Enhanced production of human full-length immunoglobulin G1 in the periplasm of Escherichia coli

• Published in: Applied microbiology and biotechnology Vol. 98; no. 3; pp. 1237 - 1246
• Main Authors: Lee, Yong Jae, Lee, Dong Hwa, Jeong, Ki Jun
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer-Verlag 01.02.2014; Springer Berlin Heidelberg; Springer; Springer Nature B.V
• Subjects: anthrax; Antibiotics; Antigens; Antigens, Bacterial - metabolism; Applied Genetics and Molecular Biotechnology; Bacterial Toxins - metabolism; Biomedical and Life Sciences; biopharmaceuticals; Biotechnology; Cultivation; Cytotoxicity; E coli; economics; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Fc receptors; FDA approval; Gene expression; Genetic engineering; Glucose; glycosylation; Humans; Immunoglobulin G; Immunoglobulin G - biosynthesis; Immunoglobulin G - genetics; Immunoglobulins; Life Sciences; Microbial Genetics and Genomics; Microbiology; Monoclonal antibodies; Periplasm - metabolism; Physiological aspects; Plasmids; Receptors, IgG - metabolism; Recombinant Proteins - biosynthesis; Recombinant Proteins - genetics; Studies; Toxins; South Korea; 5′ UTR; Fed-batch cultivation; Secretion; Immunoglobulin G

Monoclonal antibodies are currently the most important pharmaceutical proteins, and the economic production of functional immunoglobulin G (IgG) is an important issue in biotechnology. Recent successes in the development of aglycosylated IgG variants that do not require glycosylation for effector fu...