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 .
Application Status
This action is written in response to applicant’s correspondence received on 102/27/2025. Claims 1, 3-10, 12, 15, 23-24, 28-29, 32, and 51-53 are pending. Claims 1, 12, 24, and 32 have been amended. Claims 28-29 have been withdrawn. Claims 2, 11, 13-14, 16-22, 25-27, 30-31, 33-50, and 54-62 have been cancelled. Claims 1, 3-10, 12, 15, 23-24, 32, and 51-53 are currently under examination.
Any rejection of record in the previous office actions not addressed herein is withdrawn. New grounds of rejection are presented herein that were not necessitated by applicant’s amendment of the claims. Therefore, this action is not final.
Claim Rejections - 35 USC § 112 – New Rejection Necessitated by Amendment
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.
Claim 1, 3-10, 24, 32, and 51-53 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 1, claim 1 recites that the adenosine deaminase is SEQ ID NO: 331 and the ATPase comprises SEQ ID NO: 330. According the specification in Table 15-C, SEQ ID NOs 330 and 331 correspond to rows 29-30 of Table 15-A (see bottom of page 196 and top of page 197). Table 15A of the specification recites that both rows 29 and 30 describe an “ATPase + deaminase.” Thus, from Table 15A, the broadest reasonable interpretation of the definition of the sequence is that, for instance, SEQ ID NO: 330 comprises both an ATPase and a deaminase. Claim 1 is therefore unclear because claim 1 recites both SEQ ID NOs 330 and 331, which are recited in Table 15A to comprises both an ATPase and deaminase but theses sequences are recited to be only either an ATPase or deaminase.
Claim 1 also recites “the ATPase and deaminase are linked together.” This phrase lacks proper antecedent basis because it appears that SEQ ID NOs 330 and 331 already comprise linked ATPase and deaminase pairs but are recited in the claim to further comprise an additional ATPase and/or deaminase (i.e., SEQ ID NOs 173 and 174). It is unclear to which ATPase and deaminase is being referred by recited “the ATPase and deaminase are linked together,” and whether or not SEQ ID NO: 331, which comprises an ATPase and deaminase per the specification at Table 15A satisfies such a linking requirement, or if SEQ ID NO: 331 must be further linked with SEQ ID NO: 173. The same issue exists for the other pair recited in the claim (i.e., SEQ ID NO: 330 and 174).
Claims 2-10 and 51-53 depend from claim 1 and do not resolve this 112(b) issue. These claims are therefore also rejected.
Regarding claim 24, claim 24 recites that the ATPase comprises, for instance, one of SEQ ID NOs 328 or 330. SEQ ID NO 328 is recited in the 6th row of Table 15C on page 196, which corresponds to row 27 of Table 15A. Table 15A recites that row 27 comprises an “ATPase + deaminase.” Thus, SEQ ID NO: 328 is recited in the specification to comprise an ATPase and a deaminase. Claim 24 is unclear because it recites SEQ ID NO: 328 as being only an ATPase. The same issue exists for SEQ ID NO: 330, which is discussed in the rejection of claim 1.
Regarding claim 32, claim 32 recites “the N-terminal effector domain,” (final line). However, claim 32 recites that “at least two” of the proteins are linked together. Thus, claim 32 is broadly drawn to an engineered system which could comprise multiple, separate proteins and/or combinations of proteins. It is therefore unclear to which N-terminal domain is being referred to, as “at least two of the proteins are linked together” implies that the remaining proteins can be “unlinked” (i.e., separate proteins, which would comprise a separate N-termina domain from the “linked” proteins). The phrase “the N-terminal effector domain” therefore lacks proper antecedent basis because it is unclear to which N-terminal domain is being referred in the claim (i.e., the N-terminus of the linked proteins, the unlinked proteins?).
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.
Claims 3-4 are 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.
