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`UNITED STATES PATENT AND TRADEMARK OFFICE
`
`UNITED STATES DEPARTMENT OF COMMERCE
`United States Patent and Trademark Office
`Address: COMIVHSSIONER FOR PATENTS
`PO. Box 1450
`Alexandria1 Virginia 22313-1450
`wwwusptogov
`
`
`
`
`
`14/042,656
`
`09/30/2013
`
`Yukari HATAOKA
`
`069804—0374
`
`9443
`
`20277
`7590
`“”900”
`MCDERMOTT WILL&EMERY LLP —
`The McDermott Building
`HAQ, SHAFIQUL
`500 North Capitol Street, NW.
`WASHINGTON, DC 20001
`
`PAPER NUMBER
`
`1678
`
`NOTIFICATION DATE
`
`DELIVERY MODE
`
`01/19/2017
`
`ELECTRONIC
`
`Please find below and/0r attached an Office communication concerning this application or proceeding.
`
`The time period for reply, if any, is set in the attached communication.
`
`Notice of the Office communication was sent electronically on above—indicated "Notification Date" to the
`following e—mail address(es):
`
`ipdocketmwe @ mwe.com
`
`PTOL—90A (Rev. 04/07)
`
`

`

`
`
`Applicant(s)
`Application No.
` 14/042,656 HATAOKA, YUKARI
`
`Examiner
`Art Unit
`AIA (First Inventor to File)
`Office Action Summary
`
`SHAFIQUL HAQ its“ 1678
`
`-- The MAILING DA TE of this communication appears on the cover sheet with the correspondence address --
`Period for Reply
`
`A SHORTENED STATUTORY PERIOD FOR REPLY IS SET TO EXPIRE g MONTHS FROM THE MAILING DATE OF
`THIS COMMUNICATION.
`Extensions of time may be available under the provisions of 37 CFR1. 136( a).
`after SIX () MONTHS from the mailing date of this communication.
`If NO period for reply is specified above, the maximum statutory period will apply and will expire SIX (6) MONTHS from the mailing date of this communication.
`-
`- Failure to reply within the set or extended period for reply will, by statute, cause the application to become ABANDONED (35 U.S.C. § 133).
`Any reply received by the Office later than three months after the mailing date of this communication, even if timely filed, may reduce any
`earned patent term adjustment. See 37 CFR 1 .704(b).
`
`In no event, however, may a reply be timely filed
`
`Status
`
`1)IZI Responsive to communication(s) filed on 11/21/2016.
`El A declaration(s)/affidavit(s) under 37 CFR 1.130(b) was/were filed on
`
`2b)|:l This action is non-final.
`2a)|Z| This action is FINAL.
`3)I:I An election was made by the applicant in response to a restriction requirement set forth during the interview on
`
`; the restriction requirement and election have been incorporated into this action.
`
`4)|:| Since this application is in condition for allowance except for formal matters, prosecution as to the merits is
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`closed in accordance with the practice under Exparte Quay/e, 1935 CD. 11, 453 O.G. 213.
`
`Disposition of Claims*
`
`5)IZI Claim(s) 1-21 is/are pending in the application.
`5a) Of the above claim(s) 10-21 is/are withdrawn from consideration.
`
`is/are allowed.
`6)I:I Claim(s)
`7)|Z| CIaim(s)_1-9is/are rejected.
`8)|:I Claim(s)_ is/are objected to.
`
`
`are subject to restriction and/or election requirement.
`9)I:I Claim((s)
`* If any claims have been determined allowable, you may be eligible to benefit from the Patent Prosecution Highway program at a
`
`participating intellectual property office for the corresponding application. For more information, please see
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`:/'/\W¢W.LISI>I‘.0. ovI’ atentS/init events/
