Recombinant antibodies have many advantages in both medical and research applications, which make them a popular subject of exploration and new production against specific targets.
The most commonly used form is the single chain variable fragment (scFv), which has shown the most promising traits exploitable in human medicine and research.
[8][10] The functionality may be enhanced by site-specific chemical modifications, adding a peptide-tag or by fusion with a gene to achieve production of bifunctional recombinant antibodies.
[11] Structurally Fab fragments consist of two sets of variable and constant components, which create two polypetide chains.
It consists of determining the sequence of the desired product followed by refinement of the codon, then gene synthesis and construct generation.
[15] In the beginning phases of the recombinant antibody production it was important to achieve the assembly of a functional Fv fragment in Escherichia coli.
[16] Second essential prerequisite for the modern day production of scFv was the successful assembly of recombinant antibodies from heavy and light chain of immunoglobulin.
Using a synthetic or human Ab library, as opposed to immunization of animals and the subsequent generation of stable hybridoma cell lines, requires fewer resources and produces less waste, making the entire process more sustainable.
The hybridoma cell lines, which produced large quantities of relatively pure and predictable antibodies was first introduced in 1975.
Despite its indisputable role in scientific discoveries and numerous treatment strategies, the hybridoma technology presents researchers with some obstacles such as ethical issues, potential to lose expression of the target protein or lengthy production and most importantly the development of HAMA in patients as mentioned previously.
[5] The most commonly applied technology to produce recombinant antibodies in the laboratory settings today is the phage display.
[10] From all the possible phage display systems, the most common is the Escherichia coli, due to its rapid growth and division rate and cheap set up and maintenance.
[5] Recombinant antibodies fulfill a large spectrum of functions spanning from research to diagnosis and treatment therapies for various diseases.
Specific recombinant antibodies are designed to bind with to surface heparin sulphate proteoglycan (HSP), which complicates or even disables the entry of the HSV into the host cell.
[22] As was mentioned in the beginning of this section, recombinant antibodies can also be used in diagnosis, an example of such diagnostic application is the detection of rabies virus.
In case of rabies infection, which is only treatable shortly after exposure, accurate and precise diagnosis is vital for survival of the patient.
As mentioned previously the recombinant antibodies and especially those, which have been developed in phage display are highly specific, have great pharmacokinetics and could be used in wide range of treatments.
Last but not least of their advantages during production is the possibility to optimize and genetically engineer the recombinant antibodies based on the current demand of the patient or researcher.
[4] An experienced technician is required to perform the phage display and third it is almost inevitable to include outsource companies in the process for the gene synthesis and construct generation.