JPH10504717A - 肺炎双球菌感染症に対する免疫化のための肺炎双球菌多糖−組み換えニューモリシン結合体ワクチン類 - Google Patents
肺炎双球菌感染症に対する免疫化のための肺炎双球菌多糖−組み換えニューモリシン結合体ワクチン類Info
- Publication number
- JPH10504717A JPH10504717A JP8508142A JP50814296A JPH10504717A JP H10504717 A JPH10504717 A JP H10504717A JP 8508142 A JP8508142 A JP 8508142A JP 50814296 A JP50814296 A JP 50814296A JP H10504717 A JPH10504717 A JP H10504717A
- Authority
- JP
- Japan
- Prior art keywords
- polysaccharide
- pneumoniae
- conjugate
- rpl
- coli
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
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- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/02—Bacterial antigens
- A61K39/09—Lactobacillales, e.g. aerococcus, enterococcus, lactobacillus, lactococcus, streptococcus
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- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
- C07K14/3156—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci from Streptococcus pneumoniae (Pneumococcus)
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
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- A61K39/02—Bacterial antigens
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- A61K39/092—Streptococcus
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Abstract
Description
Claims (1)
- 【特許請求の範囲】 1.(a)ストレプトコッカル ニューモニエ(Streptococcal pneumoniae;S. pneumoniae)の莢膜多糖由来の1個の酸化された多糖、および (b)組み換え的に発現されるS.ニューモニエ(S.pneumoniae)のニューモリ シンタンパク質であって、前記酸化された多糖との結合に先立ちトキソイド化さ れず、もしくは部位特異的突然変異誘発により産生されないニューモリシンタン パク質を含んで成る、免疫原性の多糖−タンパク質のある結合体。 2.S.ニューモニエ(S.pneumoniae)の莢膜多糖がタイプ14もしくはタイプ 18C由来である請求の範囲1の結合体。 3.組み換え的に発現されるニューモリシンがE.コリ(E.coli)において発現 される請求の範囲1の結合体。 4.組み換え的に発現されるニューモリシンがSCS1と命名されるE.コリ(E .coli)株において発現され、当該株がpGEX−PL 18Cと命名されるプ ラスミド(ATCC 69654)およびpGEX−PL 18C/20と命名 されるプラスミド(ATCC 69655)を含んで成るグループから選択され る1個のプラスミドを宿す請求の範囲3の結合体。 5.組み換え的に発現されるニューモリシンが、S.ニューモニエ(S.pneumonia e)の莢膜多糖由来の酸化された多糖との結合に先立ち、まずあるスペーサーに連 結されている請求の範囲1の結合体。 6.スペーサーがアジピン酸ジヒドラジド(ADH)および6−アミノヘキサン 酸を含んで成るグループから選択される、請求の範囲5の結合体。 7.請求の範囲1の免疫原性結合体を含むワクチン。 8.免疫学的に許容しうるある希釈剤、担体もしくは補助剤のひとつもしくはそ れ以上をさらに含む請求の範囲7のワクチン。 9.異なるタイプのS.ニューモニエ(S.pneumoniae)の莢膜多糖由来の酸化さ れた多糖との免疫原性結合体の最低2個の混合物を含む請求の範囲7のワクチン 。 10.温血動物においてS.ニューモニエ(S.pneumoniae)の莢膜多糖に対する 抗体応答を導き出すある方法であって、請求の範囲7のワクチンの免疫原性の量 を前記動物に投与することを含んで成る方法。 11.温血動物におけるS.ニューモニエ(S.pneumoniae)が原因の疾患に対す る免疫化のある方法であって、請求の範囲7のワクチンを免疫原性の量において 筋肉内、腹腔内もしくは皮下注入により前記動物に投与することを含んで成る方 法。 12.S.ニューモニエ(S.pneumoniae)のタイプ18C多糖の酸化された断片 の調製方法であって、前記多糖を弱酸で処理して前記多糖を10,000ないし600,00 0ダルトンの分子量にまで部分的に解重合し、その後、前記部分的に解重合され た多糖を、過ヨウ素酸ナトリウム、過ヨウ素酸カリウムおよび過ヨウ素酸を含ん で成るグループから選択される過ヨウ素酸塩で処理し、発熱物質を含まない水に 対して透析するかもしくはゲル濾過カラムクロマトグラフィーにより精製し、そ の後酸化された多糖を濃縮しそして凍結乾燥することを含んで成る方法。
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
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US08/295,305 US5565204A (en) | 1994-08-24 | 1994-08-24 | Pneumococcal polysaccharide-recombinant pneumolysin conjugate vaccines for immunization against pneumococcal infections |
US08/295,305 | 1994-08-24 | ||
PCT/US1995/010227 WO1996005859A1 (en) | 1994-08-24 | 1995-08-10 | Pneumococcal polysaccharide-recombinant pneumolysin conjugate vaccines for immunization against pneumococcal infections |
Publications (2)
Publication Number | Publication Date |
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JPH10504717A true JPH10504717A (ja) | 1998-05-12 |
JP3927233B2 JP3927233B2 (ja) | 2007-06-06 |
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Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
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JP50814296A Expired - Fee Related JP3927233B2 (ja) | 1994-08-24 | 1995-08-10 | 肺炎双球菌感染症に対する免疫化のための肺炎双球菌多糖−組み換えニューモリシン結合体ワクチン類 |
Country Status (14)
Country | Link |
---|---|
US (1) | US5565204A (ja) |
EP (1) | EP0778781B1 (ja) |
JP (1) | JP3927233B2 (ja) |
