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 .
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 10/08/2025 has been entered.
Amended claims 1, 4-10, 16, 22, 43-48 and new claims 49-50 are pending in the present application.
Applicant elected previously without traverse the following species: (a) an AAV5 vector; (b) a further encoded therapeutic polypeptide; (c) the cell-penetrating peptide comprising the amino acid sequence of SEQ ID NO:23; and (d) an IgK peptide as an N-terminal mammalian secretion signal peptide.
Accordingly, amended claims 1, 4-10, 16, 22 and 43-50 are examined on the merits herein with the above elected species.
Response to Amendment
1. The rejection under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, for New Matter was withdrawn in light of currently amended independent claims 1 and 43, particularly with the new limitation “a cell penetrating peptide consisting of the amino acid sequence of SEQ ID NO: 23 and a secretion signal peptide”.
2. Similarly, the rejection under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, for Lack of Written Description was withdrawn in light of currently amended independent claims 1 and 43, particularly with the new limitation “a cell penetrating peptide consisting of the amino acid sequence of SEQ ID NO: 23 and a secretion signal peptide”.
Claim Rejections - 35 USC § 112 (Lack of Written Description)
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.
New claims 49-50 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.
MPEP 2163 - 35 U.S.C. 112(a) and the first paragraph of pre-AIA 35 U.S.C. 112 require that the “specification shall contain a written description of the invention ....” This requirement is separate and distinct from the enablement requirement. Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1340, 94 USPQ2d 1161, 1167 (Fed. Cir. 2010) (en banc). Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111 (Fed. Cir. 1991), clearly states that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” Vas-Cath Inc. v. Mahurkar, 19USPQ2d at 1117. The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed” Vas-Cath Inc. v. Mahurkar, 19USPQ2d at 1116. This is a new ground of rejection.
The instant claims encompass a composition comprising an adeno-associated virus (AAV) particle, wherein the AAV particle comprises: (i) an AAV capsid protein selected from an AAV5 capsid protein, an AAV1 capsid protein, an AAV2 capsid protein, and an AAV2(quadY-F+T-V) capsid protein, and (ii) a polynucleotide that comprises: (a) a first nucleic acid segment that encodes a modified, virally-derived, M013 polypeptide; and (b) a second nucleic acid segment encoding a cell penetrating peptide consisting of the amino acid sequence set forth in SEQ ID NO: 23 and a secretion signal peptide; wherein the first and second nucleic acid segments are operably linked to a promoter sequence that is active in one or more mammalian cells comprising the polynucleotide; and wherein the secretion signal peptide comprises an N-terminal mammalian secretion signal peptide of any sequence and/or any length derived or obtained from any IgK peptide.
Apart from simply disclosing the sGFP-TatM013 vector plasmid was created by subcloning the TatM013 fusion construct downstream of IgK-GFP (IgG kappa light chain leader sequence fused to the GFP sequence) while maintaining the reading frame of these elements (paragraph [0137]; and Fig. 2A); the instant disclosure fails to provide sufficient/complete written description for any other N-terminal mammalian secretion signal peptide of any sequence and/or any length derived or obtained from any IgK peptide as encompassed broadly by the instant claims? For example, apart from the N-terminal secretory signal/leader sequence of the IgG kappa light chain which particular essential structural element(s) and/or critical structural component(s) do other N-terminal mammalian secretion signal peptides derived or obtained from any IgK peptide possess such that they still function as secretion signal peptides as compassed broadly by currently claims? Particularly, what are the specific sequences for 2-, 4-, 6-, 10-, 15- or more amino-acid-residue peptides of any IgK peptide that function as an N-terminal mammalian secretion signal peptide? Li et al (US 2012/0157513; IDS) merely taught using the secretion signal containing 21 amino acid residues derived from IgK signal sequence with the sequence of Met-Glu-Thr-Asp-Thr-Leu-Leu-Leu-Trp-Val-Leu-Leu-Leu-Trp-Val-Pro-Gly-Ser-Thr-Gly-Asp (paragraph [0062]). Since the prior art did not provide sufficient description and/or guidance regarding the above issue as evidenced at least by the teachings of Ali et al (US 2010/0081707), Li et al (US 2012/0157513; IDS) and Ildefonso et al (WO 2014/164703); it is incumbent upon the present specification to do so. The present application also fails to provide a representative number of species for a broad genus of a secretion signal peptide comprising an N-terminal mammalian secretion signal peptide of an IgK peptide for the composition and the polynucleotide as claimed broadly.
