Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
Priority
The present application is a 35 U.S.C. § 371 U.S. national phase entry of International Application No. PCT/US2022/077593 having an international filing date of October 5, 2022, which claims the benefit of priority to U.S. Provisional Patent Application No. 63/252,414, filed on October 5, 2021, that is hereby acknowledged by the Examiner.
Status of the Claims
The amendment dated 11/08/2015 is acknowledged. Claims 1, 3-4, 11-12, 16, 22, 24, 27, 35, 38, 42, 48 and 50 are pending and under examination.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 06/06/2024 and 08/25/2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement(s) is/are being considered by the Examiner.
Drawings
The drawing filed on 04/05/2024 are acknowledged and accepted by the Examiner.
Claim Objections
Claim 35 is objected to for the following informalities:
Claim 35 is objected to for being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
Claim Rejections - 35 USC § 112
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.
Claims 1, 12, 22, 38 and 48 are rejected under 35 U.S.C. 112(b), as being indefinite for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention.
Claim 1 is rejected to as being indefinite for reciting the isolated peptide sequences as a combination as opposed to the alternative. The claim recites “the solid support that includes an isolated peptide, wherein the isolated peptide comprises an amino acid sequence”, which is understood to be one amino acid sequence. The claim is rendered indefinite as one would not know if the claim is in the alternative for SEQ ID NOs: 4-7 and 11-13 or encompasses all sequences in a single peptide. For examination purposes, it is understood by the Office that the claim reads in the alternative.
Claims 12 and 38 recite “substantially”. The term “substantially” is not clear in that it is a relative term. Further, the specification does not define the term “substantially” and does not provide a standard for ascertaining the requisite degree, thus a skilled artisan would not be apprised to the metes and bounds of the recitations. Thus, the claims are rendered indefinite.
Claims 22 and 48 recites trademark names. Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112, second paragraph. See Ex parte Simpson, 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name. In the present case, the trademark/trade name is used to identify/describe a reactive compound, wherein the reactive compound can be from either a redox active compound, a radical building compound, or a stabilizing compound and, accordingly, the identification/description is indefinite.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action:
(a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102 of this title, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter pertains. Patentability shall not be negatived by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims under 35 U.S.C. 103(a), the examiner presumes that the subject matter of the various claims was commonly owned at the time any inventions covered therein were made absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and invention dates of each claim that was not commonly owned at the time a later invention was made in order for the examiner to consider the applicability of 35 U.S.C. 103(c) and potential 35 U.S.C. 102(e), (f) or (g) prior art under 35 U.S.C. 103(a).
Claims 1, 3-4, 11-12, 16, 22 and 24 are rejected under 35 U.S.C. 103(a) as being unpatentable over Su et al. “Su” (US20110059553, IDS of record dated 08/25/2025), in view of UniProt Accession No. GG_HHV11 “HHV11” (UniProt Accession No. GG_HHV11, Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1), January 01, 1988 [online] <URL: https://www.uniprot.org/uniprotkb/P06484/entry>).
The claims are directed to a solid support comprising at least two regions, each region defining an area of the solid support that includes an isolated peptide, wherein the isolated peptide comprises an amino acid sequence set forth as: SEQ ID NOs: 5-7, 11-13, and and analogues thereof wherein the isolated peptide sequences comprise one or more of: a) up to 5 amino acids at the C and/or at the N terminal ends, b) one, two or three conservative amino acid substitutions, c) 98% or greater sequence homology to SEQ ID Nos. 4-7 and 11-13, and d) functional groups for covalently attaching the isolated peptide sequences to a solid support, and combinations thereof, optionally wherein the solid support is not directly linked to an antibody, optionally wherein the solid support further comprises a control region, and wherein the control region comprises a control agent, and optionally wherein the isolated peptide consists essentially of the amino acid sequence set forth as: SEQ ID NOs: 4-7 and 11-13 and analogues thereof wherein the isolated peptide sequences comprise one or more of: a) up to 5 amino acids at the C and/or at the N terminal ends, b) one, two or three conservative amino acid substitutions, c) 98% or greater sequence homology to SEQ ID Nos. 4-7 and 11-13, and d) functional groups for covalently attaching the isolated peptide sequences to a solid support.
