFGAVYYAELRGKKTAIKKMDVQAST 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 GLTSIMVAKSMEFSYQELAKATNNFSLDNKIGQGGFGAVYYAELRGKKTAIKKMDVQAST 360
Qy 361 EFLCELKVLTHVHHLNLVRLIGYCVEGSLFLVYEHIDNGNLGQYLHGSGKEPLPWSSRVQ 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 EFLCELKVLTHVHHLNLVRLIGYCVEGSLFLVYEHIDNGNLGQYLHGSGKEPLPWSSRVQ 420
Qy 421 IALDAARGLEYIHEHTVPVYIHRDVKSANILIDKNLRGKVADFGLTKLIEVGNSTLQTRL 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 IALDAARGLEYIHEHTVPVYIHRDVKSANILIDKNLRGKVADFGLTKLIEVGNSTLQTRL 480
Qy 481 VGTFGYMPPEYAQYGDISPKIDVYAFGVVLFELISAKNAVLKTGELVAESKGLVALFEEA 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 VGTFGYMPPEYAQYGDISPKIDVYAFGVVLFELISAKNAVLKTGELVAESKGLVALFEEA 540
Qy 541 LNKSDPCDALRKLVDPRLGENYPIDSVLKIAQLGRACTRDNPLLRPSMRSLVVALMTLSS 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 LNKSDPCDALRKLVDPRLGENYPIDSVLKIAQLGRACTRDNPLLRPSMRSLVVALMTLSS 600
Qy 601 LTEDCDDESSYESQTLINLLSVR 623
|||||||||||||||||||||||
Db 601 LTEDCDDESSYESQTLINLLSVR 623
Andedrsen et al. also teaches a NFR5 protein from lotus (Lotus japonicus) encoded by SEQ ID NO: 11 (page 13, para 0052, line 5-6) which is having 100% sequence identity to instant SEQ ID NO: 5, as shown below.
RESULT 1
US-17-267-240-11
Filing date in PALM: 2021-02-09
Sequence 11, US/17267240
Publication No. US20210233608A1
GENERAL INFORMATION
APPLICANT: Aarhus Universitet
TITLE OF INVENTION: GENETICALLY ALTERED LYSM RECEPTORS WITH ALTERED AGONIST
TITLE OF INVENTION: SPECIFICITY AND AFFINITY
FILE REFERENCE: 79454-20004.00
CURRENT APPLICATION NUMBER: US/17/267,240
CURRENT FILING DATE: 2021-02-09
PRIOR APPLICATION NUMBER: PCT/EP2019/071705
PRIOR FILING DATE: 2019-08-13
PRIOR APPLICATION NUMBER: US 62/718,282
PRIOR FILING DATE: 2018-08-13
NUMBER OF SEQ ID NOS: 106
SEQ ID NO 11
LENGTH: 591
TYPE: PRT
ORGANISM: Lotus japonicus
Query Match 100.0%; Score 3028; Length 591; Best Local Similarity 100.0%;
Matches 591; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MTSFFLFTNTLFLALMMFFSTTHHILAQLSHTNGTNFSCPVDSPPSCDTYVTYFAQSPNF 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MTSFFLFTNTLFLALMMFFSTTHHILAQLSHTNGTNFSCPVDSPPSCDTYVTYFAQSPNF 60
Qy 61 LTLTSISDLFDTSPLSIARASNIKDENQNLVPGQLLLVPVTCACSGSNSFSNISHMIKEG 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 LTLTSISDLFDTSPLSIARASNIKDENQNLVPGQLLLVPVTCACSGSNSFSNISHMIKEG 120
Qy 121 ESYYYLSTTSYENLTNWETVQDSNPNYNPYLLPVGIKVVIPLFCKCPSNYHLNKGIEYLI 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 ESYYYLSTTSYENLTNWETVQDSNPNYNPYLLPVGIKVVIPLFCKCPSNYHLNKGIEYLI 180
Qy 181 TYVWHNNDNVSLVASKFGVSTQDIISENNFSHQNFTAATNFPILIPVTQLPSLSQSYSSS 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 TYVWHNNDNVSLVASKFGVSTQDIISENNFSHQNFTAATNFPILIPVTQLPSLSQSYSSS 240
Qy 241 ERKRSNHIHIIISIGISLGSTLLIALLVLVSVTCLRKRKSSENKSLLSVEIAGKKLISGV 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 ERKRSNHIHIIISIGISLGSTLLIALLVLVSVTCLRKRKSSENKSLLSVEIAGKKLISGV 300
Qy 301 SNYVSKSILYEFRLIMEATLNLNEQCKIGESVYKAKLDGQVLAVKKVKEDVTEEVMILQK 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SNYVSKSILYEFRLIMEATLNLNEQCKIGESVYKAKLDGQVLAVKKVKEDVTEEVMILQK 360
Qy 361 VNHLNLVKLMGVSSGHDGNHFLVYEFAENGSLHNWLFSNSSTGSRFLTWSQRISIAVDVA 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 VNHLNLVKLMGVSSGHDGNHFLVYEFAENGSLHNWLFSNSSTGSRFLTWSQRISIAVDVA 420
Qy 421 MGLQYMHEHTQPSIVHRDITSSNILLDSNFKAKIANFSVARTSINPMILKVDVFGYGVVL 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 MGLQYMHEHTQPSIVHRDITSSNILLDSNFKAKIANFSVARTSINPMILKVDVFGYGVVL 480
Qy 481 LELLSGKKSLTNNEINHIREIFDLKEKREERIRRWMDPKIESLYPIDDALSLAFLAMNCT 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 LELLSGKKSLTNNEINHIREIFDLKEKREERIRRWMDPKIESLYPIDDALSLAFLAMNCT 540
Qy 541 SEKPLSRPTMGEVVLSLSLLMTQHSPTTLERSWTCGLDVDVTEMQTLIAAR 591
|||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 SEKPLSRPTMGEVVLSLSLLMTQHSPTTLERSWTCGLDVDVTEMQTLIAAR 591
It would have been obvious to an ordinarily skilled artisan to modify the method, as described by Broghammer et al., and use NFR1 and NFR5 proteins from lotus, a commercially important crop, as described by Andedrsen et al., to understand the TM receptor signaling process via NFR1 and NRF5, which is involved in root nodule symbiosis leading to nitrogen fixation, as described by Broghammer et al.
An ordinarily skilled artisan would have been motivated to use NFR1 and NFR5 proteins from lotus, a commercially important crop, to understand the TM receptor signaling process via NFR1 and NRF5 involved in root nodule symbiosis and nitrogen fixation in lotus.
Conclusion
No claim is allowed.
Communication
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JAY CHATTERJEE whose telephone number is (703)756-1329. The examiner can normally be reached (Mon - Fri) 8.30 am to 5.30 pm..
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Bratislav Stankovic can be reached at (571) 270-0305. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
Jay Chatterjee
Patent Examiner
Art Unit 1662
/Jay Chatterjee/ Examiner, Art Unit 1662
/BRATISLAV STANKOVIC/ Supervisory Patent Examiner, Art Units 1661 & 1662