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Antibodies
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Antibody Phage Display
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Antibody Phage Display

A special issue of Antibodies (ISSN 2073-4468).

Deadline for manuscript submissions: closed (1 May 2019) | Viewed by 42524

Special Issue Editor

Dr. Jamshid Tanha

E-Mail Website
Guest Editor
Human Health Therapeutics Portfolio, National Research Council Canada, 100 Sussex Drive, Ottawa, ON K1A 0R6, Canada
Interests: single domain antibody; single domain antibody stability; antibody phage and ribosome display technologies; antibody affinity maturation; antibody structure; recombinant antibody/intrabody; synthetic and natural antibody libraries; microbiology

Special Issue Information

Dear Colleagues,

Despite the existence of several conceptually similar antibody discovery platforms, the antibody phage display library platform remains the most popular of all, mainly due to its robust nature, simplicity of use, and highly versatile nature with respect to the selection conditions. These factors, combined with the control over the direction of the selection the platform offers, allows for the efficient isolation of antibodies with the desired affinity, specificity, stability and function. Complementing the antibody phage display library platform with automation, next-generation sequencing or other antibody display platforms has further enhanced its capacity. Many of the antibody therapeutics approved or in development are obtained from phage display libraries including some blockbusters such as Humira and Lucentis.


This Special Issue will provide recent advances in aspects of antibody phage display libraries including antigen design, presentation and expression, immunization strategies and library design, construction, selection and screening that relate to the development of therapeutic and diagnostic antibodies.

Dr. Jamshid Tanha
Guest Editor

Manuscript Submission Information

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. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short 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 thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Antibodies is an international peer-reviewed open access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Antibody phage display libraries
  • Therapeutic and diagnostic antibodies
  • Antigen design, presentation and expression
  • Immunization strategies
  • Library design, construction, selection and screening

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Published Papers (3 papers)

