AU3578199A – Process for separating HIV from a fluid
– Google Patents
AU3578199A – Process for separating HIV from a fluid
– Google Patents
Process for separating HIV from a fluid
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Publication number
AU3578199A
AU3578199A
AU35781/99A
AU3578199A
AU3578199A
AU 3578199 A
AU3578199 A
AU 3578199A
AU 35781/99 A
AU35781/99 A
AU 35781/99A
AU 3578199 A
AU3578199 A
AU 3578199A
AU 3578199 A
AU3578199 A
AU 3578199A
Authority
AU
Australia
Prior art keywords
hiv
inhibitor
fluid
blood
impregnated
Prior art date
1998-06-22
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
Application number
AU35781/99A
Other versions
AU745851B2
(en
Inventor
Albrecht Groner
Jurgen Romisch
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
CSL Behring GmbH Deutschland
Original Assignee
Aventis Behring GmbH
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.)
1998-06-22
Filing date
1999-06-21
Publication date
2000-01-06
1999-06-21
Application filed by Aventis Behring GmbH
filed
Critical
Aventis Behring GmbH
2000-01-06
Publication of AU3578199A
publication
Critical
patent/AU3578199A/en
2000-06-15
Assigned to AVENTIS BEHRING GMBH
reassignment
AVENTIS BEHRING GMBH
Amend patent request/document other than specification (104)
Assignors: CENTEON PHARMA GMBH
2002-04-11
Application granted
granted
Critical
2002-04-11
Publication of AU745851B2
publication
Critical
patent/AU745851B2/en
2019-06-21
Anticipated expiration
legal-status
Critical
Status
Ceased
legal-status
Critical
Current
Links
Espacenet
Global Dossier
Discuss
238000000034
method
Methods
0.000
title
claims
description
20
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process
Effects
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title
claims
description
18
239000012530
fluid
Substances
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title
claims
description
11
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blood
Anatomy
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claims
description
17
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blood
Substances
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claims
description
17
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c1 esterase inhibitor
Drugs
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claims
description
9
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fiber
Substances
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claims
description
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plasma
Anatomy
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description
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fibrous material
Substances
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claims
description
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material
Substances
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claims
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serum
Anatomy
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description
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affinity chromatography
Methods
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description
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matrix material
Substances
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claims
description
3
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Crataegus X brevipes
Nutrition
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claims
1
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Crataegus X haemacarpa
Nutrition
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claims
1
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Crataegus X maligna
Nutrition
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claims
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Crataegus X rubrocarnea
Nutrition
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Crataegus bullatus
Nutrition
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Crataegus chrysocarpa
Nutrition
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Crataegus limnophila
Nutrition
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Crataegus monogyna
Nutrition
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Crataegus monogyna
Species
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Crataegus paludosa
Nutrition
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claims
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Crataegus x incaedua
Nutrition
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Complement C1 Inhibitor
Human genes
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description
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Complement C1 Inhibitor
Proteins
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description
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Human immunodeficiency virus
Species
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description
27
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Sepharose
Polymers
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description
7
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biological fluid
Substances
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description
7
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gel
Substances
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7
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experimental method
Methods
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206010061218
Inflammation
Diseases
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3
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Peptidases
Proteins
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3
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Peptidases
Human genes
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Viruses
Species
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complement system
Effects
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filtration
Methods
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inflammatory process
Effects
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inhibitor
Substances
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protease
Nutrition
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separation method
Methods
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description
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Complement C2
Human genes
0.000
description
2
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Complement C2
Proteins
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description
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Hereditary angioedema
Diseases
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description
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Tris buffer
Substances
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description
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amino acids
Chemical class
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description
2
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biosynthetic process
Effects
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description
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blood circulation
Effects
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description
2
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cell culture
Methods
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constituent
Substances
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infectious disease
Diseases
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mixture
Substances
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plasma concentration
Effects
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proteins and genes
Human genes
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proteins and genes
Proteins
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supernatant
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suspension
Substances
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virion
Anatomy
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Agarose
Polymers
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NOWKCMXCCJGMRR-UHFFFAOYSA-N
