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 . 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.
Election/Restrictions
Applicants elected SEQ ID 19 without traverse in the reply filed on 10 Aug, 2025.
Claims Status
Claims 1, 2, 7, 8, 10-12, 15, 18, 19, 23, 24, 41-43, 47-50, 55, 56, 58-60, 63, 66, 67, 71, and 72 are pending.
Claims 1, 10-12, 43, 49, and 58-60 have been amended.
Claims 2, 7, 8, 10, 11, 23, 47, 50, 55, 56, 58, 59, and 71 have been withdrawn from consideration due to an election/restriction requirement.
Withdrawn Objections
The objection to the disclosure due to embedded hyperlinks is hereby withdrawn due to amendment.
New Objections
Claim Objections
Claims 1 and 49 are objected to because of the following informalities: These claims list a polypeptide sequence, but not the SEQ ID number. The MPEP states that "37 CFR 1.821(d) requires the use of the assigned sequence identifier in all instances where the description or claims of a patent application discuss sequences regardless of whether a given sequence is also embedded in the text of the description or claims of an application” (MPEP 2422.03). Appropriate correction is required.
Information Disclosure Statement
The information disclosure statement filed 5 Jan, 2026 fails to comply with 37 CFR 1.98(a)(2), which requires a legible copy of each cited foreign patent document; each non-patent literature publication or that portion which caused it to be listed; and all other information or that portion which caused it to be listed. The two documents cited in this information disclosure statement were of too poor a resolution to be read. Thus, they were not considered. Note that when documents are uploaded to the server, they are converted to a different file format, with loss of resolution. While the documents that were uploaded may have been legible, the ones in the application data file are not.
Withdrawn Rejections
The rejection of claims 1, 4, 5, 12, 15, 18, 19, 24, 41-43, 48, 49, 52, 53, 60, 63, 66, 67, and 72 under 35 U.S.C. 112(a) due to issues knowing which mutants have catalytic activity is hereby withdrawn due to amendment.
The rejection of claims 1, 4, 5, 12, 15, 18, 19, 24, 41-43, 48, 49, 52, 53, 60, 63, 66, 67, and 72 under 35 U.S.C. 112(b) due to uncertainty in what is tested for catalytic activity is hereby withdrawn due to amendment.
The rejection of claims 1, 12, 24, 41, 42, 48, 49, 60, and 72 under 35 U.S.C. 102(a)(1) as being anticipated by Lei et al (BioRxive preprint, 2 Feb, 2020 is hereby withdrawn due to amendment.
The rejection of claim(s) 1, 12, 15, 24, 41, 42, 48, 49, 60, 63, and 72 under 35 U.S.C. 103 as unpatentable over Lei et al (BioRxive preprint, 2 Feb, 2020, cited by applicants), in view of Cosman et al (Immunity (1997) 7 p273-282) is hereby withdrawn due to amendment.
Claim(s) 1, 4, 5, 12, 15, 24, 41, 42, 48, 49, 52, 53, 60, 63, and 72 are rejected under 35 U.S.C. 103 as unpatentable over Lei et al (BioRxive preprint, 2 Feb, 2020, cited by applicants), in view of Cosman et al (Immunity (1997) 7 p273-282) and Guy et al (FEBS J. (2005) 272 p3512-3520) is hereby withdrawn due to amendment.
Maintained/Modified Rejections
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1, 12, 18, 24, 41, 42, 48, 49, 60, 66, and 72 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
The rejected claims all require a linker between a mutated ACE2 extracellular domain and an antibody Fc domain, which can be mutated from the native sequence, but applicants have not defined this linker save that some dependent claims specify a number of amino acids. This means that the cutoff between the ACE2 fragment and portions other than the ACE2 fragment, the Fc region and not-Fc region, and linker and not-linker is arbitrary. A linker could be considered part of the ACE2 fragment or the Fc domain, or parts of the Fc domain or the ACE2 fragment could be considered a linker – the difference is entirely in the head of the person making the construct.
response to applicant’s arguments
Applicants state that they have rewritten the independent claims to make clear the extent of the ACE2 receptor and the linker.
Applicant's arguments filed 21 Jan, 2026 have been fully considered but they are not persuasive.
Applicants have amended claims 1 and 49 to require that the ACE2 extracellular domain comprise a given sequence. This means that additional amino acids can be added to either end and still be considered part of the extracellular domain of ACE2. There is no definition of the Fc domain, save that it is an Fc domain, and can be mutated. This does not give a clear definition of where the various domains begin and end.