Regarding claims 3 and 4, these claims recite that the ATPase or deaminase is 1100 residues or fewer. However, the ATPases and deaminases recited in claim 1 (i.e., SEQ ID NOs 173-174 and 330-331), from which claims 3-4 depend, comprise lengths of 851, 856, 907, 914, respectively (SEQ ID NOs 173-174 and 330-331). Thus, claim 1 recites ATPases and deaminases which are shorter than 1100 amino acid residues. Claims 3-4 therefore do not limit the scope of claim 1 because they in fact expand the length of the recited residues to comprise additional amino acids.
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.
New Rejection Not Necessitated by Amendment
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.
Claims 3-6, 10, 15, and 32 are 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 claim(s) contains 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Regarding claim 3, claim recites “the ATPase comprises 1100 or fewer amino acid residues.” Claim 3 depends from claim 1 which recites two ATPases: SEQ ID NO: 173 and 330. SEQ ID NO 173 is 851 amino acids in length where SEQ ID NO: 330 is 907 amino acids in length. The specification does not describe any other sequences comprising either of these two sequences with any additional residues. The Applicant has therefore not shown possession of any ATPases which are, for instance, 1100 amino acid residues in length, an embodiment encompassed by the scope of the claim.
Additionally, BLAST sequence searches do not return any sequences comprising either SEQ ID NO: 173 or SEQ ID NO: 330 where the result further comprises additional sequences to a total of 1100 residues. Thus, the Applicant has not shown any sequences of this length and such sequences are furthermore not characterized in the art. The Applicant has therefore not shown possession of the genus of ATPase claimed in claim 3, as no such sequences are known either in the art or shown in the specification.
Regarding claim 4, claim 4 suffers a similar problem as that discussed in the rejection of claim 3. Claim 4 recites “the adenosine deaminase comprises 1100 or fewer amino acid residues,” and therefore encompasses adenosine deaminases which are 1100 amino acids in length. Claim 4 depends from claim 1, where the two deaminases recited are SEQ ID NOs are 331 and 174, which are 914 and 856 residues in length, respectively. The specification does not recite additional sequences which comprises either SEQ ID NOs 331 and 174 with additional residues to total a length of 1100 residues. The Applicant has therefore not described any additional adenosine deaminases which read on the scope of the claim. For instance, the Applicant has not described deaminases which are over 1,000 residues in length but only appears to describe SEQ ID NOs 331 and 174 to read on the present claims. Thus, the Applicant has not shown possession of the recited genus.
Additionally, NCBI BLAST searches of SEQ ID NOs 331 and 174 do not return any hits to known deaminases which match the recited sequences and comprise additional sequences. Thus, no such sequences appear to be known in the art, where the deaminase comprises either SEQ ID NO: 331 or 174 with additional residues. The Applicant was therefore not in possession of the recited genus of deaminases, as they have not recited any such sequences and furthermore such sequences are not known in the art to exist.
Regarding claim 5, claim 5 is directed to the engineered system of claim 1, where claim 5 is further claiming the broad genus of “membrane” protein. Thus, claim 5 broadly encompasses an engineered system comprising the ATPase and adenosine deaminase combinations recited in claim 1 in addition to any membrane protein. This claim language is problematic because the genus “membrane protein” comprises several classes of unpredictable and uncharacterized proteins, which furthermore the specification does not show possession of sufficient species to characterize such a genus. Furthermore, the rejection of the genus “membrane protein” was introduced in the original rejection mailed 3/29/2023; the Applicant did not address the rejection of the genus “membrane protein.”
In the present application, the applicant used a systematic approach to discover novel defense genes in bacteria. The method to discover said defense genes involved examining regions of bacterial and archaeal genomes (174,080 genomes in total, first paragraph of Methods, page 113). Candidate novel defense genes were determined by their proximity to known defense systems, wherein candidate genes were given a defense score and, based on said defense score, were either further evaluated or not evaluated. As stated on page 105, paragraph 0235, “applicants identified a diverse set of putative defense gene cassettes that remain functionally uncharacterized.” Furthermore, paragraph 0235 of the specification states “applicants heterologously reconstituted 50 of these cassettes in Escherichia coli, demonstrating that 29 of them mediated defense against specific bacteriophages.” The applicant has therefore sought to characterize uncharacterized gene cassettes, and has shown that heterologous expression of these cassettes does not always work in mediating defense against bacteriophages. Therefore, the specification shows an inherent unpredictability regarding the predictions of functions of the identified the gene cassettes.
