IE63831B1 - Medication for the treatment or prevention of HIV virus infection through passive immunization and processes for its preparation - Google Patents
Medication for the treatment or prevention of HIV virus infection through passive immunization and processes for its preparationInfo
- Publication number
- IE63831B1 IE63831B1 IE400589A IE400589A IE63831B1 IE 63831 B1 IE63831 B1 IE 63831B1 IE 400589 A IE400589 A IE 400589A IE 400589 A IE400589 A IE 400589A IE 63831 B1 IE63831 B1 IE 63831B1
- Authority
- IE
- Ireland
- Prior art keywords
- hiv
- preparation
- antibodies
- virus
- envelope
- Prior art date
Links
- 241000725303 Human immunodeficiency virus Species 0.000 title claims abstract description 31
- 238000000034 method Methods 0.000 title claims abstract description 24
- 238000002360 preparation method Methods 0.000 title claims abstract description 23
- 229940079593 drug Drugs 0.000 title claims abstract description 13
- 239000003814 drug Substances 0.000 title claims abstract description 13
- 230000002265 prevention Effects 0.000 title abstract description 6
- 230000003053 immunization Effects 0.000 title abstract description 5
- 238000002649 immunization Methods 0.000 title abstract description 4
- 230000009385 viral infection Effects 0.000 title description 8
- 230000036436 anti-hiv Effects 0.000 claims abstract description 16
- 108010074605 gamma-Globulins Proteins 0.000 claims abstract description 12
- 108010003533 Viral Envelope Proteins Proteins 0.000 claims abstract description 5
- 108090000288 Glycoproteins Proteins 0.000 claims abstract description 4
- 102000003886 Glycoproteins Human genes 0.000 claims abstract description 4
- 102000004169 proteins and genes Human genes 0.000 claims description 17
- 108090000623 proteins and genes Proteins 0.000 claims description 17
- 108060003951 Immunoglobulin Proteins 0.000 claims description 13
- 102000018358 immunoglobulin Human genes 0.000 claims description 13
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 claims description 12
- 210000002826 placenta Anatomy 0.000 claims description 12
- 210000002381 plasma Anatomy 0.000 claims description 9
- 229940072221 immunoglobulins Drugs 0.000 claims description 8
- 238000000926 separation method Methods 0.000 claims description 7
- 239000000427 antigen Substances 0.000 claims description 6
- 102000036639 antigens Human genes 0.000 claims description 6
- 108091007433 antigens Proteins 0.000 claims description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 4
- 101710091045 Envelope protein Proteins 0.000 claims description 3
- 101710188315 Protein X Proteins 0.000 claims description 3
- 230000000521 hyperimmunizing effect Effects 0.000 claims description 3
- 230000006798 recombination Effects 0.000 claims description 3
- 238000002255 vaccination Methods 0.000 claims description 3
- 238000004587 chromatography analysis Methods 0.000 claims description 2
- 238000002955 isolation Methods 0.000 claims description 2
- 108010041397 CD4 Antigens Proteins 0.000 claims 1
- 102100027723 Endogenous retrovirus group K member 6 Rec protein Human genes 0.000 claims 1
- 239000007787 solid Substances 0.000 claims 1
- 208000031886 HIV Infections Diseases 0.000 abstract description 3
- 208000037357 HIV infectious disease Diseases 0.000 abstract description 3
- 208000033519 human immunodeficiency virus infectious disease Diseases 0.000 abstract description 3
- 239000000706 filtrate Substances 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 208000030507 AIDS Diseases 0.000 description 5
- 102100034349 Integrase Human genes 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 241000700605 Viruses Species 0.000 description 4
- 230000002779 inactivation Effects 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 230000003612 virological effect Effects 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 3
- 239000011543 agarose gel Substances 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 210000004366 CD4-positive T-lymphocyte Anatomy 0.000 description 2
- 102000006395 Globulins Human genes 0.000 description 2
- 108010044091 Globulins Proteins 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 102100022563 Tubulin polymerization-promoting protein Human genes 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 230000001143 conditioned effect Effects 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 1
- 102100027211 Albumin Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 101710205625 Capsid protein p24 Proteins 0.000 description 1
- 206010057248 Cell death Diseases 0.000 description 1
- 101710121417 Envelope glycoprotein Proteins 0.000 description 1
- 101710142246 External core antigen Proteins 0.000 description 1
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 1
- 241000713772 Human immunodeficiency virus 1 Species 0.000 description 1
- 241000713340 Human immunodeficiency virus 2 Species 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 101710177166 Phosphoprotein Proteins 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 101710149279 Small delta antigen Proteins 0.000 description 1
- 108010067390 Viral Proteins Proteins 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 235000013905 glycine and its sodium salt Nutrition 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 210000004779 membrane envelope Anatomy 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 238000011146 sterile filtration Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
- C07K16/1063—Lentiviridae, e.g. HIV, FIV, SIV env, e.g. gp41, gp110/120, gp160, V3, PND, CD4 binding site
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Virology (AREA)
- Immunology (AREA)
- Oncology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Public Health (AREA)
- Biophysics (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Veterinary Medicine (AREA)
- Communicable Diseases (AREA)
- AIDS & HIV (AREA)
- Hematology (AREA)
- Biochemistry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Peptides Or Proteins (AREA)
- Medicinal Preparation (AREA)
Abstract
Drug for the treatment or prevention by passive immunization of the HIV-infection and processes for preparation thereof. According to the invention, the drug consists of, or comprises, a preparation of anti-HIV gammaglobulins Ig6 and/or IgM of human origin without antibodies directed against glycoproteins of the HIV virus envelope and/or anti-CD4 antibodies.
Description
MEDICATION POR THE TREATMENT OR PREVENTION OF HIV VIRUS INFECTION THROUGH PASSIVE IMMUNIZATION AND PROCESSES FOR ITS PREPARATION.
The present invention relates to medication for the treatment or prevention of HIV virus infection, through passive immunization.
The use of specific anti-HIV gammaglobulins of human 10 origin obtained from seropositive donors for the treatment of seroprophylaxis and HIV (human immunodeficiency virus) virus infection has been contemplated previously. See Immunoglobulin preparation for HIV-infected patients P.L. YAP and P.E. WILLIAMS - Vos Sanguinis 55i 65-74 (1988).
In this manner, PCT patent application wo 89/01339 describee Immunoglobulins obtained from healthy seropositive donors and presenting an important p24 antibody titer.
However, these gammaglobulins contain a wide variety of different anti-HIV antibodies, amongst v»hich are antibodies to proteins of the viral wall (in the case of HIVi ι glycoproteins gpl20 and gp Furthermore, seropositive donors could also hold antibodies to the marker protein o£ the T4 lyraphocytcc (CD4 protein) as a result of an auto-iramunization triggered by the interaction of viral protein gpi20 with protein CD4 which constitutes the natural receptor of protein gpl20 in the T4 lymphocytes.
Thus, antibodies to the proteins of the viral envelope are suspected to facilitate instead of protect against viral infection, apparently because they would form an immune complex with the virus and provoke its phagocytosis by macrophages, thus leading to an infection of the macrophages which would consitute a reservoir for the HIV virus.
Furthermore, antibodies to the CD4 protein are also suspected to have a harmful effect during the HXV infection by triggering cytolysis of T4 lymphocytes, thereby contributing to the development of the acquired immunodeficiency syndrome (AIDS), clinical manifestation of the HIV virus infection.
Also, it has been observed that the outbreak of clinical signs or aius on a previously asymptomatic . 25 Beropositive patient is accompanied by a collapse in antip24 and anti-RT antibodies whereas the titer of neutralizing antibodies in vitro is not modified. Seet Prospects for the control of AIDS by immunizing seropositive individual: J. SALK, Nature 327« 473-76, June 11, 1987).
Other details on the HIV virus infection processes are described in« Replication of the human immunodeficiency virus - Strategies for inhibition. B.M. PETERLIN and P.A. LUCIW, Biotechnology 6i 794-799, July 1988).
The present invention intends to provide medication for the treatment or the prevention of the HIV virus infection through the use of hyperimmune anti-HIV human iramunoglobilins.
The present invention therefore relates to medication constituted by or comprising a preparation of hyperimmune anti-HIV IgG and/or IgM gammaglobulins of human origin.
The preparation is devoid of antibodies to glycoproteins of the HIV virus envelope and/or anti CD4 antibodies.
The medication of the present invention is advantageously conditioned to be administered parenterally, particularly through intramuscular cr Intravenous injection, in the same fashion as the usual immunoglobulin preparations.
IS The present invention also relates to processes for the preparation o£ the above-mentioned medication.
According to one embodiment of the processes of the present invention, plasma from blood or placentas of HIV virus seropositive donors or mothers is collected. From this material, there is obtained, through known isolation or separation processes, a total IgG and/or IgH immunoglobulin preparation, and this preparation is treated to eliminate anti-HIV envelope and/or anti CD4 antibodies.
In another embodiment of the processes of the present invention, one or more antibodies to the HIV virus but not to the envelope glycoproteins and/or CD4 are selectively extracted from plasma blood or placentas, Partlculsrly, on»* or more anti-core, snti-pJi, antip55, anti-plS, anti reverse transcriptase or anti nef antibodies may be extracted.
The extraction may, for example, be carried out by immobilizing on a support (agarose gel, for example) one or more natural HIV antigens, or antigens bearing the desired epitope, obtained through chemical synthesis or expression in a suitable recombinant system.
One of the advantages conferred by the selective extraction of the desired antibody from the collected Immunoglobulins is that higher concentration and standardization of both the titer and the extracted the collected immunoglobulin composition from 10 immunoglobulins are obtained. One may eventually mix the selectively extracted immunoglobulins and obtain standardized antibody titers.
When the anti-envelope and/or anti-CD4 antibodies are 15 selectively removed from the collected immunoglobulins, it ie preferable to repeat the removal steps several times through extraction, in order to obtain an anti-envelope and/or anti-CD4 antibody titer that is practically nonexistent .
If viral HIV particles are present in the material, the process of the present Invention also comprises a further step through which the virus is removed or inactivated .
The seropositive donors or mothers may either- b* Infected by the HIV virus or may have been veccined with inactivated total HIV virus or HIV virus from a nonlnfectlous strain.
For example, plasma, blood or placenta of HIV1 seropositive donors or mothers may be chosen but the process of the present invention may also be carried out using HIVI or a mixture of materials related co hivi and HIV2.
Total IgG and/or IgM may be obtained through different known processes. For example, they may be obtained through COHN's alcohol separation process for plasma or through TAYLOR's alcohol separation process for placenta, or through chromatography. These separation methods are well known to those skilled in the art.
When the material has been obtained from a seropositive donor infected by the wild type virus, the specific anti-HIV viral inactivation treatment may, for example, be obtained through a beta-proplolactone treatment, through exposure to heat or through an organic solvent in the presence of a detergent. These inactivation procesees, which are well known to those skilled in the art, are thoroughly described in processes for the preparation of immunoglobulins originating from plasma or placenta ( See ; Inactivation of the human immunodeficiency viruses (HIV-i and JiIV-2, 'during the manufacturing of placenta) albumin and garamaglobuline. M. GRANDGEORGE and F. PELLOCUIN, Tranefusion 29« 629-634, 1989 ) .
The removal of the anti-Hiv env._ope or anti CD4 antibodies may advantageously be carried out through bath or column immunoadsorption by contacting the immunoglobulin preparation with an Insoluble support on which envelope proteins gp!20 and/or gp4i and/or their precursor gpl60 (so far as Hivi is concerned) and/or protein CD4 have been previously immobilized through any method known to those skilled in the art. The proteins may, for example, be immobilized on an agarose support activated with cyanogen bromide. These proteins may be obtained either from natural sources (HIV and lymphocytes, or by genetic recombination.
According to another embodiment, plasma, blood or placenta of HIV seropositive donors or mothers resulting from vaccination with isolated HlV-virue proteins or obtained by genetic recombination, with the exception Oi the envelope proteins of the virus, may be utilized. In - 8 this process, the steps through which anti-envelope and/or anti CD4 antibodies are eliminated are omitted.
The preparation obtained through one of the processes referred to above is conditioned to be administered intramuscularly or intravenously through classical stabilization, additional purification, sterile filtration and eventually lyophilization steps. io The medication of the present invention may be used in the following applications: - preventing HIV infection for persons susceptible ot contracting the disease through seroprophylaxis, - adjuvant or complementary treatment o£ an anti-HIV vaccination, - treatment of the HIV infection and prevention of its clinical manifestation, AIDS, - treatment of AIDS.
Example 1.
Preparation of anti-HIV gammaglobulins concentrated in anti-.core antibodies and .devoid of_anti-enyo.lope antibodies.
The starting material is a preparation of human placenta gammaglobulins, rich in HIV antibodies, obtained from a pool of HIV seropositive women placenta, purified through an alcohol technique oompleted by a viral inactivation heating step. This gammaglobulin is adjusted at a protein concentration of 50g/litre, in a phosphate. NaCl pH 7.4 buffer. The solution is titrated in ELISA (Envacor Abbott HIV test). The solution contains a titer of« 1/700 in anti-core antibodies 1/30 in anti-envelope antibodies.
The titer is attributed by the last positive dilution in the ELISA test. - 80 ml of this solution are filtrated on a column containing 3 mg of p25 antigen immobilized on 1 ml of agarose gel.
- The resulting filtrate contains essentially all the desired gammaglobulins? adjusted at 50 g/1 in protein, the filtrate titersi 1/30 in anti-core antibodies 1/30 in anti-envelope antibodies The column is then eluted with a glycocoll acid buffer.
This elutant contains 13 mg of protein, its titer being brough back to a So g/1 protein concentration of: 1/120.000 in anti-core antibodies negative in anti-envelope antibodien This «yampjf* Illustrates the possibility of preparin an anti-HIV globulin rich in anti-core antibody an lacking anti-envelope antibodies.
Example 2 Preparation of an anti-HIV gammaglobulin lacking anti envelope antibodies.
The starting material used m identical to that used in example 1. adjusted at a protein concentration phosphate. NaCl pH 7.4 buffer. this example 1 The globulin is of 50 g/1 in a The solution is titrated in ELISA (Envacor Abott HIV test).
The solution has a titer of 1/700 in anti-core antibodies of 1/30 in anti-envelope antibodies. ml of this solution are filtrated on a column containing 4 mg of gpi60 antigen immobilized on l ml of agarose gel.
The filtrate collected contains essentially oil the proteins. Its titer, adjusted to 50 g/1 in protein, is the following! 1/500 in anti-core antibodies 1/8 in anti-envelope antibodies· A second run of the filtrate on the previously regenerated column support allows the obtention of a second filtrate which, when adjusted to 50 g/1, has the following tlteri 1/500 in anti-core antibodies 1/3 in anti-envelope antibodies.
After having carried out a third filtration on the same support, using conditions similar to those set forth above, the third filtrate obtained and adjusted at a protein concentration of 50 g/1 still contains most of the proteins and shows the following titer» 1/500 in anti-core anbibodies negative in anti-envelope antibodies.
This preparation illustrates the possibility of preparing an anti-HIV gammaglobulin containing particularly anti-core antibodies but lacking antienvelope antibodies.
Claims (9)
1. Medication constituted by or comprising' hyperimmune anti-HIV IgG and/or IgH gammaglobulins of human origin devoid of antibodies to glycoproteins of the HIV virus envelope and/or anti CD4 antibodies.
2. Process for the preparation of a medication according to claim 1 caractarised by the isolation or separation of a preparation of total IgG and/or IgM immunoglobulins from plasma, blood or placenta of Hlv-virus seropositive donors or mothers, said preparation being treated to eliminate anti-HIV envelope and/or anti CD4 antibodies.
3. Process according to claim 2, comprising a further step whereby said HIV-virus is removed or inactivated.
4. Process according to claims 2 and 3, wherein said total immunoglobulins are prepared by a process selected from COHN's alcohol separation for plasma, TAYLOR separation for placenta and chromatography.
5. Process according to claims 2 to 4, wherein said anti-HIV envelope and/or anti CD
6. Process for the preparation of medication according to claim 1, caracterised by the preparation of total IgG and/or IgM gammaglobulins from plasma, blood, or placenta of HIV seropositive donors or mothers following a vaccination with proteins isolated from the HIV-virus or obtained through genetic recombination, excluding the virus envelope proteins.
7. Process according to claim 5, wherein immuneadsorption is carried out on an insoluble support on which envelope proteins, particularly gp 120 and/or gp 160 and/or the CD4 protein have been immobilized.
8. Process according to one of claims 2 to 6, comprising a selective immunoadsorption on an insoluble support on which at least one HIV antigen, excluding the antienvelope and/or CD4 antigen, has been immobilized on a solid support.
