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Recombinant antibody technology: from plain phage display panning to complex combined approaches

Recombinant antibody technology is considered a fast and inexpensive method to recover new binders. It is also acknowledged that it enables to expand the repertoire represented by natural binders issued from immunization.  This improvement can be realized by forcing the system at different levels: i) design of the library in terms of dimension and structural characteristics; ii) panning and screening conditions for selecting antibodies with specific biophysical features; iii) in vitro and in silico maturation procedures paired to molecular engineering for optimizing the binders in the function of their final applications.

In many cases, the advancement in this research field has been the consequence of applying in creative form combinations of methodologies which initially developed separately. Examples are the alternate use of phage and yeast/ribosomal/bacterial display, the introduction of rational mutagenesis based on computational modeling to optimize the initial hits recovered by conventional panning, the use of automated systems that allow the analysis of huge amounts of biochemical (from ELISA, flow-cytometry, affinity measurement) and NGS data. These approaches simplified the isolation of antibodies for difficult targets (membrane proteins, toxic and non-immunogenic targets), specific applications (structural chaperones, allosteric inhibitors, detectors of structural conformation), and better biophysical characteristics (higher stability and yields, stronger and more selective binding, lower immunogenicity).

This special issue presents significant examples of some of these achievements and therefore should inspire to further challenge the potential of recombinant antibody technology.

Edited by Ario de Marco, University of Nova Gorica, Slovenia. If you are interested in contributing to the Special Issue, please contact the Editor:

  1. The bacteriocin nisin is naturally produced by Lactococcus lactis as an inactive prepeptide that is modified posttranslationally resulting in five (methyl-)lanthionine rings characteristic for class Ia bacterioci...

    Authors: Dominik Weixler, Max Berghoff, Kirill V. Ovchinnikov, Sebastian Reich, Oliver Goldbeck, Gerd M. Seibold, Christoph Wittmann, Nadav S. Bar, Bernhard J. Eikmanns, Dzung B. Diep and Christian U. Riedel
    Citation: Microbial Cell Factories 2022 21:11

    The Correction to this article has been published in Microbial Cell Factories 2022 21:24

  2. Pioneered exactly 20 years ago, yeast surface display (YSD) continues to take a major role in protein engineering among the high-throughput display methodologies that have been developed to date. The classical...

    Authors: Doreen K├Ânning and Harald Kolmar
    Citation: Microbial Cell Factories 2018 17:32
  3. The thorough understanding of the physiological and pathological processes mediated by extracellular vesicles (EVs) is challenged by purification methods which are cumbersome, not reproducible, or insufficient...

    Authors: Milica Popovic, Elisa Mazzega, Barbara Toffoletto and Ario de Marco
    Citation: Microbial Cell Factories 2018 17:6
  4. Yeast surface display (YSD) has proven to be a versatile platform technology for antibody discovery. However, the construction of antibody Fab libraries typically is a tedious three-step process that involves ...

    Authors: Simon Rosowski, Stefan Becker, Lars Toleikis, Bernhard Valldorf, Julius Grzeschik, Deniz Demir, Iris Willenb├╝cher, Ramona Gaa, Harald Kolmar, Stefan Zielonka and Simon Krah
    Citation: Microbial Cell Factories 2018 17:3
  5. A key advantage of recombinant antibody technology is the ability to optimize and tailor reagents. Single domain antibodies (sdAbs), the recombinantly produced variable domains derived from camelid and shark h...

    Authors: Jinny L. Liu, Lisa C. Shriver-Lake, George P. Anderson, Dan Zabetakis and Ellen R. Goldman
    Citation: Microbial Cell Factories 2017 16:223