Regarding claims 1, 16 and 24, Su teaches a solid support comprising regions, each region defining an area of the solid support that includes an isolated peptide (Claim 1 – A method of detecting the presence or absence of a specific anti-herpes simplex virus type-2 (HSV-2) antibody in a biological sample comprising: (a) contacting a biological sample suspected of containing anti-HSV-2 antibodies with a first antigen comprising the amino acid sequence AAKTPPTTPAP (SEQ ID NO:06), wherein said first antigen is not a full length glycoprotein G2 (gG2) polypeptide, (b) contacting said biological sample with a second antigen capable of binding said specific anti-HSV-2 antibody, and (c) detecting the presence or absence of specific anti-HSV-2 antibody in said biological sample wherein said specific anti-HSV-2 antibody detected in said sample is bound to said second antigen, wherein said first antigen is not reactive with said specific anti-HSV-2 antibody.'; Claim 6 - 'The method of claim 1, wherein at least one oi said antigens is immobilized on a solid support.'; Claim 7 - 'The method of claim 6, wherein said solid support is selected from the group consisting of: a microparticle, an agarose bead, and a magnetic bead.'; para
[0133] - 'In another non-limiting example, the apparatus will generally employ a continuous flow-path of a suitable filter or membrane, such as a nitrocellulose membrane, having at least three regions, a fluid transport region, a sample region, and a measuring region .... The fluid transfer region may have immobilized cross-reactive antigens in order to bind cross-reactive HSV antibodies.'; para [0134] - 'In yet another non-limiting example the device is a dipstick, to the surface of which is bound in distinct regions: (1) specific gG2 antigens and (2) crossreactive antigens an affinity reagent.'). Su does not expressly teach at least two regions of the solid support that includes an isolated peptide. However, since Su teaches using two antigens and two solid supports that are contiguous (para [0092] - 'In certain embodiments, the biological sample will be contacted with at least two cross-reactive antigens,'; Claim 9 - 'The method of claim 1, wherein said first antigen is immobilized on a first solid support, and said second antigen is immobilized on a second solid support.'; para [0012] - 'In some embodiments, the composition further comprises a specific HSV-2 gG2 antigen) immobilized on a second support .... In certain embodiments, the first support is in fluid communication with the second support. In further embodiments, the first support and second support are contiguous.'; para [0022] - 'In some embodiments, the second polypeptide is immobilized on a first support.'), it would have been obvious to one of ordinary skill in the art that the method of Su could be modified to instead have a single solid support with two
regions where the peptide is bound, and the same peptide could be used for immo6ilization at the two regions, for any improvement in the sensitivity and specificity of the detection assay.
Su does not teach wherein the isolated peptide comprises an amino acid sequence set forth as:
VPINVSSTTQPQLQTTGRPSHEAPNMTQTGTTDSPTAISLITPDHIPPMPSIGLEEEEEEE
GAGDGEFILEGGDGTRDILPQSPGPAFPLAEDVEKDKPNRPWPSPDPNN SPARPETSRP
KTPPTIIGPLATRPTTRL TSKGRPLVPTPQHTPLFSFLTASPALDT (SEQ ID No. 4),
and analogues thereof wherein the isolated peptide sequences comprise one or more of:
a) up to 5 amino acids at the C and/or at the N terminal ends,
b) one, two or three conservative amino acid substitutions,
c) 98% or greater sequence homology to SEQ ID Nos. 4-7 and 11-13.
d) functional groups for covalently attaching the isolated peptide sequences to a solid support, and combinations thereof.
HHV11, however, teaches Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) Envelope glycoprotein G sequence with 100% identity to the isolated peptide of claimed SEQ ID NO: 4 (GG_HHV11, aa 25-190 has 100% identity to claimed SEQ ID NO:4).
