Transient expression of rabies virus glycoprotein (RVGP) in Drosophila melanogaster Schneider 2 (S2) cells

Transient expression of rabies virus G-glycoprotein using BHK-21 cells cultured in suspension

“…However, the RVGP volumetric and per cell number yields for SFV vector in combination of BHK-21 cell line cultured in suspension, both cell culture plate and spinner flask were higher than those obtained for transient expression of the same protein using plasmid vector and D. melanogaster Schneider 2 (S2) cells as a host. Specifically, in spinner flask, the RVGP per cell number yield in SFV-BHK-21 system (present study) was 40-fold higher than that reported for plasmid vector-(S2) cells (Suárez-Patiño et al 2014). Thus, the transient SFV-BHK-21 system could be an alternative for RVGP expression for use in lab-scale (structural and functional studies).…”

Purification of rabies virus glycoprotein produced in Drosophila melanogaster S2 cells: An efficient immunoaffinity method

“…2 Rabies virus glycoprotein (G in the native virus) is a protein present in the virus envelope and responsible for the main immune response. Insect cells have been constantly used for RVGP production [3][4][5][6][7] due to their capacity to grow in suspension and to require milder culture conditions than mammalian cells (such as no need for a CO 2 buffering system), also showing the capacity to promote several post-translational modifications. 8,9 Drosophila melanogaster Schneider 2 cells (S2 cells) constitute a robust and efficient expression system, [10][11][12] capable of promoting several posttranslational modifications, including a homogeneous glycan profile, with high reproducibility between protein production runs.…”

“…13 This cell line has been extensively studied for RVGP production. 7,8,14 RVGP is a membrane anchored, highly hydrophobic protein. 15,16 For purification of recombinant protein expressed in cellular membranes, cells need to be disrupted, generating a large number of contaminants and an increase in viscosity and proteolytic activity during the protein extraction, which increases the complexity of the purification process.…”

“…Drosophila melanogaster Schneider 2 cells (S2 cells) constitute a robust and efficient expression system, 10‐12 capable of promoting several post‐translational modifications, including a homogeneous glycan profile, with high reproducibility between protein production runs 13 . This cell line has been extensively studied for RVGP production 7,8,14 …”

Efficient production of antibody Fab fragment by transient gene expression in insect cells

“…They can also produce considerable amounts of recombinant proteins through posttranslational processing and modifications that are similar to those performed in mammalian cells (4). While insect cells have been widely used in the baculovirusinsect cell system for recombinant protein production (4)(5)(6)(7)(8), only a few studies have reported transient gene expression using insect cells as host cells (9)(10)(11).…”