FI110613B - Kapsidia muodostava ja kysteiini-modifioitu kimeerinen MS2-vaippaproteiini - Google Patents

Kapsidia muodostava ja kysteiini-modifioitu kimeerinen MS2-vaippaproteiini Download PDF

Info

Publication number: FI110613B
Authority: FI; Finland
Prior art keywords: protein; att; modified; modifierat; enligt
Prior art date: 1991-06-28

Application number

FI935877A

Other languages

English (en)

Finnish (fi)

Swedish (sv)

Other versions

FI935877L (fi

FI935877A0 (fi

Inventor

Robert Allan Mastico

Peter George Stockley

Original Assignee

British Tech Group

Priority date (The priority date 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 date listed.)

1991-06-28

Filing date

1993-12-27

Publication date

2003-02-28

1993-12-27 Application filed by British Tech Group filed Critical British Tech Group

1993-12-27 Publication of FI935877L publication Critical patent/FI935877L/fi

1993-12-27 Publication of FI935877A0 publication Critical patent/FI935877A0/fi

2003-02-28 Application granted granted Critical

2003-02-28 Publication of FI110613B publication Critical patent/FI110613B/fi

Links

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Classifications

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- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
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- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
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- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/54—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic compound
- A—HUMAN NECESSITIES
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- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/54—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic compound
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
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- C12N2760/00011—Details
- C12N2760/16011—Orthomyxoviridae
- C12N2760/16022—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes

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FI935877A 1991-06-28 1993-12-27 Kapsidia muodostava ja kysteiini-modifioitu kimeerinen MS2-vaippaproteiini FI110613B (fi)

Applications Claiming Priority (4)

Application Number	Priority Date	Filing Date	Title
GB919114003A GB9114003D0 (en)	1991-06-28	1991-06-28	Chimaeric protein
GB9114003		1991-06-28
GB9201159		1992-06-26
PCT/GB1992/001159 WO1993000434A1 (fr)	1991-06-28	1992-06-26	Proteine chimerique d'enveloppe de ms2 formant capside et modifiee par cysteine

Publications (3)

Publication Number	Publication Date
FI935877L FI935877L (fi)	1993-12-27
FI935877A0 FI935877A0 (fi)	1993-12-27
FI110613B true FI110613B (fi)	2003-02-28

Family

ID=10697502

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
FI935877A FI110613B (fi)	1991-06-28	1993-12-27	Kapsidia muodostava ja kysteiini-modifioitu kimeerinen MS2-vaippaproteiini

Country Status (15)

Country	Link
US (1)	US5698424A (fr)
EP (1)	EP0591369B1 (fr)
JP (1)	JP3514755B2 (fr)
KR (1)	KR100222163B1 (fr)
AT (1)	ATE205880T1 (fr)
AU (1)	AU657560B2 (fr)
CA (1)	CA2111683A1 (fr)
DE (1)	DE69232069T2 (fr)
FI (1)	FI110613B (fr)
GB (2)	GB9114003D0 (fr)
IE (1)	IE922085A1 (fr)
NO (1)	NO315050B1 (fr)
NZ (1)	NZ243330A (fr)
WO (1)	WO1993000434A1 (fr)
ZA (1)	ZA924774B (fr)