Claim Rejections - 35 USC § 103
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
first rejection
Claim(s) 1, 12, 15, 24, 41, 42, 48, 49, 60, 63, and 72 are rejected under 35 U.S.C. 103 as unpatentable over Lei et al (BioRxive preprint, 2 Feb, 2020, cited by applicants), in view of Cosman et al (Immunity (1997) 7 p273-282) and Guy et al (FEBS J. (2005) 272 p3512-3520)
Lei discusses neutralization of COVID 19 with recombinant ACE2-Ig (title), where ACE2 was attached to an antibody Fc domain (abstract). This ACE2 domain was the extracellular domain with H374 and H378 mutated to asparagine to reduce catalytic activity (3d page, 3d paragraph). Material was injected into mice (6th page, 2nd paragraph), which requires a pharmaceutical composition.
The difference between this reference and the examined claims is that this reference does not mention the H345 mutation, nor does it describe the linker.
Cosman et al discuss the interactions of the LIR-1 receptor (abstract). To rule out the possibility that the receptor was binding to the Fc domain of the construct used for testing, the extracellular domain of the LIR-1 receptor was fused to an antibody Fc domain (p274, 2nd column, 3d paragraph). This construct was made with a factor Xa cleavage site as a linker, with the sequence IEGR (p280, 1st column, 2nd paragraph). This reference discusses an IEGR linker in the context of a fusion protein with an antibody Fc domain.
Guy et al discusses the critical active site residues in ACE2 (title). His345 plays a key role in binding of the substrate in the active site (p3514, 2nd column, 2nd paragraph). A variant with an H345A mutation was made, and determined to have about two orders of magnitude less catalytic activity than the native sequence (p3514, 1st column, 1st paragraph, fig 2, p3514, 1st column, top of page, and table 1, p3514, 2nd column, top of page). This reference discusses alternative ACE2 variants with greatly reduced activity.
Therefore, it would be obvious to link the ACE2 domain of Lei et al to the Fc domain with an IEGR linker, to include a factor Xa cleavage site to allow for cleavage of the two domains. As Cosman et al discuss a fusion protein with an antibody Fc domain and this linker, an artisan in this field would attempt this modification with a reasonable expectation of success.
Furthermore, it would be obvious to substitute the ACE2 variant of Lei et al with the ACE2 variant of Guy et al, as a substitution of one known element (the sequence of Lei et al) for another (the sequence of Guy et al) yielding expected results (an inactive ACE2). As Guy et al demonstrate lowered activity, an artisan in this field would attempt this mutation with a reasonable expectation of success. While the reference does not state that this variant has increased neutralization of SARS-CoV-2 viral infection compared to the wild type, given the mutation rate of the spike protein, there necessarily must be a variant of the protein for which this holds.
response to applicant’s arguments
Applicants argue that the rejection does not meet the newly added limitation that the fusion protein exhibit increased neutralization of SARS-CoV-2 than a construct with the wild type ACE2 receptor.
Applicant's arguments filed 21 Jan, 2026 have been fully considered but they are not persuasive.
The rejection has been amended to take this limitation into account.
second rejection
Claim(s) 1 , 12, 15, 18, 19, 24, 41-43, 48, 60, 63, 66, 67, and 72 are rejected under 35 U.S.C. 103 as unpatentable over Lei et al (BioRxive preprint, 2 Feb, 2020, cited by applicants), in view of Cosman et al (Immunity (1997) 7 p273-282), Guy et al (FEBS J. (2005) 272 p3512-3520) and Graus et al (US 20050226876).
Lei discusses neutralization of COVID 19 with recombinant ACE2-Ig (title), where ACE2 was attached to an antibody Fc domain (abstract). This ACE2 domain was the extracellular domain with H374 and H378 mutated to asparagine to reduce catalytic activity (3d page, 3d paragraph). Material was injected into mice (6th page, 2nd paragraph), which requires a pharmaceutical composition.
Cosman et al discuss the interactions of the LIR-1 receptor (abstract). To rule out the possibility that the receptor was binding to the Fc domain of the construct used for testing, the extracellular domain of the LIR-1 receptor was fused to an antibody Fc domain (p274, 2nd column, 3d paragraph). This construct was made with a factor Xa cleavage site as a linker, with the sequence IEGR (p280, 1st column, 2nd paragraph). This reference discusses an IEGR linker in the context of a fusion protein with an antibody Fc domain.