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It would have been obvious to one of ordinary skill in the art to generate a solid support comprising at least two regions defining an area of the solid support that includes an isolated peptide as disclosed by Su, whereby the HHV-1 envelop glycoprotein G sequence of GG_HHV11 could be utilized as taught by HHV1. One of ordinary skill in the art would have been motivated to do so with a reasonable expectation of success for the benefit of increasing the accuracy and specificity for detection of anti-HHV-1 antibodies.
Regarding claims 3 and 4, Su in view of HHV11 makes obvious the solid support of claim 1, wherein Su further teaches for one of the at least two regions, the isolated peptide is linked to the solid support (para [0110] – “In general, a solid support is first reacted with a solid phase component (e.g., one or more specific gG2 antigens) under suitable binding conditions such that the component is sufficiently immobilized to the support. Optionally, immobilization of the antigen to the support can be enhanced by first coupling the antigen to a protein with better binding properties. Suitable coupling proteins include, but are not limited to, macromolecules such as serum albumins including bovine serum albumin (BSA), keyhole limpet hemocyanin, immunoglobulin molecules, thyroglobulin, ovalbumin, and other proteins well known to those skilled in the art”; para [0132]- “In some embodiments, the cross-reactive antigen is immobilized to the solid phase particle by a linking moiety such as, for example, a polypeptide”).
Regarding claim 11, with respect to the solid support comprising at least three regions, it is not inventive and considered routine and obvious as mere routine optimization. According to section 2144.05 of the M.P.E.P., "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum of workable ranges by routine experimentation." Application of Aller, 220 F.2d 454, 456, 105 USPQ 233, 235-236 (C.C.P.A. 1955). "No invention is involved in discovering optimum ranges of a process by routine experimentation." Id. at 458, 105 USPQ at 236-237. The "discovery of an optimum value of a result effective variable in a known process is ordinarily within the skill of the art." Application of Boesch, 617 F.2d 272, 276, 205 USPQ 215, 218-219 (C.C.P.A. 1980). It would have been obvious for one of ordinary skill to determine the appropriate number of regions in the solid support disclosed by the prior art by routine experimentation procedures known in the art. Routine experimentation based on the teachings of these references would have led those of ordinary skill in the art to increase the number of regions in order to achieve the maximum (production or activity or therapeutic) response from the solid support.
Regarding claim 12, Su teaches a solid support, wherein: the support comprises:
a wicking material for directing material flow along a direction of the solid support (para [0133] - 'In another non-limiting example, the apparatus will generally employ a continuous flow-path of a suitable filter or membrane, such as a nitrocellulose membrane, having at least three regions, a fluid transport region, a sample region, and a measuring region .... The fluid transfer region may have immobilized crossreactive antigens in order to bind cross-reactive HSV antibodies.'); a sample region comprising a first isolated peptide, wherein the first isolated peptide is not linked to the solid support, and wherein the first isolated peptide is fused to a heterologous protein (para [0133] - 'In another non-limiting example, the apparatus will generally employ a continuous flow-path of a suitable filter or membrane, such as a nitrocellulose membrane, having at least three regions, a fluid transport region, a sample region, and a measuring region .... The fluid transfer region may have immobilized cross-reactive antigens in order to