KR (1) | KR100385411B1 (ja) |
AT (1) | ATE198051T1 (ja) |
AU (1) | AU704450B2 (ja) |
CA (1) | CA2198251C (ja) |
DE (1) | DE69519634T2 (ja) |
DK (1) | DK0778781T3 (ja) |
ES (1) | ES2152421T3 (ja) |
GR (1) | GR3035081T3 (ja) |
IL (1) | IL115047A (ja) |
PT (1) | PT778781E (ja) |
WO (1) | WO1996005859A1 (ja) |
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JP2006506989A (ja) * | 2002-11-07 | 2006-03-02 | シナジー アメリカ,インコーポレイテッド | 肺炎球菌感染を治療または予防するための組成物および方法 |
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US7301554B2 (en) * | 2002-09-20 | 2007-11-27 | Ricoh Company, Ltd. | Light scanning device, scanning line adjusting method, scanning line adjusting control method, image forming apparatus, and image forming method |
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CA2844154C (en) | 2003-08-06 | 2016-12-20 | The Government Of The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Polysaccharide-protein conjugate vaccines |
US8048432B2 (en) | 2003-08-06 | 2011-11-01 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Polysaccharide-protein conjugate vaccines |
DE602004028262D1 (de) | 2003-10-02 | 2010-09-02 | Glaxosmithkline Biolog Sa | B. pertussis antigene und ihre verwendung bei der vakzinierung |
GB0410220D0 (en) | 2004-05-07 | 2004-06-09 | Kirkham Lea Ann | Mutant pneumolysin proteins |
GB0505996D0 (en) | 2005-03-23 | 2005-04-27 | Glaxosmithkline Biolog Sa | Fermentation process |
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US9370557B2 (en) * | 2006-06-15 | 2016-06-21 | The University Court Of The University Of Glasgow | Adjuvant compounds |
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AR064642A1 (es) | 2006-12-22 | 2009-04-15 | Wyeth Corp | Polinucleotido vector que lo comprende celula recombinante que comprende el vector polipeptido , anticuerpo , composicion que comprende el polinucleotido , vector , celula recombinante polipeptido o anticuerpo , uso de la composicion y metodo para preparar la composicion misma y preparar una composi |
BRPI0810211A2 (pt) | 2007-04-13 | 2014-10-21 | Univ Oklahoma | Citolisina dependente de colesterol mutante purficada, composição, vacina, método para vacinar um paciente, anticorpo monoclonal, ácido nucléico, e, célula hospedeira. |
EP2252326A4 (en) * | 2008-02-01 | 2012-08-29 | Newcastle Innovation Ltd | VACCINE COMPOSITIONS |
WO2010064437A1 (ja) | 2008-12-03 | 2010-06-10 | 株式会社カネカ | ホルミル基含有多孔質担体、それを用いた吸着体、およびそれらの製造方法 |
GB201003922D0 (en) | 2010-03-09 | 2010-04-21 | Glaxosmithkline Biolog Sa | Conjugation process |
JP2013521770A (ja) | 2010-03-10 | 2013-06-13 | グラクソスミスクライン バイオロジカルズ ソシエテ アノニム | ワクチン組成物 |
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GB201015132D0 (en) | 2010-09-10 | 2010-10-27 | Univ Bristol | Vaccine composition |
NZ607224A (en) | 2010-09-10 | 2014-11-28 | Wyeth Llc | Non-lipidated variants of neisseria meningitidis orf2086 antigens |
ITMI20111182A1 (it) | 2011-06-28 | 2012-12-29 | Canio Buonavoglia | Vaccino per coronavirus canino |
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SA115360586B1 (ar) | 2012-03-09 | 2017-04-12 | فايزر انك | تركيبات لعلاج الالتهاب السحائي البكتيري وطرق لتحضيرها |
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US9802987B2 (en) | 2013-03-08 | 2017-10-31 | Pfizer Inc. | Immunogenic fusion polypeptides |
EP4098276A1 (en) | 2013-09-08 | 2022-12-07 | Pfizer Inc. | Neisseria meningitidis compositions and methods thereof |
US9107906B1 (en) | 2014-10-28 | 2015-08-18 | Adma Biologics, Inc. | Compositions and methods for the treatment of immunodeficiency |
MX2017006625A (es) | 2014-11-21 | 2018-01-15 | Univ Oklahoma | Mutantes de neumolisina y metodos de uso de los mismos. |
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US11951165B2 (en) | 2016-12-30 | 2024-04-09 | Vaxcyte, Inc. | Conjugated vaccine carrier proteins |
