EP2004229A2 - Konzentrat von immunglobulinen und f(ab)'2 und/oder fab fragmenten, die spezifisch für einen arbovirus sind; als medikament - Google Patents

Konzentrat von immunglobulinen und f(ab)'2 und/oder fab fragmenten, die spezifisch für einen arbovirus sind; als medikament

Info

Publication number
EP2004229A2
EP2004229A2 EP07731238A EP07731238A EP2004229A2 EP 2004229 A2 EP2004229 A2 EP 2004229A2 EP 07731238 A EP07731238 A EP 07731238A EP 07731238 A EP07731238 A EP 07731238A EP 2004229 A2 EP2004229 A2 EP 2004229A2
Authority
EP
European Patent Office
Prior art keywords
concentrate
immunoglobulins
fab
virus
igg
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.)
Withdrawn
Application number
EP07731238A
Other languages
English (en)
French (fr)
Inventor
Roland Schmitthaeusler
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.)
LFB SA
Original Assignee
LFB SA
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.)
Filing date
Publication date
Application filed by LFB SA filed Critical LFB SA
Publication of EP2004229A2 publication Critical patent/EP2004229A2/de
Withdrawn legal-status Critical Current

Links

Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
    • 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
    • C07K16/1081—Togaviridae, e.g. flavivirus, rubella virus, hog cholera virus
    • 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
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
    • A61P31/12—Antivirals
    • A61P31/14—Antivirals for RNA viruses
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
    • C07K2317/54—F(ab')2
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
    • C07K2317/55—Fab or Fab'
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
    • Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
    • Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change

