JP2019107021A - 融合ポリペプチドおよび使用方法 - Google Patents
融合ポリペプチドおよび使用方法 Download PDFInfo
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- JP2019107021A JP2019107021A JP2019039348A JP2019039348A JP2019107021A JP 2019107021 A JP2019107021 A JP 2019107021A JP 2019039348 A JP2019039348 A JP 2019039348A JP 2019039348 A JP2019039348 A JP 2019039348A JP 2019107021 A JP2019107021 A JP 2019107021A
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- fusion polypeptide
- il28b
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Abstract
Description
頁)。
IL28B、IL28AおよびIL29を含むIII型インターフェロンによって誘導される抗ウイルス活性は、脳心筋炎ウイルス(EMCV)、水疱性口内炎ウイルス(VSV)、インフルエンザ(Eur J Immunol.2004年;34巻(3号):796〜805頁、J Virol.2006年;80巻(9号):4501〜4509頁)、B型肝炎ウイルス(HBV)およびC型肝炎ウイルス(HCV)(J Virol.2005年;79巻(6号):3851〜3854頁)に対して実証された。しかし、III型インターフェロンに対する抗ウイルス応答の規模は多くの場合、多くの細胞型においてインターフェロンアルファに対するものよりも小さい。III型インターフェロンおよびインターフェロンアルファ系の間の有意差は、受容体分布のパターンである。インターフェロンアルファの受容体は、遍在的に発現されているが、III型インターフェロン受容体のIL28R構成成分は、肝細胞を含む細胞の限定的なサブセットのみに存在する(Cytokine 2005年、31巻、109〜118頁)。機能的なIL28Rは、大部分の造血細胞において著しく不在である(Hepatology.2006年;44巻(4号):896〜906頁)。前臨床毒物学試験は、ペグ化IL29ペプチドが、ペグ化インターフェロンアルファとは異なり、骨髄幹細胞コロニー形成の阻害を誘導しない、または末梢血白血球において抗ウイルスおよび抗増殖活性を誘導することを示した(Ann NY Acad Sci.2009年;1182巻
:80〜87頁)。
(S1)−(ヘリックスA)−(S2)−(ヘリックスC)−(S3)−(ヘリックスD)−(S4)−(ヘリックスE)−(S5)−(ヘリックスF)−(S6)
の構造を有し
a.ヘリックスDは、IL28B(配列番号2)の約V98〜Q112またはIL29(配列番号1)の約V89〜Q103の残基を有する断片に対し少なくとも90%の相同性を示すアミノ酸配列を含み、
b.ヘリックスEは、IL28B(配列番号2)の約R130〜E145またはIL29(配列番号1)の約R121〜E136の残基を有する断片に対し少なくとも90%の相同性を示すアミノ酸配列を含み、
c.S1、S2、S3、S4、S5およびS6のそれぞれは独立に、1〜約50個の間のアミノ酸残基を有するスペーサー配列である
融合ポリペプチドであって、
i.ヘリックスAが、IL28B(配列番号2)の約P27〜L44の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL29(配列番号1)の約R56〜A80の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL29(配列番号1)の約G139〜A161の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含む、または
ii.ヘリックスAが、IL29(配列番号1)の約P20〜L37の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL28B(配列番号2)の約R63〜A87の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL28B(配列番号2)の約G148〜A170の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含む、または
iii.ヘリックスAが、IL28B(配列番号2)の約P27〜L44の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL28B(配列番号2)の約R63〜A87の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL29(配列番号1)の約G139〜A161の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含む、または
iv.ヘリックスAが、IL29(配列番号1)の約P20〜L37の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL29(配列番号1)の約R56〜A80の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL28B(配列番号2)の約G148〜A170の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含む、または
v.ヘリックスAが、IL28B(配列番号2)の約P27〜L44の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL29(配列番号1)の約R56〜A80の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL28B(配列番号2)の約G148〜A170の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含む、または
vi.ヘリックスAが、IL29(配列番号1)の約P20〜L37の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL28B(配列番号2)の約R63〜A87の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL29(配列番号1)の約G139〜A161の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含むことを特徴とする融合ポリペプチドを提供する。
本発明は、例えば、以下の項目も提供する。
(項目1)
第1のインターフェロンラムダアイソフォーム由来の第1の断片と、第2のインターフェロンラムダアイソフォーム由来の第2の断片とを含む融合ポリペプチドであって、該第1の断片および該第2の断片が、融合部位において一緒に融合して、近接ポリペプチドを形成し、該融合部位が、該第1のインターフェロンラムダアイソフォームおよび該第2のインターフェロンラムダアイソフォームにおける対応する配列と同一である少なくとも約6アミノ酸の配列を含む融合ポリペプチド。
(項目2)
前記第1のアイソフォームまたは前記第2のアイソフォームの二次構造を保持する、項目1に記載の融合ポリペプチド。
(項目3)
前記第1のアイソフォームまたは前記第2のアイソフォームの場合と比較して、いかなる追加的なT−エピトープも欠く、項目1に記載の融合ポリペプチド。
(項目4)
前記第1のアイソフォームまたは前記第2のアイソフォームの場合と比較して、いかなる追加的なB−エピトープも欠く、項目1に記載の融合ポリペプチド。
(項目5)
前記第1のインターフェロンラムダアイソフォームが、IL29アイソフォームである、項目1に記載の融合ポリペプチド。
(項目6)
前記第2のインターフェロンラムダアイソフォームが、IL28Bアイソフォームである、項目1に記載の融合ポリペプチド。
(項目7)
前記第1のインターフェロンラムダアイソフォームが、IL29アイソフォームであり、前記第2のインターフェロンラムダアイソフォームが、IL28Bアイソフォームである、項目1に記載の融合ポリペプチド。
(項目8)
前記融合部位が、前記第1のインターフェロンラムダアイソフォームおよび前記第2のインターフェロンラムダアイソフォームにおける対応する配列と同一である少なくとも約8アミノ酸の配列を含む、項目1に記載の融合ポリペプチド。
(項目9)
式I:
(S1)−(ヘリックスA)−(S2)−(ヘリックスC)−(S3)−(ヘリックスD)−(S4)−(ヘリックスE)−(S5)−(ヘリックスF)−(S6)
の構造を有し、
a.ヘリックスDは、IL28B(配列番号2)の約V98〜Q112またはIL29(配列番号1)の約V89〜Q103の残基を有する断片に対し少なくとも90%の相同性を示すアミノ酸配列を含み、
b.ヘリックスEは、IL28B(配列番号2)の約R130〜E145またはIL29(配列番号1)の約R121〜E136の残基を有する断片に対し少なくとも90%の相同性を示すアミノ酸配列を含み、
c.S1、S2、S3、S4、S5およびS6のそれぞれは独立に、1〜約50個の間のアミノ酸残基を有するスペーサー配列である
融合ポリペプチドであって、
i.ヘリックスAが、IL28B(配列番号2)の約P27〜L44の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL29(配列番号1)の約R56〜A80の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL29(配列番号1)の約G139〜A161の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含む、または
ii.ヘリックスAが、IL29(配列番号1)の約P20〜L37の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL28B(配列番号2)の約R63〜A87の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL28B(配列番号2)の約G148〜A170の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含む、または
iii.ヘリックスAが、IL28B(配列番号2)の約P27〜L44の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL28B(配列番号2)の約R63〜A87の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL29(配列番号1)の約G139〜A161の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含む、または
iv.ヘリックスAが、IL29(配列番号1)の約P20〜L37の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL29(配列番号1)の約R56〜A80の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL28B(配列番号2)の約G148〜A170の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含む、または
v.ヘリックスAが、IL28B(配列番号2)の約P27〜L44の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL29(配列番号1)の約R56〜A80の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL28B(配列番号2)の約G148〜A170の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含む、または
vi.ヘリックスAが、IL29(配列番号1)の約P20〜L37の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスCが、IL28B(配列番号2)の約R63〜A87の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含み、ヘリックスFが、IL29(配列番号1)の約G139〜A161の残基を有する断片に対し少なくとも95%の相同性を示すアミノ酸配列を含むことを特徴とする融合ポリペプチド。
(項目10)
ヘリックスAが、IL28B(配列番号2)の約P27〜L44の残基を有する断片と同一である、項目9に記載の融合ポリペプチド。
(項目11)
ヘリックスAが、IL29(配列番号1)の約P20〜L37の残基を有する断片と同一である、項目9に記載の融合ポリペプチド。
(項目12)
ヘリックスCが、IL28B(配列番号2)の約R63〜A87の残基を有する断片と同一である、項目9に記載の融合ポリペプチド。
(項目13)
ヘリックスCが、IL29(配列番号1)の約R56〜A80の残基を有する断片と同一である、項目9に記載の融合ポリペプチド。
(項目14)
ヘリックスFが、IL28B(配列番号2)の約G148〜A170の残基を有する断片と同一である、項目9に記載の融合ポリペプチド。
(項目15)
ヘリックスFが、IL29(配列番号1)の約G139〜A161の残基を有する断片と同一である、項目9に記載の融合ポリペプチド。
(項目16)
S2が、ヘリックスBをさらに含む、項目9に記載の融合ポリペプチド。
(項目17)
IL28B(配列番号2)に対応するアミノ酸残基に少なくとも1個の修飾をさらに含み、該少なくとも1個の修飾が、dV2、dP3、dV4、dA5、dR6、dL7、dR8、G9K、A10P、L11T、P12T、D13T、A14G、R15K、A20G、Q21R、Q31A、A32S、R35K、K37R、L45K、D48N、C49W、K50S、R52S、R54P、L55V、R58G、T59N、Q64L、T88A、dD90、dT91、D92P、G96E、R114Q、T127P、C168S、C175S、P3G、V4P、A5V、R6P、L7TおよびR8Sからなる群から選択される、項目1または9に記載の融合ポリペプチド。
(項目18)
IL29(配列番号1)に対応するアミノ酸残基に少なくとも1個の修飾をさらに含み、該少なくとも1個の修飾が、R14Q、L57Q、A81T、82aD、82bT、G83D、E87G、Q105R、P118TおよびD162Eからなる群から選択される、項目1または9に記載の融合ポリペプチド。
(項目19)
IL28B(配列番号2)およびIL29(配列番号1)における対応する配列と同一である少なくとも約6アミノ酸の配列を含む融合部位をさらに含む、項目9に記載の融合ポリペプチド。
(項目20)
前記融合部位が、IL28B(配列番号2)およびIL29(配列番号1)における対応する配列と同一である少なくとも約8アミノ酸の配列を含む、項目19に記載の融合ポリペプチド。
(項目21)
前記融合部位が、前記少なくとも2種のインターフェロンラムダアイソフォームの対応する配列と同一である少なくとも約6〜25アミノ酸の配列を含む、項目1または9に記載の融合ポリペプチド。
(項目22)
IL28B(配列番号2)またはIL29(配列番号1)の二次構造を保持する、項目1または9に記載の融合ポリペプチド。
(項目23)
IL28B(配列番号2)またはIL29(配列番号1)の場合と比較して、いかなる追加的なT−エピトープも欠く、項目1または9に記載の融合ポリペプチド。
(項目24)
IL28B(配列番号2)またはIL29(配列番号1)の場合と比較して、いかなる追加的なB−エピトープも欠く、項目1または9に記載の融合ポリペプチド。
(項目25)
IL28B(配列番号2)またはIL29(配列番号1)に対し少なくとも90%の配列相同性を示す、項目1または9に記載の融合ポリペプチド。
