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.
