SK2232001A3 - Process for purifying human papillomavirus virus-like particles - Google Patents

Process for purifying human papillomavirus virus-like particles Download PDF

Info

Publication number: SK2232001A3
Authority: SK; Slovakia
Prior art keywords: vlps; hpv; protein; vlp; hpv type
Prior art date: 1998-08-14

Application number

SK223-2001A

Other languages

English (en)

Slovak (sk)

Inventor

James C Cook

Original Assignee

Merck & Co Inc

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.)

1998-08-14

Filing date

1999-08-10

Publication date

2001-08-06

1999-08-10 Application filed by Merck & Co Inc filed Critical Merck & Co Inc

2001-08-06 Publication of SK2232001A3 publication Critical patent/SK2232001A3/sk

Links

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Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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SK223-2001A 1998-08-14 1999-08-10 Process for purifying human papillomavirus virus-like particles SK2232001A3 (en)

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US9656898P	1998-08-14	1998-08-14
PCT/US1999/017930 WO2000009671A1 (en)	1998-08-14	1999-08-10	Process for purifying human papillomavirus virus-like particles

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SK223-2001A SK2232001A3 (en)	1998-08-14	1999-08-10	Process for purifying human papillomavirus virus-like particles

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US (1)	US6602697B1 (zh)
EP (1)	EP1105466B1 (zh)
JP (1)	JP4440471B2 (zh)
KR (1)	KR20010072470A (zh)
CN (1)	CN1354787A (zh)
AT (1)	ATE324436T1 (zh)
AU (1)	AU760633B2 (zh)
BR (1)	BR9913026A (zh)
CA (1)	CA2339034C (zh)
CY (1)	CY1105084T1 (zh)
CZ (1)	CZ2001570A3 (zh)
DE (1)	DE69931053T2 (zh)
DK (1)	DK1105466T3 (zh)
EA (1)	EA200100236A1 (zh)
ES (1)	ES2262333T3 (zh)
HR (1)	HRP20010113A2 (zh)
HU (1)	HUP0103091A3 (zh)
IL (1)	IL141130A0 (zh)
NZ (1)	NZ509610A (zh)
PL (1)	PL347472A1 (zh)
PT (1)	PT1105466E (zh)
SI (1)	SI1105466T1 (zh)
SK (1)	SK2232001A3 (zh)
WO (1)	WO2000009671A1 (zh)

Families Citing this family (36)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
PL201482B1 (pl) *	1998-10-16	2009-04-30	Smithkline Beecham Biolog	Sposoby wytwarzania kompozycji szczepionki oraz kompozycja szczepionki
JP2000262280A (ja) *	1999-03-18	2000-09-26	Asahi Optical Co Ltd	ウィルスまたはウィルス性抗原の精製方法およびワクチンの製造方法
US6436402B1 (en) *	1999-10-15	2002-08-20	Merck & Co., Inc.	Process for making human papillomavirus virus-like particles with improved properties
GB0206360D0 (en)	2002-03-18	2002-05-01	Glaxosmithkline Biolog Sa	Viral antigens
MY139500A (en) *	2003-11-12	2009-10-30	Merck Sharp & Dohme	Optimized expression of hpv 58 l1 in yeast
SG150501A1 (en) *	2004-02-05	2009-03-30	Millipore Corp	Porous adsorptive or chromatographic media
PT1730175E (pt) *	2004-03-24	2010-06-25	Merck Sharp & Dohme	Expressão optimizada de hpv 52 l1 em levedura
DE602005022458D1 (de)	2004-09-10	2010-09-02	Asahi Glass Co Ltd	Impfstoff gegen humanes papillomavirus zur oralen verabreichung
EP1736538A1 (en) *	2005-06-21	2006-12-27	Cytos Biotechnology AG	Process for the preparative purification of virus-like-particles (VLPs)
WO2008027861A1 (en) *	2006-08-30	2008-03-06	Ge Healthcare Bio-Sciences Corp.	System and method for characterizing membranes and membrane filtration devices
SG174845A1 (en)	2006-09-29	2011-10-28	Ligocyte Pharmaceuticals Inc	Norovirus vaccine formulations
CA2677023C (en) *	2007-02-22	2016-08-30	Baxter International Inc.	Method of purification of hydrophobic proteins
KR20150098681A (ko)	2007-03-14	2015-08-28	다케다 백신즈 인코포레이티드	바이러스 유사 입자 정제
DK2147926T3 (en)	2007-04-29	2016-11-28	Beijing Wantai Biological Pharmacy Entpr Co Ltd	Truncated human papillomavirus type 18 L1 protein
BRPI0811016B1 (pt)	2007-04-29	2021-09-21	Xiamen Innovax Biotech Co., Ltd.	Proteína li truncada do papiloma vírus humano tipo 16
BRPI0810951B8 (pt) *	2007-05-29	2021-05-25	Beijing Wantai Biological Pharmacy Entpr Co Ltd	proteína l1 do hpv6, polinucleotídeo, vetor, célula, partícula semelhante ao vírus (vlp) hpv6, método para produzir a proteína hpv6 l1 truncada, vacina para prevenção de condiloma acuminado ou de infecções por hpv, uso da proteína hpv6 l1 truncada, método para prevenção de condiloma acuminado ou infecções por hpv, método para obter uma vlp de uma proteína l1 do hpv6 e método para produzir uma vacina para a prevenção de condiloma acuminado ou de infecções por hpv
US9433922B2 (en) *	2007-08-14	2016-09-06	Emd Millipore Corporation	Media for membrane ion exchange chromatography based on polymeric primary amines, sorption device containing that media, and chromatography scheme and purification method using the same
US20100266636A1 (en)	2007-09-18	2010-10-21	Ligocyte Pharmaceuticals, Inc.	Method of conferring a protective immune response to norovirus
JP2010539192A (ja) *	2007-09-18	2010-12-16	リゴサイトファーマスーティカルズ，インコーポレイテッド	ノロウイルスに対して防御免疫応答を付与する方法
DE602007007927D1 (de) *	2007-11-05	2010-09-02	Agilent Technologies Inc	Einfrierung eines mikrofluidischen Chips
US20090130738A1 (en) *	2007-11-19	2009-05-21	Mikhail Kozlov	Media for membrane ion exchange chromatography
KR101793161B1 (ko) *	2008-08-08	2017-11-03	다케다 백신즈 인코포레이티드	강화된 교차 반응성을 가진 복합체 캡시드 아미노산 서열들을 포함하는 바이러스-유사 입자들
EP2524215B1 (en) *	2010-01-15	2018-12-26	Bio-Rad Laboratories, Inc.	Surface neutralization of apatite
CN102985536B (zh)	2010-04-14	2017-12-05	Emd密理博公司	生产高效价、高纯度的病毒母液的方法及使用其的方法
US8895707B2 (en)	2010-08-18	2014-11-25	Bio-Rad Laboratories, Inc.	Elution of proteins from hydroxyapatite resins without resin deterioration
JP5881744B2 (ja)	2011-02-02	2016-03-09	バイオ−ラッドラボラトリーズインコーポレーティッド	アルカリ溶液でのアパタイトの表面中和方法
ES2656527T3 (es)	2011-07-11	2018-02-27	Takeda Vaccines, Inc.	Formulaciones parenterales de vacunas de norovirus
MY184076A (en) *	2011-12-01	2021-03-17	Univ Cape Town	Hpv chimaeric particle
WO2013180933A1 (en)	2012-05-30	2013-12-05	Bio-Rad Laboratories, Inc.	In situ restoration of apatite-based chromatography resins
JOP20130186B1 (ar)	2012-06-22	2021-08-17	Takeda Vaccines Montana Inc	تنقية الجزيئات الشبيهة بالفيروسات
KR101559622B1 (ko)	2012-07-30	2015-10-13	중앙대학교 산학협력단	인유두종바이러스 바이러스 유사입자의 고효율 정제방법
JP6479305B2 (ja) *	2013-07-12	2019-03-06	株式会社Ｕｍｎファーマ	ウイルス様粒子の精製方法
EP3157689B1 (en)	2014-06-23	2021-04-28	Bio-Rad Laboratories, Inc.	Apatite pretreatment
EP3157863B1 (en)	2014-06-23	2023-06-21	Bio-Rad Laboratories, Inc.	Apatite in-situ restoration
CN105907729B (zh) *	2015-05-05	2019-08-16	广东东阳光药业有限公司	一种制备人***瘤病毒l1蛋白类病毒样颗粒的方法
CN108524929B (zh) *	2017-03-06	2019-05-07	广州瑞贝斯药业有限公司	一种狂犬病疫苗的生产方法

