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Antibodies
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Nanobodies
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Nanobodies

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

Deadline for manuscript submissions: closed (31 May 2015) | Viewed by 27938

Special Issue Editors

Prof. Dr. Friedrich Koch-Nolte

E-Mail Website
Guest Editor
Institute of Immunology, University Medical Center Hamburg-Eppendorf, Martinistr. 52, D-20246 Hamburg, Germany
Interests: lymphocyte membrane proteins; antibody engineering; genetic immunization; single domain antibodies; posttranslational modifications; ADP-ribosylation; