Special Issue "Nanobody"

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

Deadline for manuscript submissions: 30 November 2018

Special Issue Editors

Guest Editor
Prof. Ulrich Rothbauer

Pharmaceutical Biotechnology, Eberhard Karls University Tuebingen, Reutlingen, Germany
Website | E-Mail
Guest Editor
Dr. Patrick Chames

Aix Marseille University, CNRS, INSERM, Institute Paoli-Calmettes, CRCM, F-13009, Marseille, France
Website | E-Mail

Special Issue Information

Dear Colleagues,

Since their first description 25 years ago, single-domain antibody fragments, derived from heavy-chain-only antibodies of camelids, so-called nanobodies, have emerged as attractive alternatives to conventional antibodies for multiple applications in biomedical research. Compared to other small antibody fragments like Fab or scFv, nanobodies have numerous advantages. First, only one domain has to be cloned and expressed to generate a fully functional binding molecule. Secondly, nanobodies are highly soluble and stable, can be easily genetically or chemically modified, and produced in various cells and/or organisms. Microbial expression systems enable the production of purified nanobodies in the mg–g range per liter of culture, thereby offering an unlimited supply of consistent binding molecules.

To date nanobodies have become outstanding tools for in vitro and in vivo imaging, as well as structural and proteome analysis. As genetically encoded intrabodies, they open new possibilities for visualization or functional studies on proteins in living cells. The recently described advances in identification of antigen-specific nanobodies from synthetic gene libraries now makes nanobody-based approaches broadly available to many researches in the field.

This Special Issue is aimed to provide an up-to-date overview of the rising field of nanobodies including generation and functionalization of nanobodies as well as their application for immunoassays, proteomics, protein crystallization and in vitro and in vivo imaging.

Prof. Ulrich Rothbauer
Dr. Patrick Chames
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 papers will be 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 350 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

  • Nanobodies
  • Nanobody Display Technologies
  • Functionalization of nanobodies
  • Unique application of nanobodies
  • Live cell imaging
  • Super resolution microscopy
  • In vivo imaging
  • Protein crystallization chaperones

Published Papers (2 papers)

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Research

Open AccessArticle Isolation and Characterization of Nanobodies against a Zinc-Transporting P-Type ATPase
Antibodies 2018, 7(4), 39; https://doi.org/10.3390/antib7040039
Received: 17 October 2018 / Revised: 31 October 2018 / Accepted: 4 November 2018 / Published: 7 November 2018
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Abstract
P-type ATPases form a large and ubiquitous superfamily of ion and lipid transporters that use ATP (adenosine triphosphate) to carry out their function. The IB subclass (PIB-ATPases) allows flux of heavy metals and are key players in metal detoxification, critical for
[...] Read more.
P-type ATPases form a large and ubiquitous superfamily of ion and lipid transporters that use ATP (adenosine triphosphate) to carry out their function. The IB subclass (PIB-ATPases) allows flux of heavy metals and are key players in metal detoxification, critical for human health, crops, and survival of pathogens. Nevertheless, PIB-ATPases remain poorly understood at a molecular level. In this study, nanobodies (Nbs) are selected against the zinc-transporting PIB-ATPase ZntA from Shigella sonnei (SsZntA), aiming at developing tools to assist the characterization of the structure and function of this class of transporters. We identify six different Nbs that bind detergent stabilized SsZntA. We further assess the effect of the Nbs on the catalytic function of SsZntA, and find that five nanobodies associate without affecting the function, while one nanobody significantly reduces the ATPase activity. This study paves the way for more refined mechanistical and structural studies of zinc-transporting PIB-ATPases. Full article
(This article belongs to the Special Issue Nanobody)
Figures

Figure 1

Open AccessFeature PaperArticle Genetic Fusion of an Anti-BclA Single-Domain Antibody with Beta Galactosidase
Antibodies 2018, 7(4), 36; https://doi.org/10.3390/antib7040036
Received: 12 September 2018 / Revised: 26 September 2018 / Accepted: 27 September 2018 / Published: 29 September 2018
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Abstract
The Bacillus collagen-like protein of anthracis (BclA), found in Bacillus anthracis spores, is an attractive target for immunoassays. Previously, using phage display we had selected llama-derived single-domain antibodies that bound to B. anthracis spore proteins including BclA. Single-domain antibodies (sdAbs), the recombinantly expressed
[...] Read more.
The Bacillus collagen-like protein of anthracis (BclA), found in Bacillus anthracis spores, is an attractive target for immunoassays. Previously, using phage display we had selected llama-derived single-domain antibodies that bound to B. anthracis spore proteins including BclA. Single-domain antibodies (sdAbs), the recombinantly expressed heavy domains from the unique heavy-chain-only antibodies found in camelids, provide stable and well-expressed binding elements with excellent affinity. In addition, sdAbs offer the important advantage that they can be tailored for specific applications through protein engineering. A fusion of a BclA targeting sdAb with the enzyme Beta galactosidase (β-gal) would enable highly sensitive immunoassays with no need for a secondary reagent. First, we evaluated five anti-BclA sdAbs, including four that had been previously identified but not characterized. Each was tested to determine its binding affinity, melting temperature, producibility, and ability to function as both capture and reporter in sandwich assays for BclA. The sdAb with the best combination of properties was constructed as a fusion with β-gal and shown to enable sensitive detection. This fusion has the potential to be incorporated into highly sensitive assays for the detection of anthrax spores. Full article
(This article belongs to the Special Issue Nanobody)
Figures