Regarding claims 5 and 6, and the recitation of “a membrane protein”, the specification recites, in paragraph 0243, that “in some cases, this system had the ATPase and deaminase only, but some variants also included a small membrane protein, either a SLATT domain or the type VI-B CRISPR ancillary gene csx27.” The specification therefore teaches that not all systems require both ATPases and membrane proteins. Given the wide extent of the search conducted by the applicant, which essentially included every bacterial and archaeal genome in the NCBI database, and the relatively small number of predicted defense systems tested in the specification and the fact that the specification states that “some” variants, but not all, included a small membrane protein, there is uncertainty as to what role small membrane proteins, and furthermore which membrane proteins, play in the potential systems recited in the specification and claims. The specification itself states that not all systems have small membrane proteins (above), which means that their role is still uncharacterized in the bacterial defense systems described. The genus “membrane protein” and its role in the present invention is therefore not adequately described by the applicant.
Furthermore, it is known in the art that the genus of “membrane protein” and the domains comprised by membrane proteins are a diverse class of protein which is not fully characterized or predictable. For instance, membrane proteins reasonably include eurkaryotic membrane proteins such as ion channels, which were not evaluated in the present context of the invention. It is unclear and unknown what a mammalian membrane protein such as an ion channel may play in a bacterial defense system, where the Applicant has not identified or characterized such a class of protein with structure-function relationships to show possession of the claimed genus. For instance, Catterall (Catterall WA. Trends Neurosci. 1993 Dec;16(12):500-6) is a review article focused on the structure and function of voltage-gated ion channels (Title, Abstract, and throughout). Catterall teaches the class of membrane protein known as synaptic membrane proteins (page 510, first paragraph). Catterall teaches the role of calcium channels in neuronal synapses (page 510, first paragraph). Thus, Catterall teaches that membrane proteins are found within higher order eukaryotes and comprise functions which are completely unrelated to bacterial defense proteins, ATPases, and/or adenosine deaminases such as those proteins recited in claim 1, from which claim 5 depends. The Applicant has not characterized or taught specific structure-function relationships between such bacterial proteins as those which are claimed, and how such proteins would interact with the widely variable group of proteins such as “membrane proteins,” which includes proteins with totally unrelated functions derived from different kingdoms of organisms.
Furthermore, bacterial membrane proteins are similarly widely diverse in structure and function. For instance, Yuan (Yuan J et al. Microlife. 2025 Nov 7;6:uqaf035) is a review article which teaches the functional diversity of small membrane proteins in bacteria (Title, Abstract, and throughout). Yuan teaches that:
“Bacteria constantly adapt to changing environmental conditions through diverse processes that involve numerous regulator and effector proteins. In this regard, small proteins play a significant role in promoting stress adaptation in bacteria. Although they were largely overlooked in early genome annotations, recent technological advances and a growing recognition of their significance have paved the way for the increasing identification and characterization of this intriguing class of proteins. Many small proteins contain a transmembrane domain and are integral to the cytoplasmic membrane. Others interact with and modulate membrane protein complexes,” (Abstract)
Thus, Yuan teaches that specific classes of membrane proteins, such as small membrane proteins, are still being characterized post-filing of the present application, where furthermore such proteins have a diverse structures and functions within the cell which are not fully characterized (above). Thus, the Applicant has not only not shown possession of the class “membrane protein,” which comprises eukaryotic membrane proteins, but has furthermore not characterized or shown sufficient possession of the genus of bacterial membrane proteins.