bind cross-reactive HSV antibodies.'; para [0110] - 'In general; a solid support is first reacted with a solid phase component (e.g., one or more specific gG2 antigens) under suitable binding conditions such that the component is sufficiently immobilized to the support. Optionally, immobilization of the antigen to the support can be enhanced by first coupling the antigen to a protein with better binding properties. Suitable coupling proteins include, but are not limited to, macromolecules such as serum albumins including bovine serum albumin (BSA), keyhole limpet hemocyanin, immunoglobulin molecules, thyroglobulin, ovalbumin, and other proteins well known to those skilled in the art.'); a detectable agent, a reactive agent, or combinations thereof (para [0133] - 'In another non-limiting example, the apparatus will generally employ a continuous flow-path of a suitable filter or membrane, such as a nitrocellulose membrane, having at least three regions, a fluid transport region, a sample region, and a measuring region .... The fluid transfer region may have immobilized cross-reactive antigens in order to bind cross-reactive HSV antibodies.'; para [0048] - 'By "detectably labeled antibody'', or "detectably labeled secondary antibody" is meant an antibody (or antibody fragment which retains binding specificity), having an attached detectable label.'); a test region positioned beyond the sample region along the direction of material flow, wherein the test region comprises a second isolated peptide linked to the solid support (para [0133] - 'In another non-limiting example, the apparatus will generally employ a continuous flowpath of a suitable filter or membrane, such as a nitrocellulose membrane, having at least three regions, a fluid transport region, a sample region, and a measuring region .... The fluid transfer region may have immobilized cross-reactive antigens in order to bind cross-reactive HSV antibodies.'; para [0092] - 'In certain embodiments, the biological sample will be contacted with at least two cross-reactive antigens,';
Claim. 9 - 'The method of claim· 1, wherein said first antigen is immobilized on a first solid support, and said second antigen is immobilized on a second solid support.'; para [0012] - 'In some embodiments, the composition further comprises a specific HSV-2 gG2 antigen immobilized on a second support .... In certain embodiments, the first support is in fluid communication with the second support. In further embodiments, the first support and second support are contiguous.'; para [0022] - 'In some embodiments, the second polypeptide is immobilized on a first support.').
Sue does not teach a control region positioned beyond the test region along the direction of material flow, wherein the control region comprises a control agent, and wherein each of the first isolated peptide and the second isolated peptide comprise an amino acid sequence set forth as:
VPINVSSTTQPQLQTTGRPSHEAPNMTQTGTTDSPTAISLITPDHIPPMPSIGLEEEEEEE
GAGDGEFILEGGDGTRDILPQSPGPAFPLAEDVEKDKPNRPWPSPDPNN SPARPETSRP
KTPPTIIGPLATRF\TTRLTSKGRPLVPTPQHTPLFSFLTASPALDT (SEQ ID No. 4), and analogues thereof wherein the first and second isolated peptide sequences comprise one or more of: a) up to 5 amino acids at the 'c and/or at the N terminal ends, b) one, two or ttiree conservative amino acid substitutions, c) 98% or great~r sequence homology to SEQ ID No. 4, d) functional grtjups for covalently attaching the first and/or second isolated peptide sequences to a solid support.
HHV11, however, teaches Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) Envelope glycoprotein G sequence with 100% identity to the isolated peptide of claimed SEQ ID NO:4 (GG_HHV11, aa 25-190 has 100% identity to claimed SEQ ID NO:4).
It would have been obvious to one of ordinary skill in the art that the HHV-1 envelop glycoprotein G sequence of HHV11 could be used for immobilization on the solid support of Su. One of ordinary skill in the art would have been motivated to do so with a reasonable expectation of success for the benefit of increasing the accuracy and specificity for detection of anti-HHV-1 antibodies.
Regarding claim 22, with respect to administering a therapeutic agent to a patient that test positive for HSV-1 and/or HSV-2 infection from the method of claim 16, it is not inventive and considered routine and obvious to one of ordinary skill in the art to generate a method for detecting anti-Herpes Simplex Virus antibodies as taught by Su, followed by administering a therapeutic agent to a patient infected with said virus. One of ordinary skill in the art would have been motivated to do so with a reasonable expectation of success given the knowledge that the field has established therapeutic agents in the treatment of HSV-1 and/or HSV-2 infected patients such as the optionally listed agents in the instant claim.
Therefore, the claimed invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
Claims 27, 42, 48 and 50 are rejected under 35 U.S.C. 103(a) as being unpatentable over Su et al. “Su” (US20110059553, IDS of record dated 08/25/2025), in view of Day et al. “Day” (WO2003086308).
The teachings of Su are outlined above and incorporated herein.