The claimed invention as a whole is not adequately described if the claims require essential or critical elements which are not adequately described in the specification and which are not conventional in the art as of Applicants’ filing date. Possession may be shown by actual reduction to practice, clear depiction of the invention in a detailed drawing, or by describing the invention with sufficient relevant identifying characteristics such that a person skilled in the art would recognize that the inventor had possession of the claimed invention. Pfaff v. Wells Electronics, Inc., 48 USPQ2d 1641, 1646 (1998). The skilled artisan cannot envision the complete detailed structure of a representative number of species for a broad genus of a secretion signal peptide comprising an N-terminal mammalian secretion signal peptide of an IgK peptide for the composition and the polynucleotide as claimed broadly, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method. Adequate written description requires more than a mere statement that it is part of the invention and reference to a method of isolating it. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (Fed. Cir. 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016 (Fed. Cir. 1991). One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481, 1483.
Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115).
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.
Amended claims 1, 5-10, 16, 22 and 43-50 are rejected under 35 U.S.C. 103 as being unpatentable over Ali et al (US 2010/0081707) in view of Ambati et al (WO 2013/012806; IDS), Rahman et al (PLoS Pathogens 5(10):e1000635.doi:10.1371/jornal.ppat.1000635, pages 1-14, 2009; IDS), Li et al (US 2012/0157513; IDS) and Mansbridge (US 7,160,726). This is a new ground of rejection.
The instant claims encompass a composition comprising an adeno-associated virus (AAV) particle, wherein the AAV particle comprises: (i) an AAV capsid protein selected from an AAV5 capsid protein, an AAV1 capsid protein, an AAV2 capsid protein, and an AAV2(quadY-F+T-V) capsid protein, and (ii) a polynucleotide that comprises: (a) a first nucleic acid segment that encodes a modified, virally-derived, M013 polypeptide; and (b) a second nucleic acid segment encoding a cell penetrating peptide consisting of the amino acid sequence set forth in SEQ ID NO: 23 and a secretion signal peptide; wherein the first and second nucleic acid segments are operably linked to a promoter sequence that is active in one or more mammalian cells comprising the polynucleotide.
Ali et al disclosed at least a rAAV vector composition formulated for administration by subretinal injection to treat various ocular disorders (e.g., autosomal recessive severe early-onset retinal degeneration, atrophic age-related macular degeneration, and intraocular inflammation) in a human, wherein the composition comprises a rAAV vector encoding a therapeutic polypeptide (e.g., anti-inflammatory factors such as IL-10, IL1-ra, TGFbeta and IL4A, neurotrophic factors such as GDNF, CNTF, FGF2, PEDF, EPO) or a therapeutic RNA, and the rAAV vector is encapsidated into a rAAV virus particle (see at least Abstract; particularly sections titled “Vectors for delivery of polynucleotides” and “Vector compositions” at paragraphs [0079]-[0090]). Ali et al also taught that the heterologous polynucleotide encoding a therapeutic polypeptide or a therapeutic RNA is flanked by two AAV ITRs (5’-AAV ITR and 3’-AAV ITR); the rAAV vector is derived from the genome of any AAV serotype, including AAV2, AAV4, AAV5, or AAV8, and being encapsidated by AAV capsid proteins derived from any AAV serotype (paragraphs [010]-[012], [0050]-[0055], [0081]; and exemplary Fig. 8). Ali et al also disclosed that the polynucleotides of the invention may encode polypeptides that are intracellular proteins, anchored in the cell membrane, remain within the cell, or are secreted by the cell transduced with the disclosed AAV vectors (paragraph [0088]); one or more of the AAV vectors may be administered to the eye at the same or different times (paragraph [0085]); and the use of human RPE65 promoter in the exemplary AAV2/2.hRPE65P.hRPE65 vector construct for AAV-mediated RPE65 gene therapy in human patients (Examples 1-3).
Ali et al did not teach specifically at least a rAAV particle comprising a polynucleotide that comprises: (a) a first nucleic acid segment that encodes a modified virally-derived M013 polypeptide, and (b) a second nucleic acid segment encoding a cell penetrating peptide consisting of the amino acid sequence of SEQ ID NO: 23 and a secretion signal peptide; wherein the first and second nucleic acid segments are operably linked to a promoter sequence that is active in one or more mammalian cells comprising the polynucleotide for treating an ocular disorder such as atrophic age-related macular degeneration, and intraocular inflammation.
