Expression and N-glycan analysis of human 90K glycoprotein in Drosophila S2 cells

Kim, Kyoung Ro; Kim, Yeon Kyu; Cheong, Hogyun; Kim, Jaoon Young Hwan; Joon, Hyung

doi:10.1016/j.enzmictec.2013.03.020

Cited by 7 publications

(2 citation statements)

References 18 publications

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“…codon pair bias | arbovirus | dengue | vaccine I nsects and mammals are separated by about 1 billion years of evolution (1), and besides obvious differences at the organismal level, they differ also in many biochemical processes (2)(3)(4)(5). They have subtle differences in how they encode proteins: for instance, their genes have different codon preferences (6, 7), different dinucleotide frequencies (8), and different codon pair preferences (see below).…”

mentioning

confidence: 99%

Large-scale recoding of an arbovirus genome to rebalance its insect versus mammalian preference

Shen¹,

Stauft

Gorbatsevych³

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

133

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The protein synthesis machineries of two distinct phyla of the Animal kingdom, insects of Arthropoda and mammals of Chordata, have different preferences for how to best encode proteins. Nevertheless, arboviruses (arthropod-borne viruses) are capable of infecting both mammals and insects just like arboviruses that use insect vectors to infect plants. These organisms have evolved carefully balanced genomes that can efficiently use the translational machineries of different phyla, even if the phyla belong to different kingdoms. Using dengue virus as an example, we have undone the genome encoding balance and specifically shifted the encoding preference away from mammals. These mammalian-attenuated viruses grow to high titers in insect cells but low titers in mammalian cells, have dramatically increased LD50s in newborn mice, and induce high levels of protective antibodies. Recoded arboviruses with a bias toward phylum-specific expression could form the basis of a new generation of live attenuated vaccine candidates.

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mentioning

confidence: 99%

Large-scale recoding of an arbovirus genome to rebalance its insect versus mammalian preference

Shen¹,

Stauft

Gorbatsevych³

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

133

View full text Add to dashboard Cite

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“…Recently, Olivero et al have demonstrated that Drosophila S2 cells co-transfected with the env and gag sequences were able to form virus-like particles (VLPs) displaying a BLV Env which retains structural motifs on its surface 42 . Stably transfected Drosophila melanogaster S2 cells have appeared as a major platform for recombinant protein expression 43 , 44 . N-glycosylation in S2 insect cells gives oligomannosidic or paucimannosidic glycans with lower complexity than mammalian cells 45 , making it a suitable eukaryotic expression system for biophysical, biochemical and structural characterization of recombinant secreted viral glycoproteins, as well documented in Carrión et al and others 46 , 47 .…”

Section: Introductionmentioning

confidence: 99%

Characterization and application of recombinant Bovine Leukemia Virus Env protein

Tomé-Poderti,

Olivero-Deibe,

Carrión

et al. 2024

Sci Rep

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The Bovine Leukemia Virus (BLV) Envelope (Env) glycoprotein complex is instrumental in viral infectivity and shapes the host’s immune response. This study presents the production and characterization of a soluble furin-mutated BLV Env ectodomain (sBLV-EnvFm) expressed in a stable S2 insect cell line. We purified a 63 kDa soluble protein, corresponding to the monomeric sBLV-EnvFm, which predominantly presented oligomannose and paucimannose N-glycans, with a high content of core fucose structures. Our results demonstrate that our recombinant protein can be recognized from specific antibodies in BLV infected cattle, suggesting its potential as a powerful diagnostic tool. Moreover, the robust humoral immune response it elicited in mice shows its potential contribution to the development of subunit-based vaccines against BLV.

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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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Expression and N-glycan analysis of human 90K glycoprotein in Drosophila S2 cells

Cited by 7 publications

References 18 publications

Large-scale recoding of an arbovirus genome to rebalance its insect versus mammalian preference

Large-scale recoding of an arbovirus genome to rebalance its insect versus mammalian preference

Characterization and application of recombinant Bovine Leukemia Virus Env protein

Glycosylation in Drosophila S2 cells

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