Agency: Cordis | Branch: FP7 | Program: CP | Phase: SEC-2009-4.3-01 | Award Amount: 3.90M | Year: 2010
Botulinum neurotoxins (BoNTs), the most toxic substances known, are susceptible for use as bioweapons (listed as class A agents by CDC). Currently licensed animal derived antibodies or F(ab)2 preparations, are at a high risk of inducing adverse effects and their privately-owned stockpiles are limited. In this project, we will target the most lethal types of BoNTs: A (subtypes A1 and A2), B (B1 and B2) and E (E1). The antibodies will be directed against the C-terminus of the heavy chain and the light chain of each of these three BoNTs, as these domains contain neutralizing epitopes, according to the latest scientific data. The six corresponding immunogens will be produced in recombinant form, and utilized to immunize macaques (Macaca fascicularis), from which phage-displayed immune libraries will be built. Utilizing the phage technology, scFvs cross- reacting with A1 and A2, or B1 and B2subtypes will be panned. The best scFv from each library will be selected according to its high affinity and in vitro neutralization property. The six most neutralizing scFvs will then be super-humanized (germline-humanized) and expressed as IgGs, which will be tested in vivo, in a standardised model of protection and against toxins obtained from collections of clostridia strains. The project includes representatives of medical first-responders who will disseminate our results, and help create a market so that the necessary clinical studies could be performed in future. The project will offer an unequalled level of security against biothreats in Europe, based upon a family of well-tolerated and effective molecules.
Lfb Biotechnologies and Etat Francais Represente Par Le Delegue General Pour Larmement | Date: 2013-08-15
A chimeric monoclonal antibody targeted to ricin is presented. The light chain and heavy chain constant regions are respectively made up of the light chain and heavy chain constant regions of human immunoglobulin, and the light chain and heavy chain variable regions respectively include the light chain and heavy chain variable regions of macaque immunoglobulin. The antibody does not substantially induce any immune response against chimeric antibodies.
Lfb Biotechnologies | Date: 2013-06-05
The invention relates to a method for extracting a protein from milk, having at least one hydrophobic pocket and a negative charge to the natural pH of milk, that comprises the following steps: a) skimming and delipidation of the milk; b) passing the delipidated and skimmed fraction containing the protein on a chromatographic substrate on which is grafted a ligand having both a hydrophobic characteristic and an ionic characteristic in pH conditions enabling the protein to be retained on the substrate, the pH being higher than 4.6; c) elution of the protein; d) purification of the eluted fraction by removing the milk proteins from the eluted fraction; and e) recovering the protein.
Lfb Biotechnologies and NanoCarrier Co | Date: 2013-02-06
The invention relates to a pharmaceutical composition comprising factor VII encapsulated in micelles formed from block copolymer molecules containing (i) a hydrophilic polymer segment consisting of a polyalkylene glycol and (ii) a hydrophobic polymer segment consisting of a polyamino acid, with said polyamino acid comprising exclusively amino acid residues selected from the goup consisting of histidine, lysine, aspartic acid and glutamic acid residues, wherein a part of said amino acid residues is substituted with a hydrophobic group.
Lfb Biotechnologies | Date: 2011-05-10
The invention relates to an anti-idiotypical antibody targeting an antibody inhibiting the human fact VIII, said inhibiting antibody targeting the C2 region of the human factor VIII, the variable region of each of the light chains thereof being encoded by a sequence of nucleic acids of which at least 70% is identical to the murine sequence of nucleic acids SEQ ID NO: 1, and the variable region of each of the heavy chains thereof being encoded by a sequence of nucleic acids of which at least 70% is identical to the murine sequence of nucleic acids SEQ ID NO: 2, the constant regions of the light chains and the heavy chains being constant regions from a non-murine species. The invention also relates to the use of said antibody for activating the FcRIII receptors of cytotoxic immune cells, and to the production of a medicament especially for the treatment of haemophilia A.
Lfb Biotechnologies | Date: 2012-12-05
The present invention concerns a recombinant or transgenic factor VII compound, each factor VII molecule of the compound having glycan forms linked to N-glycosylation sites, wherein among all the factor VII molecules in said compound, glycan, biantennary, bisialylated and non-fucosylated forms are in the majority. The invention also concerns such a compound for use as a medication, and a method for preparing said compound, among others.
Lfb Biotechnologies | Date: 2013-05-02
The invention is related to a composition of recombinant or transgenic Factor VII, each molecule of Factor VII of the composition exhibiting two N-glycosylation sites, wherein, among all the molecules of FVII of the composition, the rate of Gal1,3G al glycan moieties is comprised between 0 and 4%. The invention is also related to a process for preparing such a composition of FVII.
Lfb Biotechnologies and Millegen | Date: 2012-12-26
The invention relates to a method for producing a variant of a parent polypeptide comprising a Fc region, which variant exhibits reduced binding to the protein C1 q and to at least one receptor FcyR as compared to the said parent polypeptide.
Lfb Biotechnologies | Date: 2011-12-30
The invention relates to a method for immobilizing nucleic ligands including at least one reactive amine function, by grafting on an activated solid substrate, including a step of coupling said nucleic acids on said activated solid substrate having a pH of less than 6.
Lfb Biotechnologies, Montpellier University, Center National Of Lutte Contre Le Cancer, French Institute of Health and Medical Research | Date: 2015-03-16
Novel mutated humanized 12G4 antibodies, and fragments thereof, directed against the anti-Mllerian hormone type II receptor.