Figure 1

Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

1) Single-domain antibodies as versatile tools for CNS research

Kasandra Belanger; Umar Iqbal; Jamshid Tanha; Maria Moreno; Danica Stanimirovic

2) Title: Using nanobodies to study protein function in developing organisms

Shinya Matsuda, Gustavo Aguilar, Alessandra Vigano and Markus Affolter *;

* Biozentrum, University of Basel, Switzerland

3) Title: Crossing the barrier of life: a future for single domain antibody-mediated drug transport over the Blood-brain-barrier?

Peter Durand Skottrup; Research Bioanalysis, Global Research Technologies, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark

4) Title: Nanobodies for super resolution microscopy

Helge Ewers; Prof. for Membrane Biochemistry, Freie Universität Berlin, Germany

5) Title: Analysis of camelid single-domain antibody responses against linear peptide epitopes

Kevin Henry; National Research Council Canada

6) Title: Single-domain antibodies and their formatting to combat viral infections

Dorien De Vlieger 1,2, Iebe Rossey 1,2, Marlies Ballegeer 1,2, Bert Schepens 1,2, Xavier Saelens 1,2

1 VIB Medical Biotechnology Center, VIB, 9052 Ghent, Belgium

2 Department of Biomedical Molecular Biology, Ghent University, 9052 Ghent, Belgium

7) Title: Design of targeted fluorescent tracers for image-guided surgery: potential of nanobody-based tracers

Pieterjan Debie and Sophie Hernot; Laboratory for In vivo Cellular and Molecular Imaging (ICMI - BEFY/MIMA), Vrije Universiteit Brussel, Brussels, Belgium

8) Title: Isolation and characterization of nanobodies against a zinc-transporting P-type ATPase (SUBMITTED)

Elena Longhin, Christina Grønberg, Qiaoxia Hu, Kasper Røjkjær Andersen, Nick Stub Laursen, Pontus Gourdon *;


9) Title: Isolation of nanobodies specific for influenza B hemagglutinin and the use of yeast display to structurally characterise lineage specific binding

Walter Ramage 1, Tiziano Gaiotto 1, Christina Ball 1, Paul Risley 1, George Carnell 3, Nigel Temperton 3, Chung Cheung 2, Othmar Engelhardt 2, Simon E Hufton 1 ;

1 Biotherapeutics Division, 2 Division of Virology, National Institute for Biological Standards and Control, a centre of the Medicines and Healthcare Products Regulatory Agency, Blanche Lane, South Mimms, Potters Bar, Herts EN6 3QG, United Kingdom

3 Infectious Diseases and Allergy group School of Pharmacy, University of Kent, Kent, ME4 4TB, United Kingdom

10) Title: Selection and characterization of specific nanobodies for analytical purposes from a semisynthetic library

Udo Conrad, IPK Gatersleben, Corrensstrasse 3, D-06466 Seeland OT Gatersleben

11) Title: One fits all: Tag-specific nanobodies and their growing application in biomedical research

Bjoern Traenkle1 and Ulrich Rothbauer1,2;

1 Pharmaceutical Biotechnology, Eberhard Karls University Tuebingen, Germany

2 Natural and Medical Sciences Institute at the University of Tuebingen, Reutlingen, Germany

12) Nanobody Engineering: Toward Next Gen Immunotherapies and Immunoimaging

Timothée Chanier1 and Patrick Chames1;

1Aix Marseille Univ, CNRS, INSERM, Institut Paoli-Calmettes, CRCM, Marseille, France

13) The recombinant protein complexes based on anti-TNF nanobodies fused with the far-red fluorescent protein Katushka

Irina V Astrakhantseva's group

14) Selection of Single Domain Antibodies towards Western Equine Encephalitis Virus, WEEV

George P. Anderson

US Naval Research Laboratory, Center for Biomolecular Science and Engineering

 

 

 

 

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