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`iindex.‘s or send an inquiry to PPI-iieedback{®usgtc.00v.
`
`Application Papers
`
`10)I:l The specification is objected to by the Examiner.
`11)I:l The drawing(s) filed on
`is/are: a)I:I accepted or b)I:I objected to by the Examiner.
`Applicant may not request that any objection to the drawing(s) be held in abeyance. See 37 CFR 1.85(a).
`
`Replacement drawing sheet(s) including the correction is required if the drawing(s) is objected to. See 37 CFR 1.121 (d).
`
`Priority under 35 U.S.C. § 119
`
`12)I:| Acknowledgment is made of a claim for foreign priority under 35 U.S.C. § 119(a)-(d) or (f).
`Certified copies:
`
`a)I:l All
`
`b)|:l Some” c)I:l None of the:
`
`1.I:I Certified copies of the priority documents have been received.
`2.|:l Certified copies of the priority documents have been received in Application No.
`3.|:| Copies of the certified copies of the priority documents have been received in this National Stage
`
`application from the International Bureau (PCT Rule 17.2(a)).
`** See the attached detailed Office action for a list of the certified copies not received.
`
`Attachment(s)
`
`
`
`3) D Interview Summary (PTO-413)
`1) D Notice of References Cited (PTO-892)
`Paper No(s)/Mai| Date.
`.
`.
`4) I:I Other'
`2) I] InformatIon DIsclosure Statement(s) (PTO/SB/08a and/or PTO/SB/08b)
`Paper No(s)/Mai| Date
`
`US. Patent and Trademark Office
`PTOL—326 (Rev. 11-13)
`
`Office Action Summary
`
`Part of Paper No./Mai| Date 20170111
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 2
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`The present application is being examined under the pre-AIA first to invent provisions.
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`DETAILED ACTION
`
`1 .
`
`Claims 1-21 are pending and claims 1-9 are examined on merits in this office action.
`
`See office action of 08/24/2016 for withdrawal of claims from further consideration as
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`being directed to a non-elected invention.
`
`Claim Rejections - 35 USC § 103
`
`The following is a quotation of 35 U.S.C. 103(a) which forms the basis for all
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`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.
`
`Claims 1-9 are rejected under 35 U.S.C. 103(a) as being unpatentable over Wagner
`
`et a/ (US 6,406,921 B1) in view of Chen (2010/0113476) and Besselink (Applied
`
`Biochemistry and Biotechnology 1993).
`
`Wagner discloses protein arrays on a substrate (Abstract). Wagner discloses a
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`protein immobilized substrate wherein the substrate comprises a self-assembled
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`monolayer 7 linked to affinity molecule 8, which is in turn is linked to a protein (Fig.
`
`6) (Col. 14,
`
`line 5 to col.15,
`
`line 4; col. 18,
`
`lines 29-44). Wagner teaches that an
`
`affinity tag enhances site-specific immobilization of protein onto the monolayer
`
`(col.3,
`
`lines 56-58). Wagner teaches that affinity tag confer enhanced binding or
`
`reaction of the protein with Y (col. 12, lines 59-67). Wagner teaches that affinity tag
`
`allows for common immobilization strategy to be used with multiple different proteins
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`