Family Cites Families (8)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS6078999A (ja)	1983-10-05	1985-05-04	Chemo Sero Therapeut Res Inst	ＨＢｓ抗原の精製方法
SE9000650L (sv)	1989-02-28	1990-08-29	Asahi Optical Co Ltd	Separation av celler eller virus
ATE328068T1 (de) *	1994-05-16	2006-06-15	Merck & Co Inc	Papillomavirus vakzine
SK35897A3 (en) *	1994-09-22	1998-02-04	Merck & Co Inc	Isolated and purified dna molecule, encoding human papillomavirus type 6a, method of expression, pharmaceutical composition, a vaccine and use
AR004464A1 (es) *	1994-11-14	1998-12-16	Merck Sharp & Dohme	Un metodo para producir una proteina de capside de papilomavirus
IL117459A (en) *	1995-03-22	2005-11-20	Merck & Co Inc	Dna encoding human papillomavirus type 18
IL117591A0 (en) *	1995-03-30	1996-07-23	Merck & Co Inc	Synthetic DNA encoding human papillomavirus type 11 L1 protein
CA2625279A1 (en)	1995-08-30	1997-03-06	Genzyme Corporation	Chromatographic purification of adenovirus and aav

1999
- 1999-08-10 BR BR9913026A patent/BR9913026A/pt not_active Application Discontinuation
- 1999-08-10 CZ CZ2001570A patent/CZ2001570A3/cs unknown
- 1999-08-10 IL IL14113099A patent/IL141130A0/xx unknown
- 1999-08-10 ES ES99940950T patent/ES2262333T3/es not_active Expired - Lifetime
- 1999-08-10 SI SI9930901T patent/SI1105466T1/sl unknown
- 1999-08-10 AU AU54698/99A patent/AU760633B2/en not_active Expired
- 1999-08-10 PL PL34747299A patent/PL347472A1/xx unknown
- 1999-08-10 SK SK223-2001A patent/SK2232001A3/sk unknown
- 1999-08-10 DK DK99940950T patent/DK1105466T3/da active
- 1999-08-10 CN CN99811968A patent/CN1354787A/zh active Pending
- 1999-08-10 AT AT99940950T patent/ATE324436T1/de active
- 1999-08-10 DE DE1999631053 patent/DE69931053T2/de not_active Expired - Lifetime
- 1999-08-10 JP JP2000565108A patent/JP4440471B2/ja not_active Expired - Lifetime
- 1999-08-10 PT PT99940950T patent/PT1105466E/pt unknown
- 1999-08-10 US US09/762,662 patent/US6602697B1/en not_active Expired - Lifetime
- 1999-08-10 NZ NZ50961099A patent/NZ509610A/xx not_active IP Right Cessation
- 1999-08-10 CA CA 2339034 patent/CA2339034C/en not_active Expired - Lifetime
- 1999-08-10 HU HU0103091A patent/HUP0103091A3/hu unknown
- 1999-08-10 EA EA200100236A patent/EA200100236A1/ru unknown
- 1999-08-10 WO PCT/US1999/017930 patent/WO2000009671A1/en active IP Right Grant
- 1999-08-10 KR KR1020017001885A patent/KR20010072470A/ko not_active Application Discontinuation
- 1999-08-10 EP EP99940950A patent/EP1105466B1/en not_active Expired - Lifetime
2001
- 2001-02-14 HR HR20010113A patent/HRP20010113A2/hr not_active Application Discontinuation
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Publication number	Publication date
HUP0103091A3 (en)	2002-03-28
US6602697B1 (en)	2003-08-05
DE69931053T2 (de)	2006-11-23
CA2339034A1 (en)	2000-02-24
CY1105084T1 (el)	2009-11-04
SI1105466T1 (sl)	2006-08-31
PT1105466E (pt)	2006-07-31
CA2339034C (en)	2010-10-12
EP1105466B1 (en)	2006-04-26
HUP0103091A2 (hu)	2001-12-28
NZ509610A (en)	2002-10-25
AU760633B2 (en)	2003-05-22
PL347472A1 (en)	2002-04-08
EP1105466A1 (en)	2001-06-13
JP2003520188A (ja)	2003-07-02
JP4440471B2 (ja)	2010-03-24
EA200100236A1 (ru)	2001-08-27
EP1105466A4 (en)	2002-05-15
DE69931053D1 (de)	2006-06-01
WO2000009671A1 (en)	2000-02-24
CZ2001570A3 (cs)	2001-09-12
CN1354787A (zh)	2002-06-19
ES2262333T3 (es)	2006-11-16
ATE324436T1 (de)	2006-05-15
IL141130A0 (en)	2002-02-10
DK1105466T3 (da)	2006-08-14
KR20010072470A (ko)	2001-07-31
BR9913026A (pt)	2001-09-25
HRP20010113A2 (en)	2002-02-28
AU5469899A (en)	2000-03-06

Publication	Publication Date	Title
AU760633B2 (en)	2003-05-22	Process for purifying human papillomavirus virus-like particles
Cook et al.	1999	Purification of virus-like particles of recombinant human papillomavirus type 11 major capsid protein L1 from Saccharomyces cerevisiae
Kim et al.	2010	One-step chromatographic purification of human papillomavirus type 16 L1 protein from Saccharomyces cerevisiae
KR101576219B1 (ko)	2015-12-10	바이러스 유사 입자 정제
JPS61158795A (ja)	1986-07-18	アデノウイルスプロモ−タ−の制御下で所定のポリペプチドをコ−ドしているヌクレオチド配列を含む組換えｄｎａ
GB2604692A (en)	2022-09-14	Method for preparing recombinant subunit vaccine against novel coronavirus
SUN et al.	1995	Sequences required for the nuclear targeting and accumulation of human papillomavirus type 6B L2 protein
RU2161651C2 (ru)	2001-01-10	Очищенные белки вируса папилломы
WO2002004007A9 (en)	2002-10-10	Stable (fixed) forms of viral capsid proteins, fusion proteins and uses thereof
Roldão et al.	2011	Quality control and analytical methods for baculovirus-based products
KR20230118619A (ko)	2023-08-11	아데노바이러스의 정제 방법
WO2007134325A2 (en)	2007-11-22	Methods and compositions for protein production using adenoviral vectors
AU753391B2 (en)	2002-10-17	Protein delivery system using human papillomavirus virus-like particles
JPH03191790A (ja)	1991-08-21	酵母から得られる組換え肝炎ｂ型ウイルス表面タンパク質を安定化する方法
KR101559622B1 (ko)	2015-10-13	인유두종바이러스 바이러스 유사입자의 고효율 정제방법
Rosmeita et al.	2023	Expression, purification, and characterization of self-assembly virus-like particles of capsid protein L1 HPV 52 in Pichia pastoris GS115
Swartz et al.	2022	Binding of Coxsackievirus A21 procapsids to immobilized glutathione depends on cell culture conditions during infection
Willis et al.	1998	Expression and purification of secreted forms of HSV glycoproteins from baculovirus-infected insect cells
MXPA01001647A (en)	2001-11-21	Process for purifying human papillomavirus virus-like particles
JPH0734753B2 (ja)	1995-04-19	組換え宿主細胞から得られる組換えｂ型肝炎ウイルス表面タンパク質の安定化方法
US5077213A (en)	1991-12-31	Recombinant vaccinia virus
JPH02475A (ja)	1990-01-05	Ｖｅｒｏ細胞、酵母細胞又はｌ細胞からの組換えエプスタイン−バールウイルス抗原の精製
CA2355883A1 (en)	2000-07-06	Neutralizing assay using human papillomavirus virus-like particles
WO2015128788A1 (en)	2015-09-03	Purification of papillomavirus l2 protein
CA2182272C (en)	2006-03-21	Modified papilloma virus l2 protein and vlps formed therefrom