Aziridine
Chemical compound
C1CN1
NOWKCMXCCJGMRR-UHFFFAOYSA-N
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description
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102000004127
Cytokines
Human genes
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description
1
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Cytokines
Proteins
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description
1
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Dextran
Polymers
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description
1
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Esterase inhibitor
Drugs
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description
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Factor XII
Proteins
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description
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Factor XII
Human genes
0.000
description
1
108010080805
Factor XIa
Proteins
0.000
description
1
108060005987
Kallikrein
Proteins
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description
1
102000001399
Kallikrein
Human genes
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description
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206010033645
Pancreatitis
Diseases
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1
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RPMI medium
Substances
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Tissue Plasminogen Activator
Human genes
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description
1
108090000373
Tissue Plasminogen Activator
Proteins
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description
1
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activation
Effects
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acute effect
Effects
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1
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biological regulation
Effects
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description
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blood coagulation factor inhibitor
Substances
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bone marrow
Anatomy
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cellular effect
Effects
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chemical reaction
Methods
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chemical substances by application
Substances
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chemotherapy
Methods
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column chromatography
Methods
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complementary DNA
Substances
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1
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deficiency
Effects
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dilution
Methods
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dilution
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diseases, disorders, signs and symptoms
Diseases
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208000035475
disorder
Diseases
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1
230000000694
effects
Effects
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erythrocyte
Anatomy
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1
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esterase inhibitor
Substances
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filtrate
Substances
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harmful effect
Effects
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infectious effect
Effects
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infective effect
Effects
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inflammatory effect
Effects
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leukocyte
Anatomy
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mutation
Effects
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pathway
Effects
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plasmin
Drugs
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polyacrylamide
Polymers
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preparation method
Methods
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processed proteins & peptides
Human genes
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processed proteins & peptides
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reserpine
Chemical compound
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QEVHRUUCFGRFIF-MDEJGZGSSA-N
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reserpine
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serine protease inhibitor
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tissue plasminogen activator
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Classifications
C—CHEMISTRY; METALLURGY
C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
C12N7/00—Viruses; Bacteriophages; Compositions thereof; Preparation or purification thereof
C—CHEMISTRY; METALLURGY
C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
C12N7/00—Viruses; Bacteriophages; Compositions thereof; Preparation or purification thereof
C12N7/02—Recovery or purification
A—HUMAN NECESSITIES
A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
A61L2/00—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor
A61L2/0005—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor for pharmaceuticals, biologicals or living parts
A61L2/0011—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor for pharmaceuticals, biologicals or living parts using physical methods
A61L2/0017—Filtration
A—HUMAN NECESSITIES
A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
A61L2/00—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor
A61L2/0005—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor for pharmaceuticals, biologicals or living parts
A61L2/0082—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor for pharmaceuticals, biologicals or living parts using chemical substances
C—CHEMISTRY; METALLURGY
C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
C12N2740/00—Reverse transcribing RNA viruses
C12N2740/00011—Details
C12N2740/10011—Retroviridae
C12N2740/16011—Human Immunodeficiency Virus, HIV
C12N2740/16051—Methods of production or purification of viral material
Description
r/UU/U I 1 28/5/91 Regulation 3.2(2)
AUSTRALIA
Patents Act 1990
ORIGINAL
COMPLETE SPECIFICATION STANDARD PATENT Application Number: Lodged: Invention Title: PROCESS FOR SEPARATING HIV FROM A FLUID The following statement is a full description of this Invention, including the best method of performing it known to us CENTEON PHARMA GMBH 1998/Z006 Ma 1174 C16 Process for separating HIV from a fluid The invention relates to a process for separating human immunodeficiency virus or viruses (HIV) from a fluid, in particular from blood, blood plasma or blood serum. The process can be carried out both for the preparation of HIV-free blood donations and therapeutically for the reduction of the virus load in the blood by means of a blood lavage under the conditions of an extracorporeal blood circulation.
The invention is moreover directed at a filter which is suitable for the separation of HIV from a fluid.
It is known that the removal of HIV from all sorts of biological fluids, but S•especially from blood, blood plasma or blood serum, is an important prerequisite for its risk-free use for all sorts of medical purposes.
Numerous processes have therefore already been proposed using which removal of HIV from biological fluids should be achieved. Thus, in the “i international Patent Application WO97/07674, a process has been proposed using which HIV can be removed from biological fluids or inactivated by treating it with certain ethylenimine oligomers. It is important in this case that other constituents of the blood, in particular the cellular constituents, especially the erythrocytes, are not damaged by a treatment of this type and the removal of the HIV can be carried out in a simple manner and short period of time in order that sufficiently large amounts of purified blood can be obtained in an economically justifiable process.
