University Biology Report: Phage Display and Antibody Development

This report delves into the phage display technique, a crucial process used in laboratories for studying protein-protein interactions, particularly in the context of antibody production. The report highlights the advantages of phage display, such as large-scale antibody production, time efficiency, and better control over the selection process. It compares phage display to other techniques like hybridoma development and chimeric antibody creation, emphasizing the role of recombinant DNA technology. The report discusses the process of phage display, which involves displaying foreign peptides on phage particle surfaces, enabling the screening of toxic antigens and providing direct access to the sequence. It also explores the applications of phage display in various fields, including antivenom research and toxicology. Finally, the report concludes that phage display is an effective technique for the development of humanized antibodies, supported by the references provided.

Running head: BIOLOGY
PHAGE DISPLAY
Name of the Student
Name of the University
Author Note

1Running head: BIOLOGY
Phage display is a process used in laboratories, which allows the researchers to study
protein-protein interactions. These interactions are studied on a large scale and the proteins
are selected by their affinity levels for their specific targets. APD (Antibody phage display)
allows the in vitro selection of monoclonal antibodies, which are specific and have a high
affinity for their targets (1). However, Phage display is not the only process used for
producing humanized antigens. Hybridoma development technologies are mostly used to
produce humanized antibodies (monoclonal antibodies). Repertoire cloning is another
technique used for the production of humanized antibody fragments (2). The chimeric
antibody creating process is another process that is widely used in the production of
humanized antibodies. However, recombinant DNA technology has been considered as the
most effective strategy for this process of antibody development (3).
There are various techniques, which have been discovered in the fields of molecular
biology for the production of humanized antibodies and antibody fragments. Most of these
antibodies have been produced on the basis of monoclonal antibody generation. The process
of phage display was discovered a decade ago, which opened new windows for the
recombinant antibody fragments production. This process utilizes a phage to display the
foreign peptides on the phage particle surface (4). The central advantages of the phage
display system are its large scale production of antibodies, time-efficient process, better
control over the selection process, various probabilities to screen the toxic antigens and to
provide direct access to the sequence (5). According to various researches made with the
phage display system, a connection between the phenotype and genotype is generated due to
the expression of peptides on the surface of the bacteriophage capsid. The phage has been
observed to infect Escherichia coli and use its internal system of replication to display new
phages instead of killing the host cells. Therefore, it can be stated that this process increases
the rate of production of antibodies. Another major advantage of this process is that it can be

2Running head: BIOLOGY
used to generate libraries from any animal or humans making it possible for the direct
screening of antibodies (). This process enables to have an immune or naïve library of phage
and can be used to detect an antibody and antigen interaction. However, hybridoma
developmental techniques can be used when a library is already available. This process is
also large and lasts for only a short length of time. This process also allows a greater diversity
in the screening of antibodies. The display of phage can also be used for antivenom research
and toxicology because of the ability to facilitate works with non-immunogenic and toxic
antigens (5). The main advantages of hybridoma technologies use a large-scale production of
antibodies along with a higher specificity and antibody yield with sensitivity. The primary
disadvantage lies in the fact that there is longer generation time for the bacteria and phage
complex, incomplete generation of epitopes and often requires further humanization. The
process of phage display is more expensive, binders may have a lower affinity and the
process is more difficult from a technical point of view (5). Thus, it can be stated that the
phage display technique is of better use because of a higher number of advantages available
for the process of phage display. Another technique used for the production of humanized
antibody fragments is the generation of chimeric antibodies (6). Mouse and human antibodies
are similar in structure as per the research studies. This process utilizes the combination of
mouse DNA encoding the binding portion of monoclonal antibodies and human DNA
segments producing the antibodies in living cells. This process has made it possible to
develop a part human and part mouse antibody. However, it can still be stated that the phage
display technique also is used for the variable antibody domain expression on the filamentous
coat proteins of phage (5).
On a concluding note, it can be stated that there are various strategies that are used to
develop the humanized antibody fragments. There are techniques which utilize only the
human antibodies, some utilize the combination of two prokaryotic organisms to create one

3Running head: BIOLOGY
humanized antigen (phage display technique) and some form chimeric antibodies. All the
techniques have merits and limitations for each of them. On a group, it can be stated that
recombinant DNA technology can be used to produce the most effective antibodies. Thus,
phage display can be stated as the most effective process for the development of humanized
antibodies.

4Running head: BIOLOGY
References:
1. Frenzel A, Schirrmann T, Hust M. Phage display-derived human antibodies in clinical
development and therapy. InMAbs 2016 Oct 2 (Vol. 8, No. 7, pp. 1177-1194). Taylor &
Francis.
2. Miyama T, Kawase T, Kitaura K, Chishaki R, Shibata M, Oshima K, Hamana H, Kishi H,
Kuzushima K, Saji H, Suzuki R. Comprehensive T-Cell Receptor Repertoire Analysis Using
Deep Sequencing and Single Cell Cloning Reveals Extreme Oligoclonality of Ex Vivo
Expanded Cytomegalovirus-Reactive Cytotoxic T-Cells.
3. Marvin, J.S. and Lowman, H.B., 2015. Antibody humanization and affinity maturation
using phage display. Phage Display in Biotechnology and Drug Discovery.
4. Frenzel A, Kügler J, Helmsing S, Meier D, Schirrmann T, Hust M, Dübel S. Designing
human antibodies by phage display. Transfusion Medicine and Hemotherapy.
2017;44(5):312-5. Shim H. Therapeutic antibodies by phage display. Current pharmaceutical
design. 2016 Dec 1;22(43):6538-59.
6. Guo H, Chen H, Zhu Q, Yu X, Rong R, Merugu SB, Mangukiya HB, Li D. A humanized
monoclonal antibody targeting secreted anterior gradient 2 effectively inhibits the xenograft
tumor growth. Biochemical and biophysical research communications. 2016 Jun
17;475(1):57-63.