Expression and Immunogenicity of a Recombinant Chimeric Protein of Human Colorectal Cancer Antigen GA733-2 and an Fc Antibody Fragment in Stably Transformed Drosophila melanogaster S2 Cells

Seok, Yeon Ju; Kim, Kyung Il; Yoo, Ki Hyun; Jeon, Hoon; Lee, Hyun Ho; Shon, Dong Hwa; Ko, Ki Sung; Kang, Hyung Sik; Lee, Kyung Jin; Oh, Doo-Byoung; Joung, Young Hee; Chung, In Sik

doi:10.1007/s12010-010-8909-0

Appl Biochem Biotechnol

2010

DOI: 10.1007/s12010-010-8909-0

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Expression and Immunogenicity of a Recombinant Chimeric Protein of Human Colorectal Cancer Antigen GA733-2 and an Fc Antibody Fragment in Stably Transformed Drosophila melanogaster S2 Cells

Yeon Ju Seok

Kyung Il Kim

Ki Hyun Yoo

et al.

Abstract: Human colorectal cancer antigen GA733-2 fused to the immunoglobin Fc fragment (GA733-2-Fc) was expressed in stably transformed Drosophila melanogaster S2 cells, and the immunogenicity of recombinant GA733-2-Fc was investigated in mice. Recombinant GA733-2-Fc was secreted into a culture medium with a molecular mass of approximately 65 kDa. Recombinant GA733-2-Fc was purified to homogeneity using affinity fractionation with Protein A sepharose 4 Fast Flow. Recombinant GA733-2-Fc proteins elicited production of s… Show more

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Cited by 4 publications

References 17 publications

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Glycosylation in Drosophila S2 cells

Xu,

Tong,

Zhang

et al. 2024

Biotech & Bioengineering

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In recent years, there has been a remarkable surge in the approval of therapeutic protein drugs, particularly recombinant glycoproteins. Drosophila melanogaster S2 cells have become an appealing platform for the production of recombinant proteins due to their simplicity and low cost in cell culture. However, a significant limitation associated with using the S2 cell expression system is its propensity to introduce simple paucimannosidic glycosylation structures, which differs from that in the mammalian expression system. It is well established that the glycosylation patterns of glycoproteins have a profound impact on the physicochemical properties, bioactivity, and immunogenicity. Therefore, understanding the mechanisms behind these glycosylation modifications and implementing measures to address it has become a subject of considerable interest. This review aims to comprehensively summarize recent advancements in glycosylation modification in S2 cells, with a particular focus on comparing the glycosylation patterns among S2, other insect cells, and mammalian cells, as well as developing strategies for altering the glycosylation patterns of recombinant glycoproteins.

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Glycosylation in Drosophila S2 cells

Xu,

Tong,

Zhang

et al. 2024

Biotech & Bioengineering

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Expression of a recombinant chimeric protein of hepatitis A virus VP1-Fc using a replicating vector based on Beet curly top virus in tobacco leaves and its immunogenicity in mice

et al. 2011

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We describe the expression and immunogenicity of a recombinant chimeric protein (HAV VP1-Fc) consisting of human hepatitis A virus VP1 and an Fc antibody fragment using a replicating vector based on Beet curly top virus (BCTV) in Agrobacterium-infiltrated Nicotiana benthamiana leaves. Recombinant HAV VP1-Fc was expressed with a molecular mass of approximately 68 kDa. Recombinant HAV VP1-Fc, purified using Protein A Sepharose affinity chromatography, elicited production of specific IgG antibodies in the serum after intraperitoneal immunization. Following vaccination with recombinant HAV VP1-Fc protein, expressions of IFN-γ and IL-4 were increased in splenocytes at the time of sacrifice. Recombinant VP1-Fc from infiltrated tobacco plants can be used as an effective experimental immunogen for research into vaccine development.

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Optimized expression of the antimicrobial protein Gloverin from Galleria mellonella using stably transformed Drosophila melanogaster S2 cells

2017

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Antimicrobial proteins and peptides (AMPs) are valuable as leads in the pharmaceutical industry for the development of novel anti-infective drugs. Here we describe the efficient heterologous expression and basic characterization of a Gloverin-family AMP derived from the greater wax moth Galleria mellonella. Highly productive single-cell clones prepared by limiting dilution achieved a 100% increase in productivity compared to the original polyclonal Drosophila melanogaster S2 cell line. Comprehensive screening for suitable expression conditions using statistical experimental designs revealed that optimal induction was achieved using 600 µM CuSO at the mid-exponential growth phase. Under these conditions, 25 mg/L of the AMP was expressed at the 1-L bioreactor scale, with optimal induction and harvest times ensured by dielectric spectroscopy and the online measurement of optical density. Gloverin was purified from the supernatant by immobilized metal ion affinity chromatography followed by dialysis. In growth assays, the purified protein showed specific antimicrobial activity against two different strains of Escherichia coli.

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Expression and Immunogenicity of a Recombinant Chimeric Protein of Human Colorectal Cancer Antigen GA733-2 and an Fc Antibody Fragment in Stably Transformed Drosophila melanogaster S2 Cells

Cited by 4 publications

References 17 publications

Glycosylation in Drosophila S2 cells

Glycosylation in Drosophila S2 cells

Expression of a recombinant chimeric protein of hepatitis A virus VP1-Fc using a replicating vector based on Beet curly top virus in tobacco leaves and its immunogenicity in mice

Optimized expression of the antimicrobial protein Gloverin from Galleria mellonella using stably transformed Drosophila melanogaster S2 cells

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