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Plant-Based Production of Biosimilar Drug Products
Published in Laszlo Endrenyi, Paul Jules Declerck, Shein-Chung Chow, Biosimilar Drug Product Development, 2017
Kenny K. Y. So, Michael R. Marit, Michael D. McLean, J. Christopher Hall
Despite the high degree of conservation in glycosylation patterns in eukaryotes, N-glycosylation mutants of Arabidopsis thaliana show no abnormal morphology. However, improper N-glycosylation in humans has been correlated with the pathogenesis of various acquired and immunological diseases (Nagels et al., 2012; Strasser et al., 2004b; Varki and Freeze, 2009; Xue et al., 2013). With regard to therapeutic proteins, proper N-glycosylation is of particular concern as it is required to maintain the pharmaceutical efficacy of the therapeutic; improper N-glycosylation may result in diminished therapeutic efficacy and could also lead to immunogenicity in the patient.
Cell Physiology
Published in Wei-Shou Hu, Cell Culture Bioprocess Engineering, 2020
N-glycosylation is initiated by the transfer of a preassembled oligosaccharide (Glc3Man9GlcNAc2, an oligosaccharide of three glucose, nine mannose, and two N-acetylglucosamine) to the asparagine in a recognition sequence of a nascent protein in the ER lumen (Figure 3.21).7
Model-guided concurrent data assimilation for calibrating cardiac ion-channel kinetics
Published in IISE Transactions on Healthcare Systems Engineering, 2023
Haedong Kim, Hui Yang, Andrew R. Ednie, Eric S. Bennett
To further investigate it, we generated the histograms of the maximum conductance of IKslow1 (G Kslow1), which is the most significant parameter determining the magnitude of the current (see Fig. 9(b)), and experimental IK density from the in-vitro data. There is clear skewness in MGAT1KO IKsum density (small variance), while WT IK density is more disperse (high variance). Calibrated parameters, for example G Kslow1 , likely show smaller variations in MGAT1KO to address this trend in the experimental data. It is likely due to significant IK reduction in the diseased group combined with the elimination of complex N-glycosylation, thereby minimizing potential variability of N-glycan structures
Effects of various pine needle extracts on Chinese hamster ovary cell growth and monoclonal antibody quality
Published in Preparative Biochemistry & Biotechnology, 2023
Dingyue Zhang, Jinshu Qiu, Qing-Tian Niu, Tingting Liu, Rulin Gu, Xiaoying Zhang, Shun Luo
Many studies have found that pine needles are extremely rich in flavonoids, vitamins, amino acids, mineral elements, alkaloids, and polysaccharides.[11] And possess hypoglycemic, lipid regulation, antitumor, anti-aging, and antibacterial properties.[12,13] The natural water-soluble bioflavonoid concentrates and alkaloids from pine needle extracts have antioxidant activity functions, which can effectively remove free radicals.[14–16] Plant polysaccharides have a wide range of biological activities and desirable functional properties.[17] It has been reported that some small antioxidant molecules without direct nutritional value added to the cell culture medium can increase the productivity of CHO cells or protect the mAb from being oxidized.[18] Many infrequently used sugars, and the corresponding cellular response toward them as substrates led to differences in the protein N-glycosylation profile of a recombinant glycoprotein.[19] It has also been reported that the addition of bioflavonoids to animal cell cultures can effectively reduce the acidic charge variants on recombinant mAbs and their dual variable regions. Besides reducing the acidic charge variants of mAbs, the use of bioflavonoids can improve the structure and function of antibodies to varying degrees,[20] as well as product quality with less heterogeneity. The antioxidants, bioflavonoids, and polysaccharides in the pine needle extract have potential effects on the growth of CHO cells and the production of mAbs.
Production and characterization of a fusion form of hepatitis E virus tORF2 capsid protein in Escherichia coli
Published in Preparative Biochemistry & Biotechnology, 2021
Mohamed Boumaiza, Khaled Trabelsi, Zeineb Choucha, Ines Akrouti, Serena Leone, Delia Picone, Héla Kallel
Hepatitis E virus (HEV), a small, non-enveloped RNA virus of the family Hepeviridae, is associated with endemic and epidemic acute viral hepatitis in developing countries. HEV genome is a positive-sense, single-stranded, 7.2-kb RNA containing three open reading frames (ORFs). ORF1 encodes nonstructural polyprotein (nsP) with multiple domains.[1]ORF2 encodes the viral structural protein of 660 amino acids (aa) which is involved in virion assembly and immunogenicity[2] and ORF3 encodes a small protein associated with virion morphogenesis and release.[3] It has been reported that this protein, encoded by ORF3, generates transient antibodies that are unsuitable for serological diagnosis of HEV.[4] Clinical strains of HEV have been diagnosed by quantifying viral RNA in culture supernatants and cell lysates.[5] On the other hand, the ORF2 gene is highly conserved among HEV species and has been shown to induce long-lived immunity, therefore it has been selected for serological diagnosis of HEV and used as the main antigen for vaccine development against HEV infection.[4,6,7] Furthermore, it has been reported that HEV infection leads to the secretion of 3 forms of ORF2: infectious ORF2 (ORF2i), glycosylated ORF2 (ORF2g), and cleaved ORF2 (ORF2c).[8] Indeed, TORF2i, which correspond to the structural component of infectious particles, is not glycosylated. However, it has been demonstrated recently that ORFg/c protein is N-glycosylated on N1 and N3 sites but not on the N2 site and that N-glycosylation of ORF2 protein does not play any role in replication and assembly of infectious HEV particles.[9]