It has now been found that these requirements can be fulfilled in an outstanding manner by a process if the C1 inhibitor is employed for the removal of the HIV from biological fluids.
2 The C1 inhibitor, also called C1 esterase inhibitor, is a protein which is present in the blood and is the main inhibitor of the classical pathway of the complement system and of the contact system. The C1 inhibitor can inhibit the activated form of factor XII and of kallikrein (Schapira M. et al., 1985, Complement 2: 111; DavisA.E., 1988, Ann Rev Immunol 6: 595; Sim R.B. et al., 1979, FEBS Lett 97: 111; De Agostini A. et al., 1984, J Clin Invest 73: 1542; Pixley R.A. et al., 1985, J Biol Chem 206: 1723; Schapira M. et al., 1982, J Clin Invest 69: 462; Van der Graaf F. et al., 1983 J Clin Invest 71: 149; Harpel P.C. et al., 1975, J Clin Invest 55: 593).
The C1 inhibitor thus regulates the activities of two plasma cascades, namely the complement system and the contact system, by which S” biologically active peptides are produced. The C1 inhibitor is therefore also an important regulator of the inflammatory system. Moreover, the C1 inhibitor inhibits activated factor XI (Meijers J.C.M. et al., 1988, Biochemistry 27: 959; Wuillemin W.A. et al., 1995, Blood 85: 1517). It follows from this that the C1 inhibitor can be considered as a coagulation inhibitor. The tissue plasminogen activator and plasmin are also inhibited to a certain extent by the C1 inhibitor, although that is not its main function (Harpel P.C. et al., 1975, J Clin Invest 55: 149; Booth N.A. et al., 1987 Blood 69: 1600).
The C1 inhibitor is obtained from plasma by purification to a considerable extent and utilized for clinical applications, in particular in the treatment of hereditary angioedema, a disorder which is caused by a genetically related deficiency of the C1 inhibitor. Moreover, it has already been described that good therapeutic results were achieved by administration of the C1 inhibitor in systemic inflammations [International Patent Application WO 92/22320 (Genentech in severe burns, pancreatitis, bone marrow transplants, cytokine therapy and during use in extracorporeal blood circulations [DE-A-4 227 762 (Behringwerke AG)].
I
3 The complete genomic and the cDNA which codes for the C1 inhibitor has already been cloned (Bock S.C. et al., 1986 Biochemistry 25: 4292; Carter P.E. et al., 1988, Eur J Biochem 173: 163). Various variants of the recombinant C1 inhibitor with amino acid mutations in the P1 and the P3 and/or P5 positions of the reactive center and variants which were isolated from patients with a hereditary angioedema have already been prepared recombinantly (Eldering E. et al., 1988, J Biol Chem 263: 11776; Eldering E. et al., 1993, J Biol Chem 267: 7013; Eldering E. et al., 1993, J Clin Invest 91: 1035; US-Patent 5,622,930; Davis A.E. et al., 1992, Nature Genetics 1: 354; Eldering E. et al., 1995, J Biol Chem 270: 2579; Verpy et al., 1995, J Clin Invest 95: 350).
The C1 inhibitor belongs to the large family of serine proteinase inhibitors which are also called serpines (Travis J. et al., 1983, Ann Rev Biochem 52: 655; Carrel R.W. et al., 1985, Trends Bioch Sci 10: 20). On SDSpolyacrylamide gels, the C1 inhibitor exhibits a molecular weight of approximately 105 kD. Its plasma concentration is approximately 270 mg/I ~(Schapira M. et al., 1985, Complement 2: 111; Nuijens J.H. et al., 1989, J Clin Invest 84: 443). The C1 inhibitor is a protein whose plasma level can increase up to twofold in uncomplicated infections and other inflammations (Kalter E.S. et al., 1985, J Infect Dis 151: 1019). The increased formation of the C1 inhibitor in inflammations probably serves for the protection of the body against the harmful effects of the intravascular activation of the complement system and of the contact system during the acute reactions.
The serpines react as inhibitors by formation of bimolecular complexes with the proteinase to be inhibited. In these complexes, the active center of the proteinase is bound by the active center of the serpine and thus inactive (Travis J. et al., 1983, Ann Rev Biochem 52: 655). The serpines react specifically with certain proteinases, this specificity being determined by the amino acid sequence of the reactive center.
I
4 The abovementioned varied actions of the C1 inhibitor did not, however, give any indication of its strong affinity for HIV and in particular did not suggest that separation of HIV from biological fluids such as blood, blood plasma or blood serum is possible with the aid of the C1 inhibitor. It was therefore a very unexpected finding that HIV binds to the C1 inhibitor and can thereby be separated from mixtures which contain HIV with the aid of the processes below.
The invention relates to a process for separating HIV from a fluid such as blood, blood plasma or blood serum, in which the HIV is bound to a C1 S• esterase inhibitor immobilized on a support material. This process is expediently carried out such that the C1 esterase inhibitor is bonded to an inert matrix which can be employed in affinity chromatography, by means of which the biological fluid to be freed of the HIV is added in a procedure customary in column chromatography.
Suitable matrices on which the C1 inhibitor is immobilized include dextrans, polyacrylamides and agarose, but other supports customarily employed in affinity chromatography can also be used for the process •–according to the invention. As a result, HIV-free blood donations can be obtained. However, the virus load in the blood can also be therapeutically reduced if HIV is absorbed on a matrix impregnated with a C1 inhibitor by means of an extracorporeal blood lavage before or during chemotherapy.
A particularly effective and rapid separation of the HIV can be achieved according to the invention if the fluid containing the HIV is filtered through a fiber material which is impregnated with the C1 esterase inhibitor. For this, a filter has proven suitable which consists of a container in which is packed a fiber material which is impregnated with the C1 esterase inhibitor. The fiber material can either consist of fibers which are interwoven or entangled with one another or can be present in the form of a woven or web-like material. A particularly effective and rapid filtration can in this case be 5 achieved using a filter which consists of fibers impregnated with the C1 esterase inhibitor which have an average diameter of less than 10 mm, preferably of 0.3 to 3 mm, and a bulk density of 0.15 to 0.5 g/cm 3 and an average fiber spacing of 0.5 to 0.7 mm.
Filters of this type are disclosed in European Patent Specification 0 155 003 and have proven so outstandingly suitable for filtering leukocytes from blood that they have largely been accepted in practice.
However, no impregnated fibers and only fibers not actually impregnated with the C1 inhibitor are mentioned there. If, however, fibers impregnated C1 inhibitor are employed in a filter system of this type, the affinity of this inhibitor for HIV can be combined with the advantages of rapid and effective filtration such that a biological fluid free of HIV can be obtained as a filtrate in a very simple manner.
O.
The advantages of the process according to the invention are emphasized by the following example: 6 9*
U.
U. Example The following starting materials were employed: HIV from cell cultures in RPMI medium (titer approximately 104 CCID 5 o) C1 inhibitor-Sepharose: 5 mg of Ag/ml of Sepharose in 2 M NaCI, 20 mM tris pH 7.2 AT Ill-Sepharose: 11.1 mg of Ag/ml of Sepharose in 2 M NaCI, 20 mM tris pH 7.2 Experimental procedure: HIV was pipetted 1:5 into the gel suspension (5ml to 20ml of gel suspension), the mixture was incubated at 22 0 C for 30 min, the gel was centrifuged off at a low speed of rotation and the supernatant was titrated.
The control employed was AT Ill-coupled Sepharose.
The following results were obtained: Sample: C1 inhibitor- AT III- HIV Sepharose Sepharose dilution CCIDo CCIDso* CCID0o’ CCIDso (determined) (theoreti- (determined) (theoretical) cal) 1:1000 <1.8 3.3 2.9 3.3
*CCID
5 olog 10 (cell culture infective dose 7 The experiment shows that HIV binds to C1-INH; the control experiment with AT Ill-coupled gel shows that the binding takes place specifically to C1-INH and not nonspecifically to gel.
The experiment was carried out using approximately 50,000 infectious virions of HIV in the experimental batch; at least approximately 48,000 virions were removed from the supernatant by 100 mg of gel-bound C1 inhibitor.
"Comprises/comprising" when used in this specification is taken to specify the presence of stated features, integers, steps or components but does not preclude the presence or addition of one or :.more other features, integers, steps, components or groups thereof.
