Insect cell systems have become a vital tool in production of pharmaceutically relevant protein complexes for structural biology and drug discovery research. In many cases, in order to produce functional protein for these complexes, multiple chaperones or co-factors may be required. We discuss why co-expression is superior to co-infection, and investigate the role of specific chaperones in the production of complexes with case studies on important target proteins.

Our team employs insect cell protein synthesis together with artificial intelligence to accelerate vaccine development. We have used this approach to tackle development of vaccines against major public health threats including SARS-CoV-2, SARS, MERS, and influenza and our recombinant spike protein-based COVID-19 vaccine (Covax19/SpikoGen) obtained emergency use approval in the Middle East in October 2021, making this the first recombinant spike protein in the world to achieve approval. Our COVID-19 vaccine has many promising features including high yield, low cost, temperature stability and induces strong T and B cell memory that delivers broad protection with strong safety and tolerability.

Glycosylation very often has a significant effect on the activity, function, and efficacy of protein-based therapeutics. Using the geCHO platform, different glycovariants of the protein-based drug candidates can be produced for research, development, and manufacturing of optimal glycoforms. The geCHO platform is also very useful for generating reagents for the studies of the effect of glycosylation on glycoproteins in vitro and in vivo.

Virus-like particles (VLPs) are potential vaccine candidates owing to their safety and ability to trigger an effective cellular and humoral immune response. To develop a VLP vaccine against hand, foot, and mouth disease, we tried producing Enterovirus 71 VLPs in Chinese Hamster Ovary (CHO) cells. In my presentation, I will demonstrate the potential of CHO cells as a promising production platform for Enterovirus 71 VLPs.

The effects of deleterious synonymous or co-occurring multiple SNVs are much more challenging to identify and predict than nonsynonymous SNVs. We have developed prediction tools for identifying deleterious synonymous SNVs. Furthermore, we have proposed a new approach that can successfully assist in accurately predicting the effect of co-occurring variants. In this talk, strategies for predicting SNVs and some approaches to predict such exceedingly challenging nucleotide variants will be discussed.

The Center on Membrane Protein Production and Analysis (COMPPÅ) is a resource for advanced studies on membrane proteins, emphasizing technological innovation and cutting-edge biological applications. The center offers a gene-to-structure pipeline with an emphasis on expression and purification of membrane proteins. Here we present our various expression platforms which range from a cell-free approach to several prokaryotic and eukaryotic systems.

Cell-free transcription-translation (TXTL) has become a highly versatile multidisciplinary technology for bioengineering and synthetic biology. By enabling the rapid expression of genes and gene circuits, TXTL integrates an ever-growing variety of applications. In this talk, I will present an all-E. coli TXTL system, the extent of its capabilities, and the cell-free synthesis and characterization of membrane proteins.

While proteins are typically produced within cells, cell-free protein synthesis (CFPS) is a versatile biological technique that takes the existing transcriptional and translational machinery from cells. The combination of CFPS with multiple nanodisc platforms enables the production of hard-to-produce membrane proteins in their native-like state. The process is scalable and adaptable. We combined these technologies, to produced multiple types of membrane bound Chlamydial proteins for characterization and vaccine studies.

Matrix metalloproteinases (MMPs) have been the center of attention recently as targets to develop therapeutics that can treat diseases correlated to their overexpression. To study the MMP mechanism in solution, more facile and robust recombinant protein expression and purification methods are needed to produce active, soluble MMPs. A summary of recent methods used to overcome these challenges and improve the yields of soluble active MMPs will be discussed.