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Producing recombinant therapeutic glycoproteins with enhanced sialylation using CHO-gmt4 glycosylation mutant cells.
Goh, John S Y; Liu, Yingwei; Chan, Kah Fai; Wan, Corrine; Teo, Gavin; Zhang, Peiqing; Zhang, Yuanxing; Song, Zhiwei.
Afiliación
  • Goh JS; Bioprocessing Technology Institute; Agency for Science, Technology, and Research (A*STAR); Singapore, Singapore.
  • Liu Y; State Key Laboratory of Bioreactor Engineering; East China University of Science and Technology; Shanghai, China.
  • Chan KF; Bioprocessing Technology Institute; Agency for Science, Technology, and Research (A*STAR); Singapore, Singapore.
  • Wan C; Bioprocessing Technology Institute; Agency for Science, Technology, and Research (A*STAR); Singapore, Singapore.
  • Teo G; Bioprocessing Technology Institute; Agency for Science, Technology, and Research (A*STAR); Singapore, Singapore.
  • Zhang P; Bioprocessing Technology Institute; Agency for Science, Technology, and Research (A*STAR); Singapore, Singapore.
  • Zhang Y; State Key Laboratory of Bioreactor Engineering; East China University of Science and Technology; Shanghai, China.
  • Song Z; Bioprocessing Technology Institute; Agency for Science, Technology, and Research (A*STAR); Singapore, Singapore.
Bioengineered ; 5(4): 269­73, 2014.
Article en En | MEDLINE | ID: mdl-24911584
Recombinant glycoprotein drugs require proper glycosylation for optimal therapeutic efficacy. Glycoprotein therapeutics are rapidly removed from circulation and have reduced efficacy if they are poorly sialylated. Ricinus communis agglutinin-I (RCA-I) was found highly toxic to wild-type CHO-K1 cells and all the mutants that survived RCA-I treatment contained a dysfunctional N-acetylglucosaminyltransferase I (GnT I) gene. These mutants are named CHO-gmt4 cells. Interestingly, upon restoration of GnT I, the sialylation of a model glycoprotein, erythropoietin, produced in CHO-gmt4 cells was shown to be superior to that produced in wild-type CHO-K1 cells. This addendum summarizes the applicability of this cell line, from transient to stable expression of the recombinant protein, and from a lab scale to an industrial scale perfusion bioreactor. In addition, CHO-gmt4 cells can be used to produce glycoproteins with mannose-terminated N-glycans. Recombinant glucocerebrosidase produced by CHO-gmt4 cells will not require glycan remodeling and may be directly used to treat patients with Gaucher disease. CHO-gmt4 cells can also be used to produce other glycoprotein therapeutics which target cells expressing mannose receptors.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tetrahidrofolato Deshidrogenasa / Eritropoyetina / N-Acetilglucosaminiltransferasas / Ácido N-Acetilneuramínico / Ingeniería Celular Límite: Animals / Humans Idioma: En Revista: Bioengineered Año: 2014 Tipo del documento: Article País de afiliación: Singapur Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tetrahidrofolato Deshidrogenasa / Eritropoyetina / N-Acetilglucosaminiltransferasas / Ácido N-Acetilneuramínico / Ingeniería Celular Límite: Animals / Humans Idioma: En Revista: Bioengineered Año: 2014 Tipo del documento: Article País de afiliación: Singapur Pais de publicación: Estados Unidos