`

`Application/Control Number: 14/042,656
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`Art Unit: 1678
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`Page 3
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`(col.13, lines 9-12). Wagner teaches that affinity tag may be an amino acids capable
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`of immobilizing a protein (col. 5, line 40) and in a preferred embodiment, affinity tag
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`comprises at least one amino acid (col.13,
`
`lines 23-24). Wagner teaches that the
`
`affinity tag may be a lone monolayer reactive amino acids such as cysteine, lysine,
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`histidineI arginineI tyrosine and glutamine (col.13,
`
`lines 16-19 and 21-22).
`
`Wagner teaches that
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`the affinity tag is a component of a layer of affinity tag
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`molecules immobilized on the monolayer (col.14, lines 11-13) and the affinity tag
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`can be a single amino acid (col.5, lines 36-45; col. 13, lines 16-19; col.20, lines
`
`26-30). Wagner further teaches that amino acid tag interact with Y functional group
`
`of the monolayer molecule (col.13, lines 21-23) wherein the Y functional group can
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`be a carboxylic acid activated to a reactive ester (See Figs 4 and 5; col. 11, lines
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`30-45 and col.20,
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`lines 1-12). Wagner further teaches that the protein can be
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`antibody or antibody fragment (Col.7, lines 45-47).
`
`Wagner does not have specific disclosure for
`
`the antibody linked to the
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`carboxylic acid group of a self-assembled monolayer through the single amino acid
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`wherein the amino group of the single amino acid formed a peptide bond with the
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`carboxylic acid of the self-assembled monolayer and the carboxylic acid group of the
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`single amino acid formed a peptide bond with an amino group of the antibody.
`
`Chen teaches that single amino acid linker helps to retain activity of bound
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`compound and sometimes surpassing peptidyl linkers (paragraph [0135]).
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`Besselink discloses -glycine NHS surface suitable for immobilization of amine
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`containing compound (Abstract and Scheme 1). Besselink teaches NHS activated
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`

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`Application/Control Number: 14/042,656
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`Art Unit: 1678
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`Page 4
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`surface having glycine (-glycine-NHS) is more stable than NHS activated surface
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`without glycine (page 242, 3rd paragraph) and the surface activated with —glycine-
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`NHS is more active for immobilization of amine containing compound (Fig.10; page
`
`240, see “Discussion” and page 244, last paragraph).
`
`From the forgoing description in mind,
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`it would have been a prima facie obvious
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`at the time the invention was made,
`
`for one of ordinary skill
`
`in the art to have
`
`considered attaching the antibody to the self-assembled monolayer because
`
`Wagner teaches immobilization of proteins on the array and the protein can be an
`
`specific binding partner such as an antibody or antibody fragment for detection of
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`analyte (Col.7,
`
`lines 45-47; Col.17,
`
`lines 25-30 and Col.18,
`
`lines 12-21). One of
`
`ordinary skill would be motivated to attached the antibody in the self-assembled
`
`monolayer through the affinity tag (e.g. amino acid) because Wagner teaches that
`
`affinity tag enhances site-specific immobilization of protein onto the monolayer,
`
`confer enhanced binding or
`
`reaction of
`
`the protein and allows for common
`
`immobilization strategy to be used with multiple different proteins.
`
`It would have
`
`been a prima facie obvious at the time the invention was made, for one of ordinary
`
`skill
`
`in the art
`
`to have attached the antibody to the self-assembled monolayer
`
`through a single amino acid linker because Wagner teaches attaching protein
`
`through an affinity tag wherein the affinity molecule may be a single amino acid (col.
`
`13, lines 16-19; col.20, lines 26-30) and because Wagner teaches that the affinity
`
`tag can a component of a layer immobilized on the monolayer (col.14, lines 11-13).
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`One of ordinary skill in the art would be motivated to use single amino acid linker to
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`

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`Application/Control Number: 14/042,656
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`Art Unit: 1678
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`Page 5
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`link protein to the surface because Chen teaches that single amino acid linker helps
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`to retain activity of bound compound and sometimes surpassing peptidyl
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`linkers
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`(paragraph [0135]). Moreover, one of ordinary skill
`
`in the art would be motivated to
`
`provide activated single amino acid, such as glycine-NHS on a carboxyl surface to
`
`immobilize a protein because Besselink teaches NHS activated surface having
`
`glycine (-glycine-NHS) is more stable than NHS activated surface without glycine
`
`(page 242, 3rd paragraph) and the surface activated with —glycine-NHS is more
`
`active for immobilization of amine containing compound (Fig.10; page 240, see
`
`“Discussion” and page 244, last paragraph).
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`In addition, one of ordinary skill
`
`in the
`
`art would have had a reasonable expectation of success of using the monolayer of
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`Wagner having the carboxylic acid group to provide glycine having activated NHS
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`group because Wagner teaches activation process for the carboxylic group (Figs. 4
`
`and 5 and Besselink teaches the process of immobilizing glycine through its amino
`
`group to activated surface and then activating the carboxyl group of the glycine to
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`provide the -glycine-NHS surface highly stable and highly reactive to immobilized
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`amine containing compounds.
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`Response to argument
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`4. Applicant's arguments filed 11/21/2016 have been fully considered and are
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`persuasive to overcome 35 USC 103 rejections over Hatoka et a/ (US 8,980,645 and
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`8,785,143) in view of Applicant’s arguments. The obviousness double patenting
`
`rejections have been withdrawn in view of filing of terminal disclaimer. However,
`
`