Families Citing this family (36)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB9213601D0 (en) *	1992-06-26	1992-08-12	Mastico Robert A	Protein based delivery system
DE19618797C2 (de) *	1996-05-10	2000-03-23	Bertling Wolf	Vehikel zum Transport molekularer Substanz
DE69929232T2 (de) *	1998-10-21	2006-08-31	The United States Government As Represented By The Department Of Health And Human Services	Virusähnliche partikel zur induktion von autoantikörpern
DK1135162T3 (da) *	1998-11-30	2009-01-19	Cytos Biotechnology Ag	Ordnet molekylær præsentation af allergener, fremstillingsfremgangsmåde samt anvendelse
DE19916224C1 (de)	1999-04-10	2000-06-21	November Ag Molekulare Medizin	Synthetisches biologisch aktives Molekül
PT1144607E (pt) *	1999-07-20	2009-04-22	Morphosys Ag	Novos métodos para apresentar (poli)peptídeos/ proteínas em partículas bacteriofágicas através de ligações dissulfureto
CA2407897A1 (fr)	2000-05-05	2001-11-15	Cytos Biotechnology Ag	Jeu ordonne d'antigenes moleculaires
AU2007202761B2 (en) *	2001-01-19	2010-01-21	Kuros Biosciences Ag	Molecular antigen array
US7094409B2 (en) *	2001-01-19	2006-08-22	Cytos Biotechnology Ag	Antigen arrays for treatment of allergic eosinophilic diseases
US7128911B2 (en)	2001-01-19	2006-10-31	Cytos Biotechnology Ag	Antigen arrays for treatment of bone disease
US7320793B2 (en) *	2001-01-19	2008-01-22	Cytos Biotechnology Ag	Molecular antigen array
RU2294211C2 (ru) *	2001-01-19	2007-02-27	Цитос Байотекнолоджи Аг	Композиция и способ для иммунизации, способ продуцирования неприродного, упорядоченного и повторяющегося массива антигенов
AU2002339224B2 (en) *	2001-09-14	2008-10-09	Kuros Us Llc	Packaging of immunostimulatory substances into virus-like particles: method of preparation and use
WO2003024480A2 (fr) *	2001-09-14	2003-03-27	Cytos Biotechnology Ag	Activation in vivo de cellules presentant un antigene en vue d'augmenter les reponses immunes induites par des particules de type virus
US7115266B2 (en) *	2001-10-05	2006-10-03	Cytos Biotechnology Ag	Angiotensin peptide-carrier conjugates and uses thereof
BR0213117A (pt)	2001-10-05	2004-09-21	Cytos Biotechnology Ag	Conjugados peptìdeo angiotensina-veìculo e seus usos
JP4658475B2 (ja) *	2001-11-07	2011-03-23	サイトスバイオテクノロジーアーゲー	骨疾患治療用の抗原アレイ
US20030219459A1 (en) *	2002-01-18	2003-11-27	Cytos Biotechnology Ag	Prion protein carrier-conjugates
WO2004000351A1 (fr) *	2002-06-20	2003-12-31	Cytos Biotechnology Ag	Particules pseudo-virales enveloppees destinees a etre utilisees en tant qu'adjuvants: procede de preparation et utilisation de celles-ci
BR0312935A (pt)	2002-07-17	2005-06-21	Cytos Biotechnology Ag	Partìcula semelhante a vìrus, muteìna, vetores para produzir a referida partìcula e proteìna recombinante, composição, processo para produção de fileira ordena e repetitva de antìgeno, molécula de ácido nucléico, célula hospedeira, método para produção da referida partìcula e uso da composição de vacina
CN101574518B (zh) *	2002-07-18	2012-08-22	赛托斯生物技术公司	半抗原-载体偶联物及其用途
NZ537688A (en) *	2002-07-19	2007-01-26	Cytos Biotechnology Ag	Vaccine compositions containing amyloid beta1-6 antigen arrays for treating and/or attenuating Alzheimer's disease
US20060210588A1 (en) *	2003-03-26	2006-09-21	Cytos Biotechnology Ag	Hiv-peptide-carrier-conjugates
AU2004224761A1 (en) *	2003-03-26	2004-10-07	Cytos Biotechnology Ag	HIV-peptide-carrier-conjugates
US7537767B2 (en) *	2003-03-26	2009-05-26	Cytis Biotechnology Ag	Melan-A- carrier conjugates
JP2007518762A (ja) *	2004-01-20	2007-07-12	サイトスバイオテクノロジーアーゲー	グレリン−担体結合体
MXPA06013854A (es) *	2004-06-02	2007-03-02	Cytos Biotechnology Ag	Usos medicos de conjugados portadores de peptidos del factor de necrosis tumoral, no humanos.
WO2006037787A2 (fr) *	2004-10-05	2006-04-13	Cytos Biotechnology Ag	Conjugues vlp-antigene et leur utilisation comme vaccins
JP2008517975A (ja) *	2004-10-25	2008-05-29	サイトスバイオテクノロジーアーゲー	胃酸分泌抑制ポリペプチド（ｇｉｐ）抗原アッセイ及びその使用
GB0424563D0 (en) *	2004-11-05	2004-12-08	Novartis Ag	Organic compounds
EP1855723B1 (fr)	2005-03-08	2013-05-22	Ramot at Tel-Aviv University Ltd.	Bacteriophages transportant des medicaments cibles
RU2414239C2 (ru) *	2005-03-18	2011-03-20	Цитос Биотехнологи Аг	Белки, слитые с кошачьим аллергеном, и их применение
CA2623287A1 (fr)	2005-09-28	2007-04-12	Cytos Biotechnology Ag	Conjuges d'interleukin-1 et leurs utilisations
US20070184068A1 (en)	2005-12-14	2007-08-09	Cytos Biotechnology Ag	Immunostimulatory nucleic acid packaged particles for the treatment of hypersensitivity
MX2008015529A (es)	2006-06-12	2009-01-13	Cytos Biotechnology Ag	Procesos para empacar oligonucleotidos en particulas similares a virus de bacteriofagos de arn.
EP2190987B1 (fr) *	2007-08-21	2012-11-14	MorphoSys AG	Procédés permettant la formation de liaisons disulfure

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB9101550D0 (en) *	1991-01-24	1991-03-06	Mastico Robert A	Antigen-presenting chimaeric protein