Furthermore, regarding claim 6, membrane proteins comprising SLATT domains are similarly not fully characterized within the context of bacterial cells. For instance, Burroughs (Burroughs AM et al.Nucleic Acids Res. 2015 Dec 15;43(22):10633-54) teaches that:
“A previously-uncharacterized superfamily of domains with two transmembrane (TM) helices was found to frequently link the SMODS and SLOG domains in the contextual network. This domain has representatives in most major bacterial lineages, some eukaryotes and Nucleo-Cytoplasmic Large DNA viruses (NCLDVs). While a subset of the superfamily is detected by the DUF4231 model (Domain of Unknown Function) from the Pfam database, a major fraction of this family as defined by us was not captured by this model. Multiple alignments revealed a conserved core for the domain consisting of a pair of N-terminal TM helices and a largely helical C-terminal cytoplasmic region. We accordingly term the expanded superfamily the SLATT (for SMODS and LOG-Smf/DprAAssociating Two TM) domain. Clustering analysis identified
seven monophyletic families of SLATT domains, of which five are critical components of systems we uncovered. The TM helices often contain family-specific polar residues that are likely to form an intramembrane aqueous channel that might facilitate transport of molecules across the membrane. Of the two families of SLATT domains that do not seem to occur in nucleotide centric systems, one tends to be encoded by solo genes bereft of genomic context in bacteria. The other occurs in several fungi and is typically lineage-specifically expanded in them (page 10638, final paragraph to page 10640, first paragraph).
Thus, Burroughs teaches that the SLATT domain is relatively uncharacterized, spans multiple organism taxonomies with undefined roles in bacterial defense systems (e.g., eukaryotes and fungi). Burrough further teaches that modeling does not always capture major fractions of defined family of proteins, which places further uncertainty on the class as a whole (above). Burroughs further teaches that entire subfamilies of SLATT domain proteins are “bereft of genomic context in bacteria,” (above), which places even greater burden on the Applicant to fully characterize such domains as the SLATT domain as claimed in claim 6.
Taken together, the genus of “membrane protein” as presently claimed includes a broad and uncharacterized genus spanning almost all classes of organisms, where such proteins play diverse and unpredictable roles in the presently recited context, where such membrane proteins are recited in engineered systems comprising bacterial ATPases and adenosine deaminases, as recited in independent claim 1. The Applicant has not shown sufficient possession of the genus recited.
Regarding claim 10, claim 10 recites broadly uncharacterized and unpredictable genera of phage proteins such as gp50, where the Applicant has not shown sufficient species commensurate in scope to show possession of the genus of, for instance, the phage protein gp50. It is known in the art that the phage protein “gp50” is a diverse class of proteins. For instance, Bellis (Bellis NF et al. Res Sq [Preprint]. 2025 Oct 21:rs.3.rs-7746245) is a research article which teaches the gp50 protein of bacteriophage N4 (Title, Abstract, and throughout). Bellis teaches that:
“Here, we present an integrative structural analysis of the coliphage N4 vRNAP (gp50). We find that this 383 kDa enzyme is a multi-domain, single-chain RNA polymerase, structurally distinct from both compact single-chain RNAPs and large multi subunit holoenzymes. vRNAP is composed of loosely connected domains and exhibits an intramolecular mode of allosteric regulation through its C-terminal domain. Comparative analysis of intact and genome-released virions identified gp51, which forms an outer-membrane complex, and gp52, which assembles a periplasmic tunnel. These proteins generate heterogeneous pores that facilitate the release of vRNAP,” (Abstract)
Thus, Bellis teaches that vRNAP (i.e., gp50) of the phage N4 is a multi-domain with structurally distinct characteristics, which furthermore is known to act in protein complexes with additional characteristics and functionality (above).
