Selected article for: "absence presence and protein expression"
Author: Frenzel, André; Hust, Michael; Schirrmann, Thomas
Title: Expression of Recombinant Antibodies
  • Document date: 2013_7_29
    • ID: 06o7pa3d_30
    Snippet: Secreted monomeric anti-phOx scFv were obtained at levels of up to 32 mg/L in a 6-L bioreactor with 10 9 cells per liter after 72 h with an m.o.i. of 1 (132). Production yields of 6-18 mg/L have been achieved for various IgGs (133). Immunoglobulins produced in High Five cells showed mammalian-like terminal galactosyl residues β(1,4)-linked to the biantennary GlcNAc residues. In contrast, the absence of sialylation, the formation of paucimannosid.....
    Document: Secreted monomeric anti-phOx scFv were obtained at levels of up to 32 mg/L in a 6-L bioreactor with 10 9 cells per liter after 72 h with an m.o.i. of 1 (132). Production yields of 6-18 mg/L have been achieved for various IgGs (133). Immunoglobulins produced in High Five cells showed mammalian-like terminal galactosyl residues β(1,4)-linked to the biantennary GlcNAc residues. In contrast, the absence of sialylation, the formation of paucimannosidic structures and the presence of potentially allergenic α(1,3)fucose linkages are different to mammalian glycosylation (134). Nevertheless, IgGs produced in insect cells were able to mediate effector functions like complement binding (135, 136) and ADCC (137). Insect cell protein expression was improved using protease deficient baculovirus strains or cell lines with additional glycosyltransferase gene modifications to obtain glycosylation patterns comparable to mammalian cell lines (138-141).

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