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Research

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16 pages, 2110 KiB  
Article
Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning
by Yoonji Kim, Hansaem Lee, Keunwan Park, Sora Park, Ju-Hyeon Lim, Min Kyung So, Hye-Min Woo, Hyemin Ko, Jeong-Min Lee, Sun Hee Lim, Byoung Joon Ko, Yeon-Su Park, So-Young Choi, Du Hyun Song, Joo-Yeon Lee, Sung Soon Kim and Dae Young Kim
Antibodies 2019, 8(3), 42; https://doi.org/10.3390/antib8030042 - 31 Jul 2019
Cited by 19 | Viewed by 8638
Abstract
Since its first report in the Middle East in 2012, the Middle East respiratory syndrome-coronavirus (MERS-CoV) has become a global concern due to the high morbidity and mortality of individuals infected with the virus. Although the majority of MERS-CoV cases have been reported [...] Read more.
Since its first report in the Middle East in 2012, the Middle East respiratory syndrome-coronavirus (MERS-CoV) has become a global concern due to the high morbidity and mortality of individuals infected with the virus. Although the majority of MERS-CoV cases have been reported in Saudi Arabia, the overall risk in areas outside the Middle East remains significant as inside Saudi Arabia. Additional pandemics of MERS-CoV are expected, and thus novel tools and reagents for therapy and diagnosis are urgently needed. Here, we used phage display to develop novel monoclonal antibodies (mAbs) that target MERS-CoV. A human Fab phage display library was panned against the S2 subunit of the MERS-CoV spike protein (MERS-S2P), yielding three unique Fabs (S2A3, S2A6, and S2D5). The Fabs had moderate apparent affinities (Half maximal effective concentration (EC50 = 123–421 nM) for MERS-S2P, showed no cross-reactivity to spike proteins from other CoVs, and were non-aggregating and thermostable (Tm = 61.5–80.4 °C). Reformatting the Fabs into IgGs (Immunoglobulin Gs) greatly increased their apparent affinities (KD = 0.17–1.2 nM), presumably due to the effects of avidity. These apparent affinities were notably higher than that of a previously reported anti-MERS-CoV S2 reference mAb (KD = 8.7 nM). Furthermore, two of the three mAbs (S2A3 and S2D5) bound only MERS-CoV (Erasmus Medical Center (EMC)) and not other CoVs, reflecting their high binding specificity. However, the mAbs lacked MERS-CoV neutralizing activity. Given their high affinity, specificity, and desirable stabilities, we anticipate that these anti-MERS-CoV mAbs would be suitable reagents for developing antibody-based diagnostics in laboratory or hospital settings for point-of-care testing. Full article
(This article belongs to the Special Issue Antibody Phage Display)
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20 pages, 4551 KiB  
Article
Canine CD117-Specific Antibodies with Diverse Binding Properties Isolated from a Phage Display Library Using Cell-Based Biopanning
by Mohamed A. Alfaleh, Neetika Arora, Michael Yeh, Christopher J. de Bakker, Christopher B. Howard, Philip Macpherson, Rachel E. Allavena, Xiaoli Chen, Linda Harkness, Stephen M. Mahler and Martina L. Jones
Antibodies 2019, 8(1), 15; https://doi.org/10.3390/antib8010015 - 12 Feb 2019
Cited by 3 | Viewed by 8853
Abstract
CD117 (c-Kit) is a tyrosine kinase receptor that is overexpressed in multiple dog tumors. There is 100% homology between the juxtamembrane domain of human and canine CD117, and many cancer-causing mutations occur in this region in both species. Thus, CD117 is an important [...] Read more.
CD117 (c-Kit) is a tyrosine kinase receptor that is overexpressed in multiple dog tumors. There is 100% homology between the juxtamembrane domain of human and canine CD117, and many cancer-causing mutations occur in this region in both species. Thus, CD117 is an important target for cancer treatment in dogs and for comparative oncology studies. Currently, there is no monoclonal antibody (mAb) specifically designed to target the exposed region of canine CD117, although there exist some with species cross-reactivity. We panned a naïve phage display library to isolate antibodies against recombinant CD117 on whole cells. Several mAbs were isolated and were shown to bind recombinant canine CD117 at low- to sub-nanomolar affinity. Additionally, binding to native canine CD117 was confirmed by immunohistochemistry and by flow cytometry. Competitive binding assays also identified mAbs that competed with the CD117 receptor-specific ligand, the stem cell factor (SCF). These results show the ability of our cell-based biopanning strategy to isolate a panel of antibodies that have varied characteristics when used in different binding assays. These in vitro/ex vivo assessments suggest that some of the isolated mAbs might be promising candidates for targeting overexpressed CD117 in canine cancers for different useful applications. Full article
(This article belongs to the Special Issue Antibody Phage Display)
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Review

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21 pages, 1745 KiB  
Review
Phage Display Libraries for Antibody Therapeutic Discovery and Development
by Juan C. Almagro, Martha Pedraza-Escalona, Hugo Iván Arrieta and Sonia Mayra Pérez-Tapia
Antibodies 2019, 8(3), 44; https://doi.org/10.3390/antib8030044 - 23 Aug 2019
Cited by 106 | Viewed by 24182
Abstract
Phage display technology has played a key role in the remarkable progress of discovering and optimizing antibodies for diverse applications, particularly antibody-based drugs. This technology was initially developed by George Smith in the mid-1980s and applied by John McCafferty and Gregory Winter to [...] Read more.
Phage display technology has played a key role in the remarkable progress of discovering and optimizing antibodies for diverse applications, particularly antibody-based drugs. This technology was initially developed by George Smith in the mid-1980s and applied by John McCafferty and Gregory Winter to antibody engineering at the beginning of 1990s. Here, we compare nine phage display antibody libraries published in the last decade, which represent the state of the art in the discovery and development of therapeutic antibodies using phage display. We first discuss the quality of the libraries and the diverse types of antibody repertoires used as substrates to build the libraries, i.e., naïve, synthetic, and semisynthetic. Second, we review the performance of the libraries in terms of the number of positive clones per panning, hit rate, affinity, and developability of the selected antibodies. Finally, we highlight current opportunities and challenges pertaining to phage display platforms and related display technologies. Full article
(This article belongs to the Special Issue Antibody Phage Display)
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