Definitions

  • the invention relates to a novel medicament for the treatment of • arboviruses, namely a concentrate of immunoglobulins and F (ab) '2 and / or Fab fragments specific for said arbovirus and its method of preparation.
  • arboviruses are defined by WHO as viruses that persist in nature mainly or largely through biological transmission between susceptible vertebrate hosts, by blood-sucking arthropods; they multiply and cause viremia in the vertebrate, proliferate in the tissues of the arthropod and are transmitted to a new vertebrate by arthropod p 'iqueur after extrinsic incubation period.
  • Virus transmission from a viremic host to a female adult mosquito occurs through the blood sucked in during the bite.
  • the virus multiplies in the mosquito, it crosses the stomach border of the animal and is found in its salivary glands. Contamination of a healthy man is achieved by the anti-coagulant mosquito saliva released just before the sting into a blood vessel.
  • the window during which a person is a viremic host before becoming ill is only a few days old.
  • the known arboviruses belong to five families of viruses: - Togaviri & ae, genus Alphavirus, 28 viruses, including Chikungunya, O'Nyong Nyong, Ross River, Sindbis, Maya.ro viruses
  • Flaviviridae genus Flavivirus
  • 68 viruses including yellow fever virus, dengue fever, Japanese encephalitis, West-NiIe virus, temperate Eurasian tick-borne encephalitis viruses, Kyasianur forest and Omsk haemorrhagic fever - Bunyaviridae, genus Bunyavirus (138 viruses, including Bunyamwera virus), genus Phleboviris
  • Nairovirus genus 24 viruses, including Crimean-Congo hemorrhagic fever virus
  • 41 viruses not classified Reoviridae genus Orbivirus (69 viruses) and genus Coltivirus (2 viruses) + 6 viruses not classified Rhabdoviridae, genus Vesiculoviris (18 viruses) and genus Lyssavirus (16 viruses) + 36 unclassified viruses.
  • Dengue fever is widespread in all tropical and subtropical areas of the world and is the first public health problem posed by arbovirosis. There are four viral serotypes called "Dengue 1, 2, 3, 4", not resulting in cross-protection. Clinically, there are several forms of dengue fever: asymptomatic dengue fever, classical dengue fever (CD) and severe forms including hemorrhagic fever, dengue haemorrhagic fever (DH) and dengue fever with shock syndrome (DSC), which can lead to death, especially in the child. The 4 types of dengue virus can be involved in both DC and DH. The physiopathological mechanisms involved in the genesis of DH are unknown.
  • the theory most often used is based on phenomenon of "immunological facilitation": a subject having been infected by one of the four serotypes not being protected against the other three, a second infection, heterologous, could result in a DH.
  • the vectors are mosquitoes of the genus Aedes: Aedes aegypti is the major vector, Aedes albopictus plays an important role in rural and peri-urban areas and tolerates well temperate climates.
  • the West NiIe virus is now considered to be the most widespread flavivirus after the dengue virus; it affects the man sporadically or epidemic. He has recently distinguished himself by emerging for the first time on the American continent, during an epidemic that occurred in New York ' in 1999 (62 cases including 7 deaths). It then spread widely in the United States, affecting more than 9000 people in 44 states in 2003, including 2866 cases of encephalitis and 264 deaths. The virus had previously been found in various parts of the globe, in Africa, the Middle East, India, and Europe. Mosquitoes are the main vectors of the West NiIe virus, mainly those of the genus Culex. The main hosts of the virus are birds, whether wild or domestic (ducks, pigeons ).
  • the West NiIe virus infects humans primarily through the bite of a vector mosquito.
  • the infection is characterized by the sudden onset of severe fever after 3 to 6 days of incubation. This fever is accompanied by headache, backache, muscle aches, coughing, swollen neck glands, and often rash, nausea, abdominal pain, diarrhea and symptoms. breathing. In less than 15% of cases, complications occur: meningitis, encephalitis, and rarely hepatitis, pancreatitis or myocarditis.
  • the patient recover spontaneously, sometimes with sequelae. But the disease can be fatal in old people, and sometimes in young children.
  • Yellow fever (FJ) remains a daunting endemic and a constant threat in Black Africa and intertropical America. It is due to the yellow fever virus. It comes as a hepatonephritis hemorrhagic, yellow fever typhus, beginning with a phase or red phase, remission on day 3, a status phase or stage with yellow jaundice, vomiting, bleeding mainly digestive syndrome renal. Epidemiology is complex because, in natural environments, yellow fever virus is constantly circulating in monkey populations, thanks to simiophilic wild mosquitoes acting as vectors. It is only accidentally, when man comes into contact with such a sylvatic cycle, that the first human cases occur.
  • Chikungunya (abbreviated 'CHIK') is transmitted by mosquitoes of the genus Aedes.
  • the name is of Bantu origin and signifies: curling, cowering, or curved man's disease because it causes very severe joint pain associated with stiffness, giving the infected patients a very characteristic curved attitude.
  • mosquito species several of them are likely to transmit chikungunya, but only Aedes aegypti and Aedes albopictus have so far been identified as epidemic vectors, because of their adaptation to areas of human habitat.
  • DHF dengue haemorrhagic fever
  • yellow fever etc.
  • the incubation of the disease lasts from four to seven days on average.
  • the viremia that is to say the period of presence of the virus in the blood and therefore of possible transmission, is spread over about five days.
  • the antibodies are then declared. They stay in the blood. Immunity is therefore normally acquired for life.
  • a vaccine is available to prevent yellow fever. Vaccination is routine in exposed populations. However, 60 to 80% of the population must be immunized (naturally or after vaccination) to avoid epidemics. The antibodies appear after about ten days. Vaccination is contraindicated in pregnant women and infants under 6 months of age. A vaccine is also used in Europe • against tick-borne encephalitis. It is marketed under the name TICOVAC® (Baxter SA). Phase I and Phase II were conducted in the United States.
  • Immunoglobulins specific for hepatitis B or anti-HBs are widely used to protect any unvaccinated person injuring themselves with contaminated material: the newborn HBs positive antigen mother (in this case the injection must be performed immediately after the birth and should be accompanied by initiation of vaccination), the liver transplant patient to avoid reinfection of the graft and the sexual partner of a HBsAg positive antigen subject pending the effectiveness of vaccination.
  • These immunoglobulins make it possible to put in place a protection, either before the exposure to the risk, or in the 24 hours which follow the infectious contact (accidental puncture).
  • the Applicant has sought to develop a medicament for treating or preventing arboviroses based on specific immunoglobulins which rapidly immunize exposed people.
  • the Applicant has surprisingly shown that such a treatment requires the combination of immunoglobulins and F (ab) '2 and / or Fab fragments specific for the arbovirus to be treated to be effective. 5
  • Immunoglobulins are heterodimers consisting of 2 heavy chains and 2 light chains, linked together by disulfide bridges. Each chain t) v 'is incorporated, position K "-terminal, d r a region' or variable domain (encoded by the rearranged genes V-
  • Heavy specific for the antigen against which the antibody is directed, and the C-terminal position, 5 of a constant region consisting of a single domain CL for the light chain or 3 domains (CHl, CH2, and CH3) for the heavy chain.
  • the combination of the variable domains and the CH1 and CL domains of the heavy and light chains forms the Fab parts, which are connected to the Fc region by a very flexible hinge region allowing each Fab to bind to its antigenic target while the Fc region, mediator of the effector properties of the antibody, remains accessible to effector molecules such as Fc ⁇ R receptors and CIq.
  • IgG is the most abundant immunoglobulin
  • immunoglobulins G cross the placenta and, as a result, cause passive immunity in the fetus.
  • IgA is found mainly in secretions such as saliva, intestinal juice, sweat and breast milk.
  • the essential role of immunoglobulins. A is to prevent pathogens bind to the cell and more specifically to de- cells " 'recouvré ⁇ rté nt ⁇ m-s ⁇ itu-ant; .->.
  • IgM are immunoglobulins secreted during the first contact of the body with an antigen. This is the first class of immunoglobulin released by plasma cells. The presence of IgM in the blood indicates an ongoing infection.
  • fragment Fab Frametic Antigen Binding
  • Fc fragment Antigen Binding
  • an F (ab ') 2 fragment is generated, where the two Fab fragments remain bound by two disulfide bridges, and the Fc fragment is cleaved into several peptides.
  • the F (ab ') 2 fragment is formed of two Fab' fragments (an Fab 'fragment consisting of an Fab and a hinge region), linked by interchain disulfide bridges to form an F (ab') 2.
  • chromatography A method of separating the constituents of a mixture based on their selective adsorption by a suitable support is called "chromatography".
  • the invention relates to a concentrate of immunoglobulins and F (ab) '2 and / or Fab fragments specific for an arbovirus as a medicament.
  • Such F (ab) '2 or Fab fragments which contain the binding site of the antibody, may have lost a number of -properties of the whole antibody
  • the arbovirus in question that can be treated with a concentrate according to the invention can be, for example, one of the dengue viruses, the fever virus
  • the concentrate according to the invention is a concentrate of immunoglobulins A, G, and M and fragments F (ab) '2 and / or Fab specific for an arbovirus.
  • the concentrate according to the invention is a concentrate of immunoglobulin G exclusively or an immunoglobulin M concentrate exclusively, and F (ab) '2 and / or Fab fragments specific for an arbovirus.
  • concentrate according to the invention consists of a concentrate of immunoglobulin G exclusively and fragments F (ab) '2 and / or Fab of IgG and IgM specific for an arbovirus.
  • the concentrate according to the invention contains at least 50% of immunoglobulins of IgG type, and 90 to 98% of proteins reacting with antibodies specifically directed against human immunoglobulins, in particular 5 to 50% of F ( ab) 2 and / or Fab, in particular at least 50 to 60 g / l Ig and fragments for a pharmaceutical preparation.
  • Another object of the invention is the use of a concentrate according to the invention, for the manufacture of a medicament for the treatment of said arbovirus.
  • This treatment is prophylactic and / or curative. It can either transfer passive immunity to people who have not yet been affected in an epidemic region, or treat patients already affected by the virus.
  • the drug is administered topically, orally, mucosally, intramuscularly or intravenously. Its effectiveness lasts several tens of days, about 21 days, period beyond which the administration must be repeated if the epidemic or the symptoms persist.
  • the invention also relates to a method for preparing a concentrate according to the invention. The method comprises mixing an arbovirus specific immunoglobulin concentrate and a specific immunoglobulin concentrate of the same proteolytically modified arbovirus to obtain F (ab) '2 and Fab fragments specific for that arbovirus. This process therefore requires the preparation of at least one immunoglobulin concentrate. This method begins with the formation of a lot 'of at least 1000 plasma donations, each donation having a sufficient titer of Ig directed against said arbovirus.
  • the supernatant resulting from centrifugation or filtration may undergo a viral inactivation treatment, for example a conventional solvent / detergent viral inactivation treatment (Triton X100). If the precipitation carried out was a "typical" precipitation as described above, the caprylic acid residues in the supernatant are removed by PO4 calcium.
  • a viral inactivation treatment for example a conventional solvent / detergent viral inactivation treatment (Triton X100). If the precipitation carried out was a "typical" precipitation as described above, the caprylic acid residues in the supernatant are removed by PO4 calcium.
  • the supernatant then undergoes an additional purification step by chromatography on an anion exchanger performed at alkaline pH.
  • the pH of the supernatant is adjusted beforehand to a pH of from 8.9 to 9.1 and the column was balanced with a buffer having a pH ranging from 8.9 to 9.1.
  • the chromatography step allows the adsorption of immunoglobulins on the column and the passage of unadsorbed proteins in the effluent.
  • the chromatography may be carried out, for example, on a crosslinked polysaccharide gel or on a vinyl polymer on which DEAE, TMAE or QAE groups have been grafted.
  • the immunoglobulins thus eluted and harvested can be concentrated by ultrafiltration and subjected, for example, to conventional sterilizing filtration and then to filtration through nanometric filters of decreasing porosity of 100 to 15 nanometers.
  • the concentrated and filtered immunoglobulin solution is added with a pharmaceutically acceptable stabilizing agent such as those described in patent application WO 2004/091656, and this solution is then packaged as a sterile solution and optionally frozen and / or freeze-dried.
  • a pharmaceutically acceptable stabilizing agent such as those described in patent application WO 2004/091656, and this solution is then packaged as a sterile solution and optionally frozen and / or freeze-dried.
  • nanofiltration makes it possible to eliminate viruses that are resistant to viral inactivation treatment by solvent / detergent.
  • the Ig concentrate and the mixture of fragments resulting from the proteolysis are then mixed.
  • One liter of plasma rich in anti-Chikungunya antibodies is collected from volunteer donors recently infected with Chikungunya virus and cured symptoms of the disease.
  • the antibody titer is determined by a method 'Elisa consists in attaching virus antigens on a microtiter plate and then revealing the specific antibodies using a horseradish peroxidase labeled anti-immunoglobulin reagent.
  • the samples that have displayed a positive test at a dilution of at least 1/1000 are retained in the context of a "specific" type Elisa method.
  • the plasma pool resulting from step 1.1 is cooled to -3 ° C. and added during the cooling of a volume of ethanol sufficient to obtain a final concentration of ethanol of 8%.
  • the precipitate formed is removed.
  • the pH of the supernatant is then adjusted to pH 5.9 by adding acetate buffer, for example, cooled to -5 ° C., and supplemented with a volume of ethanol sufficient to obtain a final concentration of ethanol of 19%.
  • the precipitate formed is collected by centrifugation, for example, and redissolved in an acetate buffer, for example, so as to obtain a pH value of 4.7 to 4.9.
  • Octanoic acid is then added at 20 ° C., with vigorous stirring, until a final octanoic acid concentration of 20 g / l is obtained.
  • the precipitate formed is separated by centrifugation or alluvial filtration and removed. Tricalcium phosphate or activated charcoal is added to the supernatant, and the mixture is clarified by deep filtration.
  • the supernatant resulting from the clarification and containing the immunoglobulins is adjusted to pH 9 by the addition of a NaOH / glycine buffer, for example, and applied on an anion exchange column.
  • Equilibration buffer washing is carried out until a DO ' at 280 nm is obtained at the column outlet close to the OD 280 measured during the establishment of the baseline.
  • the proteolysate is neutralized, for example by the addition of sodium hydroxide, at pH 6.2 +/- 0.2. Diafiltration of the neutralized proteolysate is performed against a glycine buffer at pH 6.2 +/- 0.2, until an OD280 of about 0.005 is obtained, the OD 2S o being measured on the filtrate line of the membrane with a cutoff threshold of 30 kD or less.
  • Peptides resulting from pepsin proteolysis and having a size less than or equal to 30 kD are removed during passage over the cut-off membrane.
  • the proteolysate obtained therefore contains Fab fragments, F (ab) ' 2 type fragments, but proves to be devoid of Fc type fragments.
  • the resulting proteolysate is then mixed with the remaining 75% of the first IgG-containing eluate.
  • the mixture is subsequently concentrated by ultrafiltration to reach a final concentration ranging from 50 to 160 g / l, depending on the selected mode of administration.
  • the concentrate is titrated according to the method described in Edelman, R. et al. (American Journal of Tropical Medicine and Hygiene, 62 (6), 2000, pp. 681-685).
  • the anti-Chikungunya specific antibody titre of the concentrate thus obtained is at least 3 to 10 times higher than that of the starting plasma.
  • the concentrate resulting from step 1.3 is stabilized by mixing with a formulation comprising pharmaceutically acceptable excipients, such as, for example, glycine at a final concentration of 0.22M, or such as those described in WO 200 / 091,656.
  • a formulation comprising pharmaceutically acceptable excipients, such as, for example, glycine at a final concentration of 0.22M, or such as those described in WO 200 / 091,656.
  • the pH of the formulation added to the concentrate is compatible with obtaining a liquid mixture having a pH ranging from 4.2 to 5.6.
  • the administration of the resulting liquid mixture can be carried out, for example, intravenously, subcutaneously or intramuscularly, depending on the phlebological state of the recipient.
  • the dose administered is 0.2 to 0.8 ml / kg and may, in the event of an epidemic, be administered preventively every 3 weeks to particularly exposed persons, for example the elderly, pregnant women or newborns. .