*o 9 *47
S
Claims (7)
1. A process for separating HIV from a fluid, which comprises binding the HIV to a C1 esterase inhibitor immobilized on a support material.
2. The process as claimed in claim 1, wherein the fluid employed is blood, blood plasma or blood serum.
3. The process as claimed in claims 1 and 2, wherein the support material used is an inert matrix which can be employed in affinity chromatography.
4. The process as claimed in claims 1 to 3, wherein the HIV-containing fluid is filtered through a fiber material which is impregnated with the C1 esterase inhibitor. eg.:
5. A filter for separating HIV from a fluid, which consists of a container in which is packed a fiber material which is impregnated with the C1 esterase inhibitor. C
6. The filter as claimed in claim 5, wherein the fiber material consists of fibers which are interwoven or entangled with one another or is O. present in the form of a woven or web-like material.
7. The filter as claimed in claims 5 and 6, wherein the fibers impregnated with the C1 esterase inhibitor have an average diameter of less than 10 mm, preferably of 0.3 to 3 mm, a bulk density of 0.15 to 0.5 g/cm 3 and an average fiber spacing of 0.5 to 0.7 mm. DATED this 21st day of June 1999. CENTEON PHARMA GMBH WATERMARK PATENT TRADEMARK ATTORNEYS 290 BURWOOD ROAD HAWTHORN. VIC. 3122
AU35781/99A
1998-06-22
1999-06-21
Process for separating HIV from a fluid
Ceased
AU745851B2
(en)
Applications Claiming Priority (2)
Application Number
Priority Date
Filing Date
Title
DE19827750
1998-06-22
DE19827750A
DE19827750C1
(en)
1998-06-22
1998-06-22
Separating human immunodeficiency virus from fluid, useful for lowering HIV virus load in extracorporeal blood
Publications (2)
Publication Number
Publication Date
AU3578199A
true
AU3578199A
(en)
2000-01-06
AU745851B2
AU745851B2
(en)
2002-04-11
Family
ID=7871638
Family Applications (1)
Application Number
Title
Priority Date
Filing Date
AU35781/99A
Ceased
AU745851B2
(en)
1998-06-22
1999-06-21
Process for separating HIV from a fluid
Country Status (7)
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WO2001041766A1
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1999-12-06
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H. Lundbeck A/S
The combination of a serotonin reuptake inhibitor and irindalone
US20040259076A1
(en)
*
2003-06-23
2004-12-23
Accella Scientific, Inc.
Nano and micro-technology virus detection method and device
AU2004264673A1
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*
2003-08-19
2005-02-24
Csl Behring Gmbh
C1-INH as a drug for treating viruses pathogenic to humans
US20060233776A1
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*
2003-08-19
2006-10-19
Norbert Heimburger
C1-inh as a drug for treating viruses pathogenic to humans
CN105536006A
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2015-12-31
2016-05-04
山东中保康医疗器具有限公司
Filtration frame special for virus inactivation
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US5622930A
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1989-10-27
1997-04-22
Clb
C1 inhibitor muteins and uses thereof
WO1992022320A1
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1991-06-14
1992-12-23
Genentech, Inc.
C1 inhibitor variants and treating inflammatory response with c1 inhibitor
DE4227762A1
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1992-08-24
1994-03-03
Behringwerke Ag
Use of a kallikrein inhibitor for the manufacture of a medicament for the prophylaxis and therapy of certain diseases
EP0679405A1
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*
1994-04-25
1995-11-02
Rotkreuzstiftung Zentrallaboratorium Blutspendedienst Srk
Method for separating viruses from protein solutions
JP3615785B2
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*
1994-04-28
2005-02-02
テルモ株式会社
HIV and related material removal materials
US5643770A
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*
1994-07-21
1997-07-01
Alexion Pharmaceuticals, Inc.
Retroviral vector particles expressing complement inhibitor activity
US6114108A
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*
1995-08-29
2000-09-05
V.I. Technologies, Inc.
Methods and compositions for the selective modification of viral nucleic acids
1998
1998-06-22
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DE19827750A
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1999-06-15
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2000-06-15
TC
Change of applicant's name (sec. 104)
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AVENTIS BEHRING GMBH
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FORMER NAME: CENTEON PHARMA GMBH
2002-08-08
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Letters patent sealed or granted (standard patent)
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