Before the effective filing date of the present application (03/11/2014), Ambati et al already taught at least using an inhibitor of NFkappaB and/or an inhibitor of inflammasome, including a component of an inflammasome (e.g., caspase-1, NLRP-3, PYCARD) to protect retinal pigment epithelial (RPE) cell and retinal photoreceptor cell in a subject having or suspected of having or at risk of having age-related macular degeneration (AMD) and geographic atrophy (the advanced stage of atrophic AMD) (see at least the Abstract; Summary; particularly paragraphs [0010]-[0011], [0101]-[0106], [0112]-[0113], [0118]; and Table A). Ambati et al disclosed specifically examples of inflammasome inhibitors that include virus expressed inhibitors of the inflammasome such as PYD homologs M13L-PYD, S013L; and ASC-1 inhibitors such as cellular pyrin domain (PYD) superfamily proteins also known as M013 (Rahman et al, 2009) (paragraph [0116]; and Table A).
Additionally, Rahman et al already taught that in addition to targeting the host ASC-1 protein to inhibit the cellular inflammasome complex, the Myxoma virus pyrin domain-containing protein M013 also blocks activation of NF-κB signaling pathway by interacting with NF-κB1 and preventing nuclear translocation of the transcription factor RelA/p65 (see at least the Abstract and Author Summary). Rahman et al also demonstrated that transiently expressed M013 protein alone inhibited cellular NK-κB-mediated reporter gene expression and nuclear translocation of NF-κB/p65 (sections titled “M013 protein inhibits signaling pathways leading to activation of NF-κB in the absence of virus infection” on page 8 and “”M013 protein physically interacts with NF-κB1 p105” on page 9; and Figs. 7-8). Rahman et al also stated “However, unlike most of the members of the orthopoxvirus genus, MYXV does not express any predicted secreted proteins that directly bind and neutralize proinflammatory cytokines such as IL-1β and IL-18, which are regulated by a series of cellular multi-protein complexes collectively termed inflammasomes [30,31,32]. Instead, the MYXV-encoded protein M013, which was first identified as a member of the PYRIN domain (PYD) superfamily, was shown to function as an intracellular inhibitor of inflammasome activation [33]” (page 2, left col., last paragraph).
Moreover, before the effective filing date of the present application Li et al already disclosed a delivery vector for transferring a small peptide coding sequence to a cell in the form of a rAAV vector/viral particle comprising: (i) a secretory signal sequence; (ii) a sequence encoding a carrier protein (e.g., alpha-1-antitrypsin (AAT) having pro-survival functions by inhibiting apoptosis and reducing inflammation; soluble form of RAGE (sRAGE) having beneficial effect by sequestering elevated AGE found in many pathological conditions such as oxidative stress, neurodegenerative diseases and aging; or GFP serving both as a spacer and reporter protein to monitor the expression level, cell/tissue and intracellular distribution of the expressed fusion protein) operatively associated with the secretory signal sequence; (iii) a sequence encoding a cleavage site operatively associated with the sequence encoding a carrier protein; and (iv) a sequence encoding a bioactive small peptide associated with the sequence encoding a cleavage site (e.g., a cleavage site of the ubiquitous furin, which is present in the Golgi network as well as in the extracellular space of virtually all mammalian cell types) for expression and secretion extracellular of the small peptide from a mammalian cell to cells surrounding the area of transduction, or to release the small peptide to the systemic circulation or the lymph system (Abstract; particularly paragraphs [0023]-[0024], [0029]-[0035], [0037] and [0084]; and Figs. 2, 8, 12-14 and 18). Li et al also disclosed an exemplary small peptide gp91dsTat which is a chimeric 18-amino acid peptide that has been shown to interfere with NADPH oxidase assembly and activation; with its last 9 amino acids corresponding to a specific sequence in the HIV viral coat (Tat), which allows the peptide to be internalized by cells; as part of the fusion polypeptide encoded by the above disclosed delivery vector (paragraphs [0041]- [0042]; Example 4 and Fig. 6). Li et al stated “The above-described design for expressing the gp91dsTat peptide is particularly important since many delivery vectors (including AAV vectors) transduce vascular cells poorly. In the present invention, however, the entire coding region, under the control of a promoter, e.g., a CBA promoter will express a secreted precursor protein (32 kd), and upon secretion and cleavage, releases the inhibitory peptide (gp91dsTat) to be taken up by surrounding cells mediated by the Tat signal. This is a useful feature since the peptide can now diffuse to and enter distant cells that are not usually transduced by AAV vectors, particularly retinal vascular cells. Thus, in one embodiment of the present invention, the delivery vector is utilized to produce gp91dsTat in vivo, and upon secretion from the producing cells, provide uptake of the gp91dsTat by retinal vascular cells” (paragraph [0043]). Li et al taught using the secretion signal containing 21 amino acid residues derived from IgK signal sequence (paragraph [0062]), and a chicken β-actin/CMV enhancer promoter (CBA promoter) in the delivery vector (paragraphs [0043]-[0044]).