(項目26)
IL28B(配列番号2)またはIL29(配列番号1)に対し少なくとも95%の配列相同性を示す、項目1または9に記載の融合ポリペプチド。
(項目27)
前記融合ポリペプチドのN末端が、ポリエチレングリコール(PEG)によってさらに修飾される、項目1または9に記載の融合ポリペプチド。
(項目28)
前記ポリエチレングリコールが、モノメトキシPEGプロピオンアルデヒドである、項目27に記載の融合ポリペプチド。
(項目29)
前記ポリエチレングリコールが、約12Kd〜40Kdの分子量を有する、項目27に記載の融合ポリペプチド。
(項目30)
前記ペグ化融合ポリペプチドが、IL28B(配列番号2)またはIL29(配列番号1)と比較して延長したin vivo半減期を示す、項目27に記載の融合ポリペプチド。
(項目31)
IL28B(配列番号2)またはIL29(配列番号1)と比較して増強した化学安定性を示す、項目1または9に記載の融合ポリペプチド。
(項目32)
配列番号3、配列番号4、配列番号5、配列番号6、配列番号7、配列番号8、配列番号9、配列番号10、配列番号11、配列番号12、配列番号13、配列番号14、配列番号15、配列番号16、配列番号17、配列番号18および配列番号19からなる群から選択されるアミノ酸配列を含む、項目1に記載の融合ポリペプチド。
(項目33)
項目1〜32のいずれか一項に記載の融合ポリペプチドを発現する宿主細胞。
(項目34)
原核細胞または真核細胞である、項目33に記載の宿主細胞。
(項目35)
ウイルス感染の処置を必要とする哺乳動物におけるウイルス感染を処置する方法であって、該哺乳動物に、治療有効量の項目1〜32のいずれか一項に記載の融合ポリペプチドを投与するステップを含む方法。
(項目36)
前記ウイルス感染が、B型肝炎、C型肝炎およびインフルエンザからなる群から選択されるウイルスによって与えられる、項目35に記載の方法。
(項目37)
炎症の処置を必要とする哺乳動物における炎症を処置する方法であって、該哺乳動物に、治療有効量の項目1〜32のいずれか一項に記載の融合ポリペプチドを投与するステップを含む方法。
(項目38)
前記炎症が、多発性硬化症である、項目37に記載の方法。
(項目39)
がんの処置を必要とする哺乳動物におけるがんを処置する方法であって、該哺乳動物に、治療有効量の項目1〜32のいずれか一項に記載の融合ポリペプチドを投与するステップを含む方法。
(項目40)
前記がんが、結腸がん、メラノーマおよび肝細胞癌から選択される、項目39に記載の方法。
(項目41)
項目1〜32のいずれか一項に記載の融合ポリペプチドのうち少なくとも1種と、薬学的に許容される賦形剤とを含む医薬組成物。
(項目42)
項目1〜32のいずれか一項に記載の融合ポリペプチドのうち少なくとも1種と、第2の治療剤とを含む医薬組成物。
(項目43)
項目1〜32のいずれか一項に記載の融合ポリペプチドをコードするポリヌクレオチドを含むベクター。
(項目44)
項目1〜32のいずれか一項に記載の融合ポリペプチドを産生する方法であって、タンパク質発現に適した条件下で、細胞において項目43に記載のベクターを発現させ、これにより、前記融合ポリペプチドを産生するステップを含む方法。
参照による援用
ポリペプチドの命名法
融合ポリペプチド、宿主細胞およびベクター
(S1)−(ヘリックスA)−(S2)−(ヘリックスC)−(S3)−(ヘリックスD)−(S4)−(ヘリックスE)−(S5)−(ヘリックスF)−(S6)(式中、ヘリックスA、ヘリックスC、ヘリックスD、ヘリックスEおよびヘリックスFのそれぞれは独立に、アルファヘリックスであり、S1、S2、S3、S4、S5およびS6のそれぞれは独立に、スペーサー配列である)
の構造を有することができる。
処置の方法
医薬組成物
IL28B/IL29融合ポリペプチドのクローニングおよび発現
配列番号1、2、3、4、5、6、7、8、9、10、11、12、13、14、15、16、17、18および19の融合ポリペプチドを設計し、E.coliにおいて発現させた。簡潔に説明すると、融合ポリペプチドをコードする遺伝子を、発現ベクターpET11cのNde1およびBamH1制限部位の間に挿入し、ファージT7プロモーターの制御下で発現を行った。このベクターをE.coli BL21(DE3)に形質転換した。100μg/mlのアンピシリンを補充したLB培地において、0.4〜0.6のOD450となるまで細胞を育成した。1mM IPTGの添加により12時間37℃で発現を誘導した。遠心分離により細胞を収集し、PBSに懸濁し、超音波処理した。細胞ホモジネートを遠心分離した。SDS−PAGE解析を行って、融合ポリペプチド、例えば、配列番号8および配列番号12の不溶性封入体画分における発現に成功したことを実証した(それぞれ図1&2)。
IL28B/IL29融合ポリペプチドのリフォールディングおよび精製