Bellis further teaches that:
“In stark contrast to the N4 transcriptional program, which has been studied extensively, many key questions about the role of phage N4 vRNAP [gp50] as an ejection protein and its part in the DNA ejectosome remain unanswered. vRNAP (gp50) consists of three predicted domains: a likely membrane-spanning N-terminal domain (NTD), a single subunit RNA polymerase (RNAP) domain, and a large C-terminal domain of unknown function,” (page 3, second paragraph).
Thus, Bellis teaches that the role and function of N4’s vRNAP (i.e., gp50) remain unclear, where furthermore the protein is taught to comprise only “predicted” domains, one of which is a domain of unknown function. Thus, the genus of phage protein “gp50” is unpredictable and uncharacterized in the art, as Bellis teaches that such gp50 proteins comprises unknown functional-structural relationships, where furthermore such unpredictability and complexity is compounded by the fact that such gp50 proteins are recited in context of the ATPase and deaminases recited in claim 1. For instance, the exact role and function of N4’s gp50 protein in this context is unknown and as taught by Bellis unpredictable. The Applicant has not characterized the recited phage proteins in claim 10 sufficient to show possession of the genus as a whole.
Regarding claim 15, claim 15 broadly claims the genus of “a nitrrilase.” The Applicant has not characterized the genus of nitrilase sufficiently to show possession of the scope of the claim, as the specification has not offered representative species of this diverse and unpredictable genus of enzymes. Regarding the genus of “nitrilase,” it is known in the art that this genus is highly diverse and uncharacterized. For instance, Pace (Pace HC et al. Genome Biol. 2001;2(1):REVIEWS0001) teaches that:
“The nitrilase superfamily consists of thiol enzymes involved in natural product biosynthesis and posttranslational modification in plants, animals, fungi and certain prokaryotes. On the basis of sequence similarity and the presence of additional domains, the superfamily can be classified into 13 branches, nine of which have known or deduced specificity for specific nitrile- or amide-hydrolysis or amide condensation reactions. Genetic and biochemical analysis of the family members and their associated domains assists in predicting the localization, specificity and cell biology of hundreds of uncharacterized protein sequences,” (Abstract).
Thus, Pace teaches that the nitrilase superfamily comprises hundreds of uncharacterized proteins, where the individual families have not been deduced with specificity/function, and furthermore where the family spans plants, animals, fungi, and prokaryotes. Thus, Pace teaches that the genus of “nitrilase” is an enormous genus of protein, where furthermore the Applicant has not shown any structural/functional relationship to nitrilases in the recited context of UG transcriptases (claim 15).
Pace teaches father unpredictability and characterization of the broad genus of nitrilase, teaching that:
“Automated sequence searching easily identifies predicted polypeptides as members of the nitrilase superfamily, but many database annotations have been applied haphazardly. Because members of the nitrilase superfamily are reported to be nitrilases, aliphatic amidases, β-ureidopropionases, β-alanine synthases, N-carbamyl-D-amino acid amidohydrolases and so on, these designations appear in the sequence definition lines of multiple databases, often irrespective of the activity of the most closely related characterized enzyme ,” (page 2, left column, second paragraph).
Thus, Pace teaches that the genus of “nitrilase” spans multiple domains of life and is relatively uncharacterized. Furthermore, the Applicant has not reduced to practice representative species to show possession of this broad genus, and has not identified structure-function relationships between, for instance, animal nitrilases and putative bacterial defense systems such as what the present application is directed to.
Regarding claim 32, claim 32 recites the broad and uncharacterized genus of “trypsin like-serine protease” which is a “putative effector domain.” With regards to the genus of “putative effector,” such a genus of protein is inherently uncharacterized, as “putative” effector domains are not established domains. The term “putative” is inherently speculative, where furthermore no clear determination of what such a “putative” domain would be is offered or defined with a connection to the serine protease. The Applicant did not demonstrate possession in the specification, drawings, or claims; there is no defined structure-functional relationship between the recited “putative effector” taught or recited in the specification or literature, where such a genus of protein is itself recited to be only potentially (i.e., “putatively”) an effector domain.