Guy et al discusses the critical active site residues in ACE2 (title). His345 plays a key role in binding of the substrate in the active site (p3514, 2nd column, 2nd paragraph). A variant with an H345A mutation was made, and determined to have about two orders of magnitude less catalytic activity than the native sequence (p3514, 1st column, 1st paragraph, fig 2, p3514, 1st column, top of page, and table 1, p3514, 2nd column, top of page). This reference discusses alternative ACE2 variants with greatly reduced activity.
As noted above, these references render obvious claims 1, 12, 15, 24, 41, 42, 48, 49, 52, 53, 60, 63, and 72.
The difference between these references and the remaining claims is that these references do not discuss a modified antibody Fc domain with two Leu residues mutated to Ala residues.
Graus et al discuss antibodies (title), and variants that do not bind to the human Fcγ receptor on NK cells or the C1q receptor (paragraph 6). This can avoid activating the complement cascade (paragraph 52). An example of an antibody heavy chain that doesn’t bind to these receptors is SEQ ID 26 (paragraph 84). Note that this sequence comprises an antibody Fc domain identical with that of applicant’s elected species.
Therefore, it would be obvious to use the antibody Fc domain of Graus et al in the construct of Lei et al, to reduce binding to the Fcγ receptor and the C1q receptor, as described by Graus et al. As Graus et al state that this sequence is effective in an antibody, an artisan in this field would attempt this modification with a reasonable expectation of success.
response to applicant’s arguments
Applicants have used the same arguments for all rejections under this statute, which were answered above.
New Rejections
Claim Rejections - 35 USC § 112(a)
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.
first rejection, written description
Claims 1, 12, 15, 18, 19, 24, 41-43, 48, 49, 60, 63, 66, 67, and 72 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.
The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include "level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient" (MPEP 2163).
A claimed genus may be satisfied through sufficient description of a representative number of species or disclosure of relevant, identifying characteristics such as functional characteristics coupled with a known or disclosed correlation between function and structure(MPEP 2163(3)a(II)). The number of species that describe the genus must be adequate to describe the entire genus; if there is substantial variability, a large number of species must be described.
The analysis for adequate written description considers (a) actual reduction to practice, (b) disclosure of drawings or structural chemical formulas, (c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties or functional characteristics when coupled with known or disclosed correlation with structure and (d) representative number of samples.
The issue is if a person of skill in the art would know which embodiments have increased neutralization compared to a construct comprising the wild type extracellular domain of the human ACE2 receptor and an Fc domain.
(a and b) actual reduction to practice and disclosure of drawings or structural chemical formulas: Applicants use four different sequences; WT, R273A, H345A, and the dual mutant R273A/H345A (paragraph 44). They all used the same linker, SEQ ID 2 (paragraph 61), and LALA mutations in the Fc domain (paragraph 63). These constructs gave similar results in an in-vitro neutralization assay (fig 3), and it is not clear if the results are statistically significant.
(c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties or functional characteristics when coupled with known or disclosed correlation with structure: Applicants are claiming a construct with mutations at position 345 of the ACE2 receptor, with a limitation of increased neutralization of SARS-CoV-2 compared to a wild type construct. This is a functional requirement that the claimed construct be more effective than a construct comprising the wild type extracellular domain and an Fc domain. However, applicants have not described what is required to meet this functional limitation. A person of skill in the art would not know which of the claimed embodiments will meet this functional requirement. In essence, applicants have described their invention by function. That is not sufficient to meet the written description requirement.
It is well known in the art that linkers in fusion proteins can affect a number of parameters, such as biological activity, pharmacokinetic profiles, and expression yield (Chen et al, Adv. Drug Deliv. Rev. (2013) 65(10) p1357-1369, abstract). Note that the reference explicitly discusses Fc conjugates, and how they can improve plasma half lives and therapeutic effects (1st page, 1st paragraph). Linkers affect folding and bioactivity, and selection of a proper linker can be complicated (2nd page, 2nd paragraph). Note that, to affect biological activity, the linker must interact with the active protein; presumably, a mutated active protein can interact differently.