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US10259865B2 (en) | 2017-03-15 | 2019-04-16 | Adma Biologics, Inc. | Anti-pneumococcal hyperimmune globulin for the treatment and prevention of pneumococcal infection |
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US10729763B2 (en) | 2017-06-10 | 2020-08-04 | Inventprise, Llc | Mixtures of polysaccharide-protein pegylated compounds |
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Family Cites Families (15)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4242501A (en) * | 1979-08-08 | 1980-12-30 | American Cyanamid Company | Purification of pneumococcal capsular polysaccharides |
US4356170A (en) * | 1981-05-27 | 1982-10-26 | Canadian Patents & Development Ltd. | Immunogenic polysaccharide-protein conjugates |
US5360897A (en) * | 1981-08-31 | 1994-11-01 | The University Of Rochester | Immunogenic conjugates of streptococcus pneumonial capsular polymer and toxin or in toxiad |
US4902506A (en) * | 1983-07-05 | 1990-02-20 | The University Of Rochester | Immunogenic conjugates |
US4673574A (en) * | 1981-08-31 | 1987-06-16 | Anderson Porter W | Immunogenic conjugates |
US4761283A (en) * | 1983-07-05 | 1988-08-02 | The University Of Rochester | Immunogenic conjugates |
US4686102A (en) * | 1984-04-12 | 1987-08-11 | American Cyanamid Company | Multivalent pneumococcal vaccine and preparation thereof |
NZ214503A (en) * | 1984-12-20 | 1990-02-26 | Merck & Co Inc | Covalently-modified neutral bacterial polysaccharides, stable covalent conjugates of such polysaccharides and immunogenic proteins, and methods of preparing such polysaccharides and conjugates |
US5192540A (en) * | 1988-04-19 | 1993-03-09 | American Cyanamid Company | Haemophilus influenzae type b oxidized polysaccharide-outer membrane protein conjugate vaccine |
IL92816A0 (en) * | 1988-12-22 | 1990-09-17 | Biogrowth Inc | Recombinant dna molecules,hosts,processes and human somatomedin carrier protein-like polypeptides |
IL95578A (en) * | 1989-09-15 | 1998-08-16 | Gen Hospital Corp | A vaccine made from polysaccharide and protein |
US5153312A (en) * | 1990-09-28 | 1992-10-06 | American Cyanamid Company | Oligosaccharide conjugate vaccines |
CA2059692C (en) * | 1991-01-28 | 2004-11-16 | Peter J. Kniskern | Pneumoccoccal polysaccharide conjugate vaccine |
US5371197A (en) * | 1991-09-24 | 1994-12-06 | Merck & Co., Inc. | Protein-dimeric polysaccharide conjugate vaccine |
US5445817A (en) * | 1992-08-21 | 1995-08-29 | The United States Of America As Represented By The Department Of Health And Human Services | Pertussis toxin used as a carrier protein with non-charged saccharides in conjugate vaccines |
-
1994
- 1994-08-24 US US08/295,305 patent/US5565204A/en not_active Expired - Fee Related
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1995
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JP2019163312A (ja) * | 2014-01-21 | 2019-09-26 | ファイザー・インク | 肺炎連鎖球菌(Streptococcus pneumoniae)莢膜多糖およびそのコンジュゲート |
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KR970705410A (ko) | 1997-10-09 |
IL115047A0 (en) | 1995-12-08 |
CA2198251C (en) | 2007-06-12 |
EP0778781B1 (en) | 2000-12-13 |
DK0778781T3 (da) | 2001-01-02 |
ES2152421T3 (es) | 2001-02-01 |
PT778781E (pt) | 2001-03-30 |
IL115047A (en) | 2005-08-31 |
GR3035081T3 (en) | 2001-03-30 |
US5565204A (en) | 1996-10-15 |
AU704450B2 (en) | 1999-04-22 |
AU3363695A (en) | 1996-03-14 |
DE69519634D1 (de) | 2001-01-18 |
CA2198251A1 (en) | 1996-02-29 |
KR100385411B1 (ko) | 2003-12-11 |
WO1996005859A1 (en) | 1996-02-29 |
JP3927233B2 (ja) | 2007-06-06 |
DE69519634T2 (de) | 2001-06-13 |
ATE198051T1 (de) | 2000-12-15 |
EP0778781A1 (en) | 1997-06-18 |
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