Regarding claims 27, 42 and 50, Su teaches for one of the at least two regions, the isolated peptide is linked to the solid support (para [0110] – “In general, a solid support is first reacted with a solid phase component (e.g., one or more specific gG2 antigens) under suitable binding conditions such that the component is sufficiently immobilized to the support. Optionally, immobilization of the antigen to the support can be enhanced by first coupling the antigen to a protein with better binding properties. Suitable coupling proteins include, but are not limited to, macromolecules such as serum albumins including bovine serum albumin (BSA), keyhole limpet hemocyanin, immunoglobulin molecules, thyroglobulin, ovalbumin, and other proteins well known to those skilled in the art”; para [0132]- “In some embodiments, the cross-reactive antigen is immobilized to the solid phase particle by a linking moiety such as, for example, a polypeptide”). with respect to the solid support comprising at least three regions, it is not inventive and considered routine and obvious as mere routine optimization. According to section 2144.05 of the M.P.E.P., "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum of workable ranges by routine experimentation." Application of Aller, 220 F.2d 454, 456, 105 USPQ 233, 235-236 (C.C.P.A. 1955). "No invention is involved in discovering optimum ranges of a process by routine experimentation." Id. at 458, 105 USPQ at 236-237. The "discovery of an optimum value of a result effective variable in a known process is ordinarily within the skill of the art." Application of Boesch, 617 F.2d 272, 276, 205 USPQ 215, 218-219 (C.C.P.A. 1980). It would have been obvious for one of ordinary skill to determine the appropriate number of regions in the solid support disclosed by the prior art by routine experimentation procedures known in the art. Routine experimentation based on the teachings of these references would have led those of ordinary skill in the art to increase the number of regions in order to achieve the maximum (production or activity or therapeutic) response from the solid support.
Su does not teach SEQ ID NOs: 1-3 and 8-10,
Day, however, discloses compounds and methods for the diagnosis and treatment of HSV infection are provided. The compounds comprise polypeptides that contain at least one antigenic portion of an HSV polypeptide and DNA sequences encoding such polypeptides. Pharmaceutical compositions and vaccines comprising such polypeptides or DNA sequences are also provided, together with antibodies directed against such polypeptides. Day discloses an isolated polypeptide comprising 100% sequence identity to SEQ ID NO: 8 of the instant claim (see below, SEQ ID NO: 143 of Day).
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It would have been obvious to one of ordinary skill in the art that the isolated peptide of Day could be used for immobilization on the solid support of Su. One of ordinary skill in the art would have been motivated to do so with a reasonable expectation of success for the benefit of increasing the accuracy and specificity for detection of anti-HHV-1 antibodies.
Regarding claim 48, with respect to administering a therapeutic agent to a patient that test positive for HSV-1 and/or HSV-2 infection from the method of claim 16, it is not inventive and considered routine and obvious to one of ordinary skill in the art to generate a method for detecting anti-Herpes Simplex Virus antibodies as taught by Su, followed by administering a therapeutic agent to a patient infected with said virus. One of ordinary skill in the art would have been motivated to do so with a reasonable expectation of success given the knowledge that the field has established therapeutic agents in the treatment of HSV-1 and/or HSV-2 infected patients and given the fact that Day explicitly discloses that “In yet another aspect, methods are provided for inducing protective immunity in a patient, comprising administering to a patient an effective amount of one or more of the above pharmaceutical compositions or vaccines. Any of the polypeptides identified for use in the treatment of patients can be used in conjunction with pharmaceutical agents used to treat herpes infections, such as, but not limited to, Zovirax®(Acyclovir), Valtrex® (Valacyclovir), and Famvir® (Famcyclovir)” (page 3 lines 22-27).
Therefore, the claimed invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Barry Chestnut whose telephone number is (571)270-3546. The examiner can normally be reached on M-Th 8:00 to 4:00.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Thomas Visone can be reached on 571-270-0684. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/BARRY A CHESTNUT/Primary Examiner, Art Unit 1672
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