As of applicant’s priority date, it was not possible to predict if a given molecule bound to a receptor. Lowe (blog “In the pipeline” entry of 7 Sept, 2022) describes an experiment where that was attempted. 39K compounds, including known antibiotics, were screened against E. coli for growth inhibition, finding 218 active compounds (1st page, 3d paragraph). These were computer docked to a set of 296 essential bacterial proteins by multiple docking procedures (1st page, 3d paragraph), along with 100 random inactive compounds (2nd page, 1st paragraph). The number of strong binders predicted were essentially the same between the active compounds and the controls, and out of 142 compound/target interactions previously known, the methodology found only 3 (2nd page, 2nd paragraph). While a given docking program may accurately predict if compound A binds to protein B, it is impossible to a priori know if the prediction is accurate. In other words, several years after applicant’s priority date, it was not possible to predict if a given compound and target bound to each other.
Nor is it possible to modify known sequences to reliably find new compounds. Guo et al (PNAS (2004) 101(25) p9205-9210) looked at the effect of random mutations (title). In a DNA repair enzyme, about one mutation in three killed the activity of the protein, consistent with studies with other proteins (abstract). Yampolsky et al (Genetics (2006) 170 p1459-1472), using a different methodology, found that even conservative substitutions were prone to problems (table 3, p1465, top of page). In other words, unless there is some information known about the binding, mutating the sequence is likely to be detrimental. Note that the strain of SARS CoV-2 is not specified (see rejection under 35 USC 112(b), below), so this applies to mutations of the ACE2 receptor domain, linker, Fc domain, AND spike protein.
(d) representative number of samples: Applicants describe 1 sequence that meets the structural limitations of the claim, and it is not clear that it meets the functional requirement based on applicant’s tests. The prior art clearly shows that the linker is critical for activity, and suggests that the Fc domain is as well. It is also established that mutations tend to be detrimental – and both the claimed protein and what it binds to can be mutated. Together, this indicates that applicants lack written description for this limitation.
second rejection, new matter
Claims 1, 12, 15, 18, 19, 24, 41-43, 48, 49, 60, 63, 66, 67, and 72 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.
Claims 1 and 49, and claims dependent on them, requires that the extracellular ACE2 domain comprise a polypeptide which appears to be SEQ ID 1 with the N-terminal 19 amino acids deleted. Applicants state that the first 17 or 18 amino acids are a leader sequence that is cleaved in vivo during natural production in the body (paragraph 40). However, nowhere is there a description of SEQ ID 1 with the N-terminal 19 amino acids deleted. Thus, this sequence constitutes new matter.
Claim Rejections - 35 USC § 112(b)
The legal basis for rejections under this statute was given above, and will not be repeated here.
Claims 1, 12, 15, 18, 19, 24, 41-43, 48, 49, 60, 63, 66, 67, and 72 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.
Claims 1 and 49, and claims dependent on it, require that the claimed constructs exhibit increased neutralization of SARS-CoV-2 viral infection compared to a fusion protein comprising a wild type extracellular domain of human ACE2 and a Fc region. There are a number of issues with this limitation.
First issue is that the SARS-CoV-2 strain is not specified. According to Ataya et al (Sci. Rep. (2025) 15:37546), this virus mutates rapidly, especially at the spike protein (2nd page, 1st paragraph) which is where the ACE2 receptor binds. As noted in the written description rejection, this is likely to make a difference in binding.
Second, the control construct is not defined. It requires the wild type extracellular ACE2 domain, but it is not clear exactly what applicants consider this to be – note that the leader sequence can be 17 or 18 amino acids (paragraph 40), or that the entirety of SEQ ID 1 is the extracellular domain (note the language of paragraph 44). There is no mention of a linker, except for the open language (“comprising”) describing the construct, and the Fc domain is not described at all. And, as the language is open, additional elements can be added that affect binding.
Third, it is not clear how to test for increased neutralization. Applicants used an in-vitro test. However, in-vitro testing will not necessarily give the same results as in-vivo, as there is no ADME effects in vitro, and the in-vivo subject can give different results depending on the test animal, otherwise, there’d be no need to hold human clinical trials.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 19, 43, and 67 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. Claims 1 and 49 require that the construct comprise a specific sequence with one position mutated. However, the rejected claims describe embodiments with two positions mutated. 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.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to FRED REYNOLDS whose telephone number is (571)270-7214. The examiner can normally be reached M-Th 9-3:30.
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/FRED H REYNOLDS/Primary Examiner, Art Unit 1658