Phage display is a laboratory technique for the study of
protein–protein, protein–peptide, and protein–
that uses bacteriophages (viruses that infect bacteria) to connect
proteins with the genetic information that encodes them. In this
technique, a gene encoding a protein of interest is inserted into a
phage coat protein gene, causing the phage to "display" the protein on
its outside while containing the gene for the protein on its inside,
resulting in a connection between genotype and phenotype. These
displaying phages can then be screened against other proteins,
DNA sequences, in order to detect interaction between the
displayed protein and those other molecules. In this way, large
libraries of proteins can be screened and amplified in a process
called in vitro selection, which is analogous to natural selection.
The most common bacteriophages used in phage display are M13 and fd
filamentous phage, though T4, T7, and λ phage have also been
Antibody maturation in vitro
4 General protocol
5 Selection of the coat protein
5.1 Filamentous phages
5.1.4 pVII and pIX
5.2 T7 phages
Bioinformatics resources and tools
7 See also
9 Further reading
10 External links
Phage display was first described by George P. Smith in 1985, when he
demonstrated the display of peptides on filamentous phage by fusing
the peptide of interest onto gene III of filamentous phage. A
patent by George Pieczenik claiming priority from 1985 also describes
the generation of phage display libraries. This technology was
further developed and improved by groups at the Laboratory of
Molecular Biology with
Greg Winter and John McCafferty, The Scripps
Research Institute with Lerner and Barbas and the German Cancer
Research Center with Breitling and Dübel for display of proteins such
as antibodies for therapeutic protein engineering.
Like the two-hybrid system, phage display is used for the
high-throughput screening of protein interactions. In the case of M13
filamentous phage display, the
DNA encoding the protein or peptide of
interest is ligated into the pIII or pVIII gene, encoding either the
minor or major coat protein, respectively. Multiple cloning sites are
sometimes used to ensure that the fragments are inserted in all three
possible reading frames so that the c
DNA fragment is translated in the
proper frame. The phage gene and insert
DNA hybrid is then inserted (a
process known as "transduction") into
Escherichia coli (E. coli)
bacterial cells such as TG1, SS320, ER2738, or XL1-Blue E. coli. If a
"phagemid" vector is used (a simplified display construct vector)
phage particles will not be released from the E. coli cells until they
are infected with helper phage, which enables packaging of the phage
DNA and assembly of the mature virions with the relevant protein
fragment as part of their outer coat on either the minor (pIII) or
major (pVIII) coat protein. By immobilizing a relevant
DNA or protein
target(s) to the surface of a microtiter plate well, a phage that
displays a protein that binds to one of those targets on its surface
will remain while others are removed by washing. Those that remain can
be eluted, used to produce more phage (by bacterial infection with
helper phage) and to produce a phage mixture that is enriched with
relevant (i.e. binding) phage. The repeated cycling of these steps is
referred to as 'panning', in reference to the enrichment of a sample
of gold by removing undesirable materials. Phage eluted in the final
step can be used to infect a suitable bacterial host, from which the
phagemids can be collected and the relevant
DNA sequence excised and
sequenced to identify the relevant, interacting proteins or protein
The use of a helper phage can be eliminated by using 'bacterial
packaging cell line' technology.
Elution can be done combining low-pH elution buffer with sonification,
which, in addition to loosening the peptide-target interaction, also
serves to detach the target molecule from the immobilization surface.
This ultrasound-based method enables single-step selection of a
Applications of phage display technology include determination of
interaction partners of a protein (which would be used as the
immobilised phage "bait" with a
DNA library consisting of all coding
sequences of a cell, tissue or organism) so that the function or the
mechanism of the function of that protein may be determined. Phage
display is also a widely used method for in vitro protein evolution
(also called protein engineering). As such, phage display is a useful
tool in drug discovery. It is used for finding new ligands (enzyme
inhibitors, receptor agonists and antagonists) to target
proteins. The technique is also used to determine tumour
antigens (for use in diagnosis and therapeutic targeting) and in
searching for protein-
DNA interactions using specially-constructed
DNA libraries with randomised segments. Recently, phage display has
also been used in the context of cancer treatments - such as the
adoptive cell transfer approach. In these cases, phage display is
used to create and select synthetic antibodies that target tumour
surface proteins. These are made into synthetic receptors for
T-Cells collected from the patient that are used to combat the
Competing methods for in vitro protein evolution include yeast
display, bacterial display, ribosome display, and mRNA display.