配列番号1、3、5、7、9、11、12、13、14、15、16および17の融合ポリペプチドを、次の通りにリフォールディングおよび精製した。50mM Tris pH8.0、6Mグアニジン、10mM DTTにおいて封入体ペレットを可溶化し、遠心分離により清澄化した。次に、可溶化された封入体を、50mM Tris pH7.8、1Mアルギニン、2mM GSH、1mM GSSGに対して4℃で一晩透析した(MWCO:3000)。リフォールディングされた融合ポリペプチドを、SP BB(GE Healthcare)を使用したカチオン交換クロマトグラフィー(50mM NaOAc、pH5.5、0〜1M NaCl)、続いてButyl Sepharose Fast Flow樹脂(GE Healthcare)を使用した疎水性相互作用クロマトグラフィー(50mM NaOAc、1〜0M(NH4)2SO4)によって精製した。SP HP樹脂(GE Healthcare)を使用したカチオン交換クロマトグラフィー(50mM NaOAc、pH5.5、0〜1M NaCl)により、さらなる精製を達成した。SDS−PAGE解析を行ったところ、一部の事例において、融合ポリペプチド(例えば、配列番号8)が、この方法により目に見える精製されたタンパク質を生じなかったが(図3)、他の事例においては、融合ポリペプチド(例えば、配列番号12)が、リフォールディングおよび精製に成功した(図4)ことが実証された。
N末端におけるIL28B/IL29融合ポリペプチドのペグ化
システインチオール部分におけるIL28B/IL29融合ポリペプチドのペグ化
IL28B/IL29融合ポリペプチドによるインターフェロン刺激遺伝子の誘導
抗ウイルス遺伝子誘導アッセイにおいて、IL28B/IL29融合ポリペプチドの抗ウイルス効果を評価した。このアッセイは、IL28B/IL29融合ポリペプチドの添加後に、Hep G2細胞(ATCC HB−8065)におけるインターフェロン刺激遺伝子(ISG)の誘導を測定した。
一例として、処理開始後12時間目に、参照IL−29ペプチド(配列番号1)および4種のIL−28B/IL−29融合ポリペプチド(配列番号3、5、7および12)は全て、Hep G2細胞におけるMxおよびOASの顕著な用量依存的誘導を示した(それぞれ図7&8)。10ng/mlまたはより高い濃度において、Mx発現は、200〜400倍増加し、OASレベルは、30〜60倍増加した。さらに、IL−28B/IL−29融合ポリペプチドは、参照IL−29タンパク質と同等のまたはそれより僅かに高いレベルで抗ウイルス遺伝子発現を誘導することを示した。
3時間の薬物処理後にMxおよびOAS発現の誘導が観察され、12時間後に最高誘導に達した(それぞれ図9&10)。
上述の実験において観察される効果を確認するために、95℃で5分間加熱することにより、IL−28B/IL−29融合ポリペプチドを変性させた。反復実験において陰性対照として組換えヒト成長ホルモンを使用した。結果は、IL−28B/IL−29融合ポリペプチドが先ず変性された場合、抗ウイルス遺伝子誘導が大幅に低下した一方、組換えヒト成長ホルモンによりMxおよびOAS発現における有意な効果が見られなかったことを示し、上述の実験において見られる活性が、IL−28B/IL−29融合ポリペプチドに固有であったことを示す(それぞれ図11&12)。
ペグ化IL−28B/IL−29融合ポリペプチドをさらに検査したところ、非修飾ポリペプチドと比較して、同様の抗ウイルス遺伝子誘導活性を保有することが示された(それぞれ図13&14)。
ペグ化IL−28B/IL−29融合ポリペプチドによるHuh−7.5.1細胞におけるHCV複製の阻害
HCVは、その制限された指向性のせいで従来の細胞培養物においては複製しない、一本鎖プラスセンスRNAウイルスである。細胞培養由来の感染性HCV(HCVcc)を使用した感染系の開発は、完全ウイルス複製サイクルの試験および全体的な感染性ウイルス生活環に関する創薬努力に大幅に役立った。
IL−28A/IL29融合ポリペプチドは、A549細胞におけるインフルエンザAウイルス複製を阻害する
インフルエンザウイルスの複製を阻害するIL−28B/IL29融合ポリペプチドの能力を、H3N2感染A549細胞(ヒト腺癌性肺胞基底上皮細胞)において検査した。A549細胞を被験タンパク質で24時間前処理し、続いてH3N2ウイルスに90分間感染させた;72時間後、細胞を固定し、抗NP抗体、続いて抗マウスHRPで免疫染色した;OD490nmで各ウェルの読み取り値を測定するELISAにより、薬物有効性を評価した。
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C11 | Written invitation by the commissioner to file amendments |
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A911 | Transfer to examiner for re-examination before appeal (zenchi) |
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C21 | Notice of transfer of a case for reconsideration by examiners before appeal proceedings |
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A912 | Re-examination (zenchi) completed and case transferred to appeal board |
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