Furthermore, Mansbridge already disclosed genetically engineered proteins (e.g., a growth factor, an antioxidant, an extracellular matrix component) comprising a heterologous sequence that enhances cell penetration, wherein the heterologous sequence includes the HIV-1 Tat peptide sequence of Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg (SEQ ID NO: 3) that is 100% identical to SEQ ID NO: 23 of the present application (Abstract; Summary of the Invention; col. 8, lines 38-50; and Table 1). Mansbridge also stated “[t]he heterologous peptide has been introduced into the naturally-occurring growth factor or antioxidant, typically at or near the amino terminus or the carboxy terminus, using a conventional molecular biology technique such as genetic engineering. Such a “transport-enhanced” growth factor, antioxidant, or extracellular matrix component, may, under appropriate conditions, penetrate the cell more readily or more quickly than its naturally-occurring counterpart” (col. 8, lines 39-47).
Accordingly, it would have been obvious for an ordinary skilled artisan before the effective filing date of the present application to modify the teachings of Ali et al by also selecting the virally-derived M013 polypeptide/protein as an anti-inflammatory factor to be expressed in the form of a secreted fusion protein comprising a secretion signal sequence (e.g., the 21-amino acid IgK secretion signal sequence) operably linked to the HIV-1 Tat peptide sequence of Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg fused at the N-terminus of the M013 polypeptide, such that the secreted Tat-M013 polypeptide is taken up by surrounding cells and distant cells that are not transduced by rAAV vectors via the Tat peptide sequence; in light of the teachings of Ambati et al, Rahman et al and Mansbridge as presented above.
An ordinary skilled artisan would have been motivated to carry out the above modifications because: (i) Ambati et al already taught using inflammasome inhibitors that include virus expressed inhibitors of the inflammasome such as PYD homologs M13L-PYD, S013L; and ASC-1 inhibitors such as cellular pyrin domain (PYD) superfamily proteins also known as M013 to protect retinal pigment epithelial (RPE) cell and retinal photoreceptor cell in a subject having or suspected of having or at risk of having age-related macular degeneration (AMD) and geographic atrophy (the advanced stage of atrophic AMD); while Rahman et al demonstrated that in addition to targeting the host ASC-1 protein to inhibit the cellular inflammasome complex, the Myxoma virus pyrin domain-containing protein M013 also blocks activation of NF-κB signaling pathway; (ii) Li et al already taught successfully a delivery vector in the form of a rAAV vector/viral particle for expression and extracellular secretion of a bioactive small peptide in the form of a secreted larger fusion protein, including the exemplary bioactive gp91dsTat containing a 9-amino-acid Tat signal sequence that allows the peptide to be internalized by cells surrounding the area of transduction as well as distant cells that are not usually transduced by the AAV vector; and (iii) Mannsbridge already disclosed a genetically engineered protein (e.g., a growth factor, an antioxidant, an extracellular matrix component) comprising a heterologous sequence that enhances cell penetration, wherein the heterologous sequence includes the 9-amino-acid HIV-1 Tat peptide sequence of Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg at or near the N-terminus or C-terminus of a naturally occurring protein.
The modified recombinant AAV vector/viral particle resulting from the combined teachings of Ali et al, Ambati et al, Rahman et al, Li et al and Mansbridge as set forth above is indistinguishable from the claimed compositions of the present application.
An ordinary skilled artisan would have a reasonable expectation of success in light of the teachings of Ali et al, Ambati et al, Rahman et al, Li et al and Mansbridge as set forth above; coupled with a high level of skill of an ordinary skilled artisan in the relevant ocular gene therapy art.