Antibody maturation in vitro
The invention of antibody phage display revolutionised antibody drug
discovery. Initial work was done by laboratories at the MRC Laboratory
of Molecular Biology (
Greg Winter and John McCafferty), the Scripps
Research Institute (Richard Lerner and Carlos F. Barbas) and the
German Cancer Research Centre
German Cancer Research Centre (Frank Breitling and Stefan
Dübel). In 1991, The Scripps group reported the first
display and selection of human antibodies on phage. This initial
study described the rapid isolation of human antibody Fab that bound
tetanus toxin and the method was then extended to rapidly clone human
anti-HIV-1 antibodies for vaccine design and
Phage display of antibody libraries has become a powerful method for
both studying the immune response as well as a method to rapidly
select and evolve human antibodies for therapy.
Antibody phage display
was later used by Carlos F. Barbas at The Scripps Research Institute
to create synthetic human antibody libraries, a principle first
patented in 1990 by Breitling and coworkers (Patent CA 2035384),
thereby allowing human antibodies to be created in vitro from
synthetic diversity elements.
Antibody libraries displaying millions of different antibodies on
phage are often used in the pharmaceutical industry to isolate highly
specific therapeutic antibody leads, for development into antibody
drugs primarily as anti-cancer or anti-inflammatory therapeutics. One
of the most successful was adalimumab, discovered by Cambridge
Antibody Technology as D2E7 and developed and marketed by Abbott
Laboratories. Adalimumab, an antibody to TNF alpha, was the world's
first fully human antibody, which achieved annual sales exceeding
Below is the sequence of events that are followed in phage display
screening to identify polypeptides that bind with high affinity to
desired target protein or
Target proteins or
DNA sequences are immobilised to the wells of a
Many genetic sequences are expressed in a bacteriophage library in the
form of fusions with the bacteriophage coat protein, so that they are
displayed on the surface of the viral particle. The protein displayed
corresponds to the genetic sequence within the phage.
This phage-display library is added to the dish and after allowing the
phage time to bind, the dish is washed.
Phage-displaying proteins that interact with the target molecules
remain attached to the dish, while all others are washed away.
Attached phage may be eluted and used to create more phage by
infection of suitable bacterial hosts. The new phage constitutes an
enriched mixture, containing considerably less irrelevant phage (i.e.
non-binding) than were present in the initial mixture.
Steps 3 to 6 are optionally repeated one or more times, further
enriching the phage library in binding proteins.
Following further bacterial-based amplification, the
DNA within in the
interacting phage is sequenced to identify the interacting proteins or
Selection of the coat protein
pIII is the protein that determines the infectivity of the virion.
pIII is composed of three domains (N1, N2 and CT) connected by
glycine-rich linkers. The N2 domain binds to the F pilus during
virion infection freeing the N1 domain which then interacts with a
TolA protein on the surface of the bacterium. Insertions within
this protein are usually added in position 249 (within a linker region
between CT and N2), position 198 (within the N2 domain) and at the
N-terminus (inserted between the N-terminal secretion sequence and the
N-terminus of pIII). However, when using the BamHI site located at
position 198 one must be careful of the unpaired Cysteine residue
(C201) that could cause problems during phage display if one is using
a non-truncated version of pIII.
An advantage of using pIII rather than pVIII is that pIII allows for
monovalent display when using a phagemid (Ff-phage derived plasmid)
combined with a helper phage. Moreover, pIII allows for the insertion
of larger protein sequences (>100 amino acids) and is more
tolerant to it than pVIII. However, using pIII as the fusion partner
can lead to a decrease in phage infectivity leading to problems such
as selection bias caused by difference in phage growth rate or
even worse, the phage's inability to infect its host. Loss of
phage infectivity can be avoided by using a phagemid plasmid and a
helper phage so that the resultant phage contains both wild type and
DNA has also been analyzed using pIII via a two complementary leucine
zippers system, Direct Interaction Rescue or by adding an 8-10
amino acid linker between the c
DNA and pIII at the C-terminus.
pVIII is the main coat protein of Ff phages. Peptides are usually
fused to the N-terminus of pVIII. Usually peptides that can be
fused to pVIII are 6-8 amino acids long. The size restriction
seems to have less to do with structural impediment caused by the
added section and more to do with the size exclusion caused by pIV
during coat protein export. Since there are around 2700 copies of
the protein on a typical phages, it is more likely that the protein of
interest will be expressed polyvalently even if a phagemid is
used. This makes the use of this protein unfavorable for the
discovery of high affinity binding partners.
