Special Issue "Phage Display"

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry, Molecular Biology and Biophysics".

Deadline for manuscript submissions: closed (29 February 2012)

Special Issue Editors

Guest Editor
Prof. Dr. Stephen Mahler
Australian Institute for Bioengineering and Nanotechnology (AIBN), Corner College and Cooper Rds (Bldg 75), The University of Queensland, Brisbane Qld 4072, Australia
E-Mail: s.mahler@eng.uq.edu.au

Guest Editor
Dr. Martina Jones
Australian Institute for Bioengineering and Nanotechnology (AIBN), The University of Queensland, Brisbane Qld 4072, Australia
E-Mail: martina.jones@uq.edu.au

Special Issue Information

Dear Colleagues,

Antibodies have proven to be one of the most important classes of biological molecules with widespread use as research, diagnostic and therapeutic reagents, due to their unique and high affinity binding to a diverse range of targets. In vitro display technology, such as the display of antibody fragments on the surface of M13, fd and f1 filamentous bacteriophage (phage display), offers a highly powerful method capable of generating antibodies to any desired target with specificity and affinity that is not achievable using established hybridoma approaches [1].

The success or failure of in vitro display is dependent on a number of variables including;

  • Size and diversity of immunoglobulin gene library
  • Quality and purity of target antigen
  • Complexity of target
  • Biopanning strategies

Immunoglobulin gene libraries can be composed of natural antibody sequences isolated from either naïve or immunised antibody-producing cells, or can be synthesised to contain random complementarity-determining sequences, allowing isolation of non-naturally occurring binders. Antigens for panning are commonly purified native or recombinant proteins, or whole cells or viruses, but may also be non-protein samples such as lipids or carbohydrates.

The isolation of antibodies against a given target antigen is relatively straight forward, and three to four iterations (rounds) of biopanning generally result in the isolation of one or more antibodies to different epitopes located on the target. However there are more complex scenarios for isolation of antibodies against targets, which require designing specific strategies for biopanning, often incorporating combinations of negative selection steps, to deplete the repertoire of irrelevant antibodies. Such examples include isolation of antibodies against viral antigens that are able to discriminate between closely related subtypes [2], or panning against whole cells where the desired target is only a fraction of the available epitopes present on the cell.

Phage display is ideal for such complex scenarios as experimental conditions can easily be altered such as stringency of selection or negative depletion. Additionally, isolated antibodies can easily be mutagenised for affinity maturation.

Prof. Dr. Stephen Mahler
Dr. Martina Jones
Guest Editors

References

1. Smith, G.P.; Petrenko, V.A. Phage Display. Chem. Rev. 1997, 97, 391–410.
2. Bradbury, A.R.M.; Sidhu, S.; Dubel, S.; McCafferty, J. Beyond natural antibodies: the power of in vitro display technologies. Nat. Biotechnol. 2011, 29, 245–254

Keywords

  • antibodies
  • biopanning
  • phage display
  • subtractive selection
  • whole cell panning

Published Papers (7 papers)

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Displaying article 1-7
p. 7038-7056
by , , , , , , ,  and
Int. J. Mol. Sci. 2012, 13(6), 7038-7056; doi:10.3390/ijms13067038
Received: 13 March 2012; in revised form: 14 May 2012 / Accepted: 25 May 2012 / Published: 7 June 2012
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(This article belongs to the Special Issue Phage Display)
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p. 6582-6603
by , , ,  and
Int. J. Mol. Sci. 2012, 13(6), 6582-6603; doi:10.3390/ijms13066582
Received: 29 February 2012; in revised form: 7 April 2012 / Accepted: 17 May 2012 / Published: 29 May 2012
Show/Hide Abstract | Cited by 1 | PDF Full-text (1234 KB) | HTML Full-text | XML Full-text | Supplementary Files
(This article belongs to the Special Issue Phage Display)
p. 5179-5194
by  and
Int. J. Mol. Sci. 2012, 13(4), 5179-5194; doi:10.3390/ijms13045179
Received: 28 January 2012; in revised form: 29 February 2012 / Accepted: 19 April 2012 / Published: 24 April 2012
Show/Hide Abstract | Cited by 3 | PDF Full-text (215 KB) | HTML Full-text | XML Full-text
(This article belongs to the Special Issue Phage Display)
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p. 5254-5277
by , , ,  and
Int. J. Mol. Sci. 2012, 13(4), 5254-5277; doi:10.3390/ijms13045254
Received: 9 February 2012; in revised form: 9 April 2012 / Accepted: 20 April 2012 / Published: 24 April 2012
Show/Hide Abstract | Cited by 1 | PDF Full-text (390 KB) | HTML Full-text | XML Full-text
(This article belongs to the Special Issue Phage Display)
p. 4937-4948
by , , , , , ,  and
Int. J. Mol. Sci. 2012, 13(4), 4937-4948; doi:10.3390/ijms13044937
Received: 1 March 2012; in revised form: 27 March 2012 / Accepted: 11 April 2012 / Published: 19 April 2012
Show/Hide Abstract | Cited by 3 | PDF Full-text (261 KB) | HTML Full-text | XML Full-text
(This article belongs to the Special Issue Phage Display)
p. 4727-4794
by ,  and
Int. J. Mol. Sci. 2012, 13(4), 4727-4794; doi:10.3390/ijms13044727
Received: 1 March 2012; in revised form: 26 March 2012 / Accepted: 30 March 2012 / Published: 13 April 2012
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(This article belongs to the Special Issue Phage Display)
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p. 2618-2635
by , , , , ,  and
Int. J. Mol. Sci. 2012, 13(3), 2618-2635; doi:10.3390/ijms13032618
Received: 29 January 2012; in revised form: 14 February 2012 / Accepted: 20 February 2012 / Published: 27 February 2012
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Last update: 26 February 2014

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert