Special Issue "Phage Display"
Deadline for manuscript submissions: closed (29 February 2012)
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
Dr. Martina Jones
Australian Institute for Bioengineering and Nanotechnology (AIBN), The University of Queensland, Brisbane Qld 4072, Australia
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 .
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 , 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
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
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed Open Access monthly journal published by MDPI.
- phage display
- subtractive selection
- whole cell panning
Article: Phage Display Approaches for the Isolation of Monoclonal Antibodies Against Dengue Virus Envelope Domain III from Human and Mouse Derived Libraries
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| Download PDF Full-text (629 KB) | Download XML Full-text
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| Download PDF Full-text (848 KB) | Download XML Full-text
Article: Generation and Characterization of a Novel Recombinant Antibody Against 15-Ketocholestane Isolated by Phage-Display
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| Download PDF Full-text (261 KB) | Download XML Full-text
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| Download PDF Full-text (215 KB) | Download XML Full-text
Review: Phage Displayed Peptides/Antibodies Recognizing Growth Factors and Their Tyrosine Kinase Receptors as Tools for Anti-Cancer Therapeutics
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| Download PDF Full-text (390 KB) | Download XML Full-text
Article: Identification of Late Embryogenesis Abundant (LEA) Protein Putative Interactors Using Phage Display
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| Download PDF Full-text (1234 KB) | Download XML Full-text |
Article: Generation of a Highly Reactive Chicken-Derived Single-Chain Variable Fragment against Fusarium verticillioides by Phage Display
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| Download PDF Full-text (529 KB) | Download XML Full-text
Last update: 18 May 2011