Bacteria were among the first life forms to appear on Earth, and are present in most of its habitats. We can find bacteria in soil, water, acidic hot springs, radioactive waste, and the deep portions of Earth's crust. Moreover, they may even flourish in manned spacecraft. Among all, however, the most common one is to be found in plants and animals that bacteria are living in symbiotic and parasitic relationships with.
Why Scientists Put Much Strength in Bacteria Research and Development?
Bacteria exist among all our surroundings, thus research into them has become an essential task. Scientists never stop their steps in moving further in this field from its fist discovery in the 16th century by Antony van Leeuwemhoek, the farther modern microbiology. As the development of biotechnology, scientists now can use more advanced technique to push forward this research, bacterial display.
Why We Need Bacterial Display?
Bacterial display or bacterial surface display is a commonly used protein engineering technique, especially in terms of in vitro protein evolution. Libraries of polypeptides displayed on the surface of bacteria can be screened using flow cytometry or iterative selection procedures. This protein engineering technique allows us to put together the function of a protein and the gene that encodes it. Bacterial display can be used to find target proteins with desired properties and can be used to make affinity ligands which are cell-specific. This system can be used in many applications including the creation of novel vaccines, the identification of enzyme substrates and finding the affinity of a ligand for its target protein.
Hi-affinityTM Bacterial Display Technology for Creating Therapeutic Antibodies
Hi-affinityTM, offered by Creative Biolabs, is a unique branch of bacterial display technology based on a proprietary synthetic bacterial display human antibody library and a unique selection process natural to E. coli. This bacterial surface display technology enables the rapid isolation of target-specific antibodies without the labor intensive screening common to other recombinant and non-recombinant antibody production methods, resulting in unique single-chain variable fragment (scFV) antibodies that have both high specificity and extremely high affinity [Kd up to10-12] for the target antigen.
Creative Biolabs created the Hi-affinityTM human scFv antibody library by combining a highly diverse collection of synthetically-constructed randomized CDR sequences that are further diversified by random lengths using a unique proprietary technique. The large library has been specifically optimized to eliminate unwanted stop codons and aggregation-prone sequences. scFv molecules are first expressed in E. coli cytoplasm and then translocated and anchored into the bacterial plasma membrane. In the end, binder panels are selected by FACS or panning. Furthermore, multiple rounds of affinity maturation during library screening are incorporated through error prone PCR mutagenesis either directed at CDR or flanking sequences and selection by varying antigen dose.
Hi-affinityTM platform of Creative Biolabs utilizes a unique antibody selection process that relies on the natural twin-arginine translocation (Tat) system in E. coli. The featured benefit of Hi-affinityTM is its capacity of generating human antibodies with exceptionally high affinity.
From the starting point of knowing the existence of bacterial to research into them and put them into biotech development by now, it is easy to predict that there is more for human to explore.