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`Application/Control Number: 14/042,656
`
`Art Unit: 1678
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`Page 6
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`Applicant’s arguments are not persuasive to overcome the rejection under 35 USC
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`103 over Wagner et al.
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`Applicant first states that the present inventor discovered that the amount of the
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`antibody immobilized per unit area was increased significantly by binding one
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`molecule amino acid to a self-assembled monolayer and then immobilizing the
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`antibody,
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`that
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`is,
`
`the combination antibody/one molecule of amino acid/self-
`
`assembled monolayer provides a significant increase in the immobilization amount
`
`of the antibody and this effect was demonstrated in the examples and reported in
`
`Table 1 of the specification. Applicant
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`then argued that
`
`in Wagner there is no
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`disclosure of an example which shows that
`
`the immobilization amount of
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`the
`
`antibody to the self-assembled monolayer can be increased by inserting one
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`molecule of amino acid between the self-assembled monolayer and the antibody.
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`Applicant argued that Wagner did not appreciate the advantages of the specific
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`structure of the antibody/one molecule of amino acid/self-assembled monolayer
`
`provided by the method of the present claims. Applicant argued that Chen fails to
`
`disclose compounds in which a single amino acid is used as the linker and also fails
`
`to appreciate that using a single amino acid as the linker can have good activity or
`
`that a single amino acid is preferable for the linker. Although argued that Besselink
`
`discloses that NHS enhances the coupling reaction between the amino compound
`
`and Sepharose-glycine and there is no disclosure of enhancing the coupling reaction
`
`by glycine coupled to Sepharose. Based on the above arguments, Applicant
`
`conclude that
`
`the combination of
`
`references fails
`
`to teach or suggest
`
`the
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`

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`Application/Control Number: 14/042,656
`
`Art Unit: 1678
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`Page 7
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`antibody/one molecule of amino acid/self-assembled monolayer provided by the
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`method of the present claims and they all fail to even recognize an appropriate linker
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`and structure for increasing the immobilization amount of an antibody.
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`The above arguments have fully been considered but are not found persuasive.
`
`Wagner suggests immobilization of proteins on self-assembled monolayer through
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`an affinity tag and suggests single amino acid in a preferred embodiment as affinity
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`tag/linker. Examiner agrees with Applicant that Wagner did not specify a specific
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`amino acid linker capable of increasing immobilization of antibody. However, as
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`described in the rejection Wagner teaches affinity tag for common immobilization
`
`strategy to be used with multiple different proteins and that affinity tag may be an
`
`amino acids capable of immobilizing a protein (col. 5, line 40; col.13, lines 9-12) and
`
`in a preferred embodiment, affinity tag comprises at least one amino acid (col.13,
`
`lines 23-24). Wagner further
`
`teaches that the affinity tag may be a lone monolayer
`
`reactive amino acids such as cysteine, lysinel histidineI arginine, tyrosine and
`
`glutamine (col.13,
`
`lines 16-19 and 21-22). The rejection is based on the
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`combination of the references of Chen and Basselink and the combination of the
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`references as described in the rejection, teach single amino acid linker to retain
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`activity of bound compound (Chen)
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`and glycine-NHS linker
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`for
`
`improved
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`immobilization of amine containing compound (Besselink). Besselink does disclose
`
`valine as an example of an amine compound immobilzed by glycine-NHS
`
`linker(Fig.10) but however, Besselink teaches that amine compound having bulky
`
`side chains such arginine or valine is less favorable (page 244, lines 1-2). Further,
`
`