To overcome the size problem of pVIII, artificial coat proteins have
been designed. An example is Weiss and Sidhu's inverted artificial
coat protein (ACP) which allows the display of large proteins at the
C-terminus. The ACP's could display a protein of 20kDa, however,
only at low levels (mostly only monovalently).
pVI has been widely used for the display of c
DNA libraries. The
display of c
DNA libraries via phage display is an attractive
alternative to the yeast-2-hybrid method for the discovery of
interacting proteins and peptides due to its high throughput
capability. pVI has been used preferentially to pVIII and pIII for
the expression of c
DNA libraries because one can add the protein of
interest to the C-terminus of pVI without greatly affecting pVI's role
in phage assembly. This means that the stop codon in the c
DNA is no
longer an issue. However, phage display of c
DNA is always limited
by the inability of most prokaryotes in producing post-translational
modifications present in eukaryotic cells or by the misfolding of
While pVI has been useful for the analysis of c
DNA libraries, pIII and
pVIII remain the most utilized coat proteins for phage display.
pVII and pIX
In an experiment in 1995, display of Glutathione S-transferase was
attempted on both pVII and pIX and failed. However, phage display
of this protein was completed successfully after the addition of a
periplasmic signal sequence (pelB or ompA) on the N-terminus. In a
recent study, it has been shown that AviTag, FLAG and His could be
displayed on pVII without the need of a signal sequence. Then the
expression of single chain Fv's (scFv), and single chain T cell
receptors (scTCR) were expressed both with and without the signal
PelB (an amino acid signal sequence that targets the protein to the
periplasm where a signal peptidase then cleaves off PelB) improved the
phage display level when compared to pVII and pIX fusions without the
signal sequence. However, this led to the incorporation of more helper
phage genomes rather than phagemid genomes. In all cases, phage
display levels were lower than using pIII fusion. However, lower
display might be more favorable for the selection of binders due to
lower display being closer to true monovalent display. In five out of
six occasions, pVII and pIX fusions without pelB was more efficient
than pIII fusions in affinity selection assays. The paper even goes on
to state that pVII and pIX display platforms may outperform pIII in
the long run.
The use of pVII and pIX instead of pIII might also be an advantage
because virion rescue may be undertaken without breaking the
virion-antigen bond if the pIII used is wild type. Instead, one could
cleave in a section between the bead and the antigen to elute. Since
the pIII is intact it does not matter whether the antigen remains
bound to the phage.
The issue of using Ff phages for phage display is that they require
the protein of interest to be translocated across the bacterial inner
membrane before they are assembled into the phage. Some proteins
cannot undergo this process and therefore cannot be displayed on the
surface of Ff phages. In these cases,
T7 phage display is used
T7 phage display, the protein to be displayed is
attached to the C-terminus of the gene 10 capsid protein of T7.
The disadvantage of using T7 is that the size of the protein that can
be expressed on the surface is limited to shorter peptides because
large changes to the T7 genome cannot be accommodated like it is in
M13 where the phage just makes its coat longer to fit the larger
genome within it. However, it can be useful for the production of a
large protein library for scFV selection where the scFV is expressed
on an M13 phage and the antigens are expressed on the surface of the
Bioinformatics resources and tools
Databases and computational tools for mimotopes have been an important
part of phage display study. Databases, programs and web
servers have been widely used to exclude target-unrelated
peptides, characterize small molecules-protein interactions and
map protein-protein interactions. Users can use three dimensional
structure of a protein and the peptides selected from phage display
experiment to map conformational eptiopes. Some of the fast and
efficient computational methods are available online (e.g. EpiSearch
 http://curie.utmb.edu/episearch.html ).
PelB leader sequence
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Selection Versus Design in Chemical Engineering
The ETH-2 human antibody phage library
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Proteins: key methods of study
Green fluorescent protein
Peptide mass fingerprinting/
Protein mass spectrometry
Surface plasmon resonance
Isothermal titration calorimetry
Freeze-fracture electron microscopy
Protein structure prediction
Protein structural alignment
Protein–protein interaction prediction
Photoactivated localization microscopy
Library resources about
Resources in your library