9. Process according to claim 8, wherein the HIV antigen is p24,25.
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FR8816580A FR2640511B1 (en) | 1988-12-15 | 1988-12-15 | MEDICINES FOR THE TREATMENT OR PREVENTION BY PASSIVE IMMUNIZATION OF HIV VIRUS INFECTION AND METHOD OF PREPARATION |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| IE894005L IE894005L (en) | 1990-06-15 |
| IE63831B1 true IE63831B1 (en) | 1995-06-14 |
Family
ID=9373004
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IE400589A IE63831B1 (en) | 1988-12-15 | 1989-12-14 | Medication for the treatment or prevention of HIV virus infection through passive immunization and processes for its preparation |
Country Status (13)
| Country | Link |
|---|---|
| EP (1) | EP0374053B1 (en) |
| JP (1) | JPH03505738A (en) |
| CN (1) | CN1045035A (en) |
| AT (1) | ATE102836T1 (en) |
| AU (1) | AU627540B2 (en) |
| CA (1) | CA2005365C (en) |
| DE (1) | DE68913932T2 (en) |
| DK (1) | DK192990D0 (en) |
| ES (1) | ES2062079T3 (en) |
| FR (1) | FR2640511B1 (en) |
| IE (1) | IE63831B1 (en) |
| WO (1) | WO1990006773A1 (en) |
| ZA (1) | ZA899533B (en) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ATE244888T1 (en) * | 1993-02-05 | 2003-07-15 | Epigen Inc | HUMAN CARCINOMA ANTIGEN (HCA), HCA ANTIBODIES, HCA IMMUNOASSAYS, RECORDING METHODS AND THERAPY |
| CN106110422B (en) * | 2016-07-01 | 2019-02-01 | 翁炳焕 | AIDS immunization therapy absorber |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3604947A1 (en) * | 1986-02-17 | 1987-08-20 | Biotest Pharma Gmbh | METHOD FOR PRODUCING AN IMMUNALLOBULIN-CONTAINING PREPARATE AND THE USE THEREOF FOR PROPHYLAXIS AND THERAPY OF AIDS |
| US4863730A (en) * | 1986-03-21 | 1989-09-05 | Cenfold Holdings, S.A. | Immunotherapy for AIDS patients |
| DE379516T1 (en) * | 1987-08-11 | 1991-01-17 | Abbott Laboratories, Abbott Park, Ill. | HYPERIMMUN GLOBULIN AGAINST HIV. |
-
1988
- 1988-12-15 FR FR8816580A patent/FR2640511B1/en not_active Expired - Fee Related
-
1989
- 1989-12-13 CA CA002005365A patent/CA2005365C/en not_active Expired - Fee Related
- 1989-12-13 ZA ZA899533A patent/ZA899533B/en unknown
- 1989-12-14 IE IE400589A patent/IE63831B1/en not_active IP Right Cessation
- 1989-12-15 DE DE68913932T patent/DE68913932T2/en not_active Expired - Fee Related
- 1989-12-15 JP JP2501084A patent/JPH03505738A/en active Pending
- 1989-12-15 WO PCT/FR1989/000656 patent/WO1990006773A1/en unknown
- 1989-12-15 AU AU48062/90A patent/AU627540B2/en not_active Ceased
- 1989-12-15 EP EP89403495A patent/EP0374053B1/en not_active Expired - Lifetime
- 1989-12-15 ES ES89403495T patent/ES2062079T3/en not_active Expired - Lifetime
- 1989-12-15 AT AT89403495T patent/ATE102836T1/en not_active IP Right Cessation
- 1989-12-15 CN CN89109300A patent/CN1045035A/en active Pending
-
1990
- 1990-08-14 DK DK192990A patent/DK192990D0/en not_active Application Discontinuation
Also Published As
| Publication number | Publication date |
|---|---|
| CN1045035A (en) | 1990-09-05 |
| EP0374053B1 (en) | 1994-03-16 |
| ES2062079T3 (en) | 1994-12-16 |
| CA2005365A1 (en) | 1990-06-15 |
| CA2005365C (en) | 1995-12-12 |
| IE894005L (en) | 1990-06-15 |
| AU4806290A (en) | 1990-07-10 |
| AU627540B2 (en) | 1992-08-27 |
| FR2640511B1 (en) | 1993-04-23 |
| DK192990A (en) | 1990-08-14 |
| JPH03505738A (en) | 1991-12-12 |
| DK192990D0 (en) | 1990-08-14 |
| WO1990006773A1 (en) | 1990-06-28 |
| ATE102836T1 (en) | 1994-04-15 |
| DE68913932T2 (en) | 1994-07-07 |
| ZA899533B (en) | 1990-12-28 |
| FR2640511A1 (en) | 1990-06-22 |
| DE68913932D1 (en) | 1994-04-21 |
| EP0374053A1 (en) | 1990-06-20 |
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