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`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 8
`
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`Besselink teaches efficient
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`immobilization of enzymes and proteins with high
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`capacity with the glycine-NHS linker (page 245, last four lines).
`
`Therefore, there are ample motivation to utilize single amino acid, specifically
`
`glycine-NHS for the affinity tag/linker of Wagner for improved and high capacity
`
`immobilization of proteins/protein A/antibody with retained activity. The combination
`
`of the reference motivates one of ordinary skill in the art to consider glycine-NHS as
`
`affinity tag/linker for Wagner and the linker Glycine-NHS would provide improved
`
`and high capacity binding of proteins and/or Protein A in view of Besselink. Applicant
`
`asserted that increased immobilization is dependent on appropriate kind of linker
`
`fl molecule to be immobilized but however Applicant did not provide any example
`
`or convincing evidence that the increased immobilization by an amino acid (any
`
`amino acid or some selected amino acid) is antibody dependent only and other
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`proteins do not show this increased immobilization. Since, Besselink teaches
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`improved and high capacity immobilization of amine containing compounds including
`
`enzymes and proteins,
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`it would be highly expected that antibody would be
`
`immobilized with improved and high capacity by utilizing glycine-NHS as affinity
`
`tag/linker in array substrate of Wagner with a reasonable expectation of success.
`
`Applicant cited Table 1 for unexpected improved immobilization by utilizing any of
`
`a single amino acid as a linker. However, as disclosed in Table 1, glutamine show
`
`negligible improvement of immobilization amount of antibody and arginine, proline,
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`Aspartic acid,
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`isoleucine and valine showed some improved binding but some
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`improved binding would be considered expected in view of the prior art references
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 9
`
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`that suggest efficient immobilization of enzymes and proteins with high capacity with
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`the glycine-NHS linker (page 245, last four lines of Besselink). Moreover, Applicant's
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`assertion that all amino acid provides unexpected improved immobilization (see
`
`claim 1 wherein 20 amino acids have been claimed) is contradictory to result in the
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`Table 1 which only show negligible increase (not unexpected) in binding using
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`glutamine and as described above some amino acids (arginine, proline, aspartic
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`acid, leucine and valine) showed expected improvements, not unexpected improved
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`results. MPEP 716.02 states, "[A]ny differences between the claimed invention and
`
`the prior art may be expected to result in some differences in properties. The issue
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`is whether the properties differ to such an extent that the difference is really
`
`unexpected." Also significant
`
`is MPEP 716.02(d) which states, "[W]hether the
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`unexpected results are the result of unexpectedly improved results or a property not
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`taught by the prior art,
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`the "obiective evidence of nonobviousness must be
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`commensurate in scope with the claims which the evidence is offered to support." In
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`other words,
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`the showing of unexpected results must be reviewed to see if the
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`results occur over the entire claimed range."
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`Conclusion
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`5. THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time
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`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
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`MONTHS from the mailing date of this action.
`
`In the event a first reply is filed within
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 10
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`TWO MONTHS of the mailing date of this final action and the advisory action is not
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`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 extension fee 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.
`
`6. Any inquiry concerning this communication or earlier communications from the
`
`examiner should be directed to SHAFIQUL HAQ whose telephone number is
`
`(571 )272—6103. The examiner can normally be reached on 7 AM to 3:30 P.M..
`
`If attempts to reach the examiner by telephone are unsuccessful, the examiner’s
`
`supervisor, Mark Shibuya can be reached on 571-272-0806. The fax phone number
`
`for the organization where this application or proceeding is assigned is 571-273-
`
`8300.
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