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Virology (AREA)
  • Organic Chemistry (AREA)
  • Medicinal Chemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Molecular Biology (AREA)
  • Veterinary Medicine (AREA)
  • Public Health (AREA)
  • Immunology (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oncology (AREA)
  • Communicable Diseases (AREA)
  • Biochemistry (AREA)
  • Biophysics (AREA)
  • Genetics & Genomics (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Microbiology (AREA)
  • Mycology (AREA)
  • Epidemiology (AREA)
  • Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
  • Peptides Or Proteins (AREA)
  • Medicinal Preparation (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
EP07731238A 2006-03-31 2007-04-02 Konzentrat von immunglobulinen und f(ab)'2 und/oder fab fragmenten, die spezifisch für einen arbovirus sind; als medikament Withdrawn EP2004229A2 (de)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
FR0602803A FR2899112B1 (fr) 2006-03-31 2006-03-31 Concentre d'immunoglobulines et de fragments f (ab)'2 et/ou fab specifiques d'un arbovirus en tant que medicament.
PCT/FR2007/000560 WO2007118986A2 (fr) 2006-03-31 2007-04-02 Concentre d'immunoglobulines et de fragments f(ab) '2 et /ou fab specifiques d'un arbovirus en tant que medicament

Publications (1)

Publication Number Publication Date
EP2004229A2 true EP2004229A2 (de) 2008-12-24

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EP07731238A Withdrawn EP2004229A2 (de) 2006-03-31 2007-04-02 Konzentrat von immunglobulinen und f(ab)'2 und/oder fab fragmenten, die spezifisch für einen arbovirus sind; als medikament

Country Status (11)

Country Link
US (1) US7771725B2 (de)
EP (1) EP2004229A2 (de)
JP (1) JP2009531400A (de)
KR (1) KR20080110828A (de)
CN (1) CN101410136A (de)
AU (1) AU2007239414A1 (de)
CA (1) CA2647504A1 (de)
FR (1) FR2899112B1 (de)
IL (1) IL193820A0 (de)
TW (1) TW200904472A (de)
WO (1) WO2007118986A2 (de)

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR2899111B1 (fr) * 2006-03-31 2010-09-03 Lab Francais Du Fractionnement Concentre d'immunoglobulines specifiques du chikungunya en tant que medicament.
WO2011124635A1 (en) 2010-04-07 2011-10-13 Humalys Binding molecules against chikungunya virus and uses thereof
EP2374816B1 (de) 2010-04-07 2016-09-28 Agency For Science, Technology And Research Bindemoleküle gegen Chikungunya-Virus und Verwendungen davon
GB201006753D0 (en) 2010-04-22 2010-06-09 Biotest Ag Process for preparing an immunolobulin composition
AR125373A1 (es) * 2021-04-19 2023-07-12 Bharat Serums & Vaccines Ltd ANTICUERPOS POLICLONALES CONTRA SARS-CoV-2 Y SUS APLICACIONES

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
ATE301653T1 (de) 2000-12-15 2005-08-15 Glaxo Group Ltd Pyrazolopyridine
FR2824568B1 (fr) 2001-05-11 2004-04-09 Lab Francais Du Fractionnement Procede de preparation de concentres d'immunoglobulines humaines a usage therapeutique
FR2853551B1 (fr) 2003-04-09 2006-08-04 Lab Francais Du Fractionnement Formulation stabilisante pour compositions d'immunoglobulines g sous forme liquide et sous forme lyophilisee

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO2007118986A2 *

Also Published As

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WO2007118986A3 (fr) 2007-12-06
KR20080110828A (ko) 2008-12-19
WO2007118986A2 (fr) 2007-10-25
CA2647504A1 (en) 2007-10-25
TW200904472A (en) 2009-02-01
FR2899112B1 (fr) 2010-09-03
US20090041780A1 (en) 2009-02-12
CN101410136A (zh) 2009-04-15
WO2007118986A8 (fr) 2010-09-10
FR2899112A1 (fr) 2007-10-05
IL193820A0 (en) 2011-08-01
US7771725B2 (en) 2010-08-10
JP2009531400A (ja) 2009-09-03
AU2007239414A1 (en) 2007-10-25

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