Furthermore, claim 32 lists 19 separate sequences, where the claim recites such sequences in any combination. Given that the genus of “putative effector” is undefined, the claimed sequences are furthermore uncharacterized in the context of the claim where it is unclear what role or influence such “putative” domains would have in the different possible combinations of proteins/domains recited in claim 32.
Furthermore, the Applicant has recited a “helical domain” with the recited functionality of being a C-terminal helical sensor domain that is induced to oligomerization upon target recognition leading to the activation of the N-terminal effector domain. The Applicant has not characterized or identified a function-structure relationship of such “helical domains,” where furthermore the protein structures claimed in claim 32 can be in any order. For instance, any such domain of the recited domains can be at the N-terminal portion of the protein; the applicant has not identified or defined a structure-function relationship between a helical domain which can function to activate each of an NTPase STAND superfamily, DUF4297, Mrr-like nuclease, SIR2, and/or a trypsin-like serine protease which is a “putative effector domain,” any of which could be the N-terminal domain as presently recited. Claim 32 is thus broadly claiming an undefined class of potential proteins which are furthermore recited to be used in combination with one another to function as an “engineered system.” It is suggested that the Applicant amend claim 32 to reflect combinations of proteins/domains and sequences of the helical domains/putative effector domains which were both taught and reduced to practice within the specification to obviate the 112(a) rejection regarding claim 32.
Response to Arguments
The Applicant argues that the claim amendments place the present claim set in condition for allowance. This argument is in part persuasive for claims 1,3-4,7-9, 12, 23-24, and 51-53, as the Applicant’s amendments address the original 112(a) issue surrounding the phrase “an amino acid” sequence (see non-final mailed 7/28/2025). However, upon further consideration, dependent claims within the claim set appear to recite uncharacterized genera of protein classes. As such, a new 112(a) written description is presented.
Regarding claim 32, while claim 32 is drawn to material originally elected and presented, the new amendments have prompted an additional 112(a) rejection set forth above. Thus, the Applicant’s amendments are not sufficient to place the claims in condition for allowance for the reasons detailed above in the 112(a) rejections.
Allowable Subject Matter
Claim 12 and 23 are allowed.
Regarding claims 12, and 23, these claims are drawn to engineered systems comprising reverse transcriptases selected from UG3, UG8, UG1, UG2, UG15, and UG16, where UG3 and UG8 are required components of the claim as well as one or more of UG1, UG2, UG15, and UG16. The transcriptases are further recited to be “linked.” The prior art does not reasonably suggest such reverse transcriptase linkages. Furthermore, each combination of linkages was searched in NCBI BLAST, and such a linked protein was found to be non-naturally occurring. For instance, the combination of UG1+UG3+UG8, UG3+UG1+UG8, UG3+UG8+UG1 was searched and was not found a naturally occurring protein. Similar NCBI BLAST searches were performed for UG2, UG15, and UG16, as well as reversing the order of UG3 and UG8 (i.e, “UG8+UG3”) in the ordering of the sequences. The search results revealed that the recited engineered systems, which require UG3, UG8, and one or more of UG1, UG2, UG15, and UG16 to be directly linked to one another to be non-naturally occurring. Furthermore, the Applicants appear to have reduced such reverse transcriptases to practice and shown efficacy in reducing phage infection in E. coli (Examples 2 and 3, page 110 first two paragraphs and pages 145-146, Figures 9B and17D). Additionally, although the Applicants did not show every combination of “UG” element, the claims require at minimum UG3+UG8 and one additional UG element selected from four. It appears that a practitioner would reasonably be enabled to elect a workable combination from the sequences recited.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DOUGLAS CHARLES RYAN whose telephone number is (571)272-8406. The examiner can normally be reached M-F 8AM - 5PM.
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/D.C.R./Examiner, Art Unit 1635
/RAM R SHUKLA/Supervisory Patent Examiner, Art Unit 1635