Therefore, the claimed invention as a whole was prima facie obvious in the absence of evidence to the contrary.
Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Ali et al (US 2010/0081707) in view of Ambati et al (WO 2013/012806; IDS), Rahman et al (PLoS Pathogens 5(10):e1000635.doi:10.1371/jornal.ppat.1000635, pages 1-14, 2009; IDS), Li et al (US 2012/0157513; IDS) and Mansbridge (US 7,160,726) as applied to claims 1, 5-10, 16, 22 and 43-50 above, and further in view of Li et al (Molecular Vision 15:267-275, 2009).
The combined teachings of Ali et al, Ambati et al, Rahman et al, Li et al and Mansbridge were presented above. However, none of the cited references teach specifically the rAAV particle comprising a self-complementary recombinant AAV vector.
Before the effective filing date of the present application (03/11/2014), Li et al (Molecular Vision) already used a pseudotyped AAV5 capsid, self-complementary (sc) AAV5 vector comprising the human RPE65 (hRPE65) cDNA with a small, hybrid cytomegalovirus (CMV)-chicken β-actin (smCBA) promoter (scAAV5-smCBA-hRPE65) to demonstrate that an initial intravitreal injection of AAV vectors to one eye of a mouse does not influence AAV-mediated gene expression or related therapeutic effects in the other eye when vectors are administered to the subretinal space, suggesting that the subretinal space possesses a unique immune privilege relative to the vitreous cavity (Abstract; and page 168, right column, last paragraph). Moreover, Li et al stated clearly “Pseudotyped AAV5 capsid, self-complementary AAV5 vectors (scAAV5) were used in this study as they have been shown to be more efficient vectors for transduction of the retina than standard, single-stranded AAV vectors [31, 32]” (page 268, right column, last paragraph).
Accordingly, it would have been obvious for an ordinary skilled artisan before the effective filing date of the present application to further modify the combined teachings of Ali et al, Ambati et al, Rahman et al, Li et al and Mansbridge by also selecting/utilizing at least a pseudotyped AAV5 capsid, recombinant scAAV5 vector for improved transduction efficiency in the retina, in light of the teachings of Li et al (Molecular Vision) as presented above.
An ordinary skilled artisan would have been motivated to further carry out the above modification because Li et al (Molecular Vision) taught that pseudotyped AAV5 capsid, self-complementary AAV5 vectors (scAAV5) are more efficient vectors for transduction of the retina than standard, single-stranded AAV vectors.
The modified rAAV particle resulting from the combined teachings of Ali et al, Ambati et al, Rahman et al, Li et al, Mansbridge and Li et al (Molecular Vision) is indistinguishable from the claimed composition of the present application.
An ordinary skilled artisan would have a reasonable expectation of success in light of the teachings of Ali et al, Ambati et al, Rahman et al, Li et al, Mansbridge and Li et al (Molecular Vision); coupled with a high level of skill for an ordinary skilled artisan in the relevant art.
Therefore, the claimed invention as a whole was prima facie obvious in the absence of evidence to the contrary.
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
Ildefonso et al (WO 2014/164703) disclosed at least a composition for treating age-related macular degeneration and other conditions involving macular degeneration or ocular inflammation, the composition comprising an expression vector that delivers a secretable and cell penetrating CARD (caspase activation and recruitment domain), with an exemplary recombinant AAV2 vector/viral particle comprising an expression construct comprising a chicken-beta actin promoter with a CMV ie enhancer that is operably linked to a nucleotide sequence encoding the IgK signal peptide-GFP-FC-TatCARD fusion protein; wherein the IgK signal peptide fused to the GFP allows the fusion protein to be targeted for secretion upon translation, and the furin cleavage (FC) site which allows the cleavage and separation of sGFP from the TatCARD upon cleavage at the cell membrane by the furin enzyme (see at least the Abstract; particularly Figure 6; and section titled “Endotoxin-induced Uveitis (EIU) mouse model” at page 32).
Conclusions
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Quang Nguyen, Ph.D., at (571) 272-0776.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s acting SPE, James D. Schultz, Ph.D., may be reached at (571) 272-0763.
To aid in correlating any papers for this application, all further correspondence regarding this application should be directed to Group Art Unit 1631; Central Fax No. (571) 273-8300.
Any inquiry of a general nature or relating to the status of this application or proceeding should be directed to (571) 272-0547.
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/QUANG NGUYEN/Primary Examiner, Art Unit 1631