1991
- 1991-06-28 GB GB919114003A patent/GB9114003D0/en active Pending
1992
- 1992-06-26 US US08/167,982 patent/US5698424A/en not_active Expired - Fee Related
- 1992-06-26 JP JP50123093A patent/JP3514755B2/ja not_active Expired - Fee Related
- 1992-06-26 KR KR1019930703986A patent/KR100222163B1/ko not_active Expired - Fee Related
- 1992-06-26 EP EP92913894A patent/EP0591369B1/fr not_active Expired - Lifetime
- 1992-06-26 AU AU21955/92A patent/AU657560B2/en not_active Ceased
- 1992-06-26 WO PCT/GB1992/001159 patent/WO1993000434A1/fr not_active Ceased
- 1992-06-26 ZA ZA924774A patent/ZA924774B/xx unknown
- 1992-06-26 NZ NZ243330A patent/NZ243330A/en unknown
- 1992-06-26 AT AT92913894T patent/ATE205880T1/de not_active IP Right Cessation
- 1992-06-26 DE DE69232069T patent/DE69232069T2/de not_active Expired - Fee Related
- 1992-06-26 CA CA002111683A patent/CA2111683A1/fr not_active Abandoned
- 1992-06-26 GB GB9213644A patent/GB2257431B/en not_active Revoked
- 1992-07-01 IE IE208592A patent/IE922085A1/en not_active Application Discontinuation
1993
- 1993-12-27 NO NO19934842A patent/NO315050B1/no not_active IP Right Cessation
- 1993-12-27 FI FI935877A patent/FI110613B/fi active

Also Published As

Publication number	Publication date
NO315050B1 (no)	2003-06-30
AU2195592A (en)	1993-01-25
DE69232069T2 (de)	2002-01-31
FI935877L (fi)	1993-12-27
JP3514755B2 (ja)	2004-03-31
GB2257431A (en)	1993-01-13
AU657560B2 (en)	1995-03-16
NO934842L (no)	1994-02-28
GB9213644D0 (en)	1992-08-12
WO1993000434A1 (fr)	1993-01-07
FI935877A0 (fi)	1993-12-27
CA2111683A1 (fr)	1993-01-07
ATE205880T1 (de)	2001-10-15
KR100222163B1 (ko)	1999-10-01
KR940701447A (ko)	1994-05-28
EP0591369A1 (fr)	1994-04-13
EP0591369B1 (fr)	2001-09-19
ZA924774B (en)	1993-04-22
NZ243330A (en)	1994-06-27
JPH06509223A (ja)	1994-10-20
GB2257431B (en)	1995-04-19
US5698424A (en)	1997-12-16
NO934842D0 (no)	1993-12-27
GB9114003D0 (en)	1991-08-14
DE69232069D1 (de)	2001-10-25
IE922085A1 (en)	1992-12-30

Publication	Publication Date	Title
FI110613B (fi)	2003-02-28	Kapsidia muodostava ja kysteiini-modifioitu kimeerinen MS2-vaippaproteiini
JP3634358B2 (ja)	2005-03-30	タンパク質に基づく輸送系
JP2974028B2 (ja)	1999-11-08	アドヒシン抗原類
CN100435846C (zh)	2008-11-26	用于口蹄疫的合成肽疫苗
JP2858848B2 (ja)	1999-02-17	Ｂ型肝炎ウイルスコア抗原粒子
JPH06504907A (ja)	1994-06-09	抗原発現キメラタンパク質
WO1999067294A1 (fr)	1999-12-29	Complexe antigenique comprenant un peptide immunostimulateur, cd4 et un domaine de recepteur de chemokine pour traiter vih et des maladies immunitaires
EA006207B1 (ru)	2005-10-27	ИММУНОГЕННЫЕ ХИМЕРНЫЕ ЧАСТИЦЫ НВс, ОБЛАДАЮЩИЕ ПОВЫШЕННОЙ СТАБИЛЬНОСТЬЮ
JP2002509700A (ja)	2002-04-02	戦略的修飾されたｂ型肝炎コアタンパク質及びそれらの誘導体
JP3764476B2 (ja)	2006-04-05	組合せポリペプチド抗原
JP3135060B2 (ja)	2001-02-13	ヘモフィルスインフルエンザｂ型菌の外皮膜タンパク質Ｐ２の部分断片を用いた接合体
US5916562A (en)	1999-06-29	Membrane proteins and peptides of haemophilus influenzae type B
JPS59173084A (ja)	1984-09-29	ポリオウイルスの免疫原性部位よりなるペプチド類及びこれらのペプチド類を暗合化するヌクレオチド配列を含有するｄｎａ類
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JPH03503359A (ja)	1991-08-01	外来シグナルペプチド及び任意のトランスメンブレンアンカー配列を包含する遺伝子発現系（特にロタウイルスｖｐ７タンパク質）
JPH03501684A (ja)	1991-04-18	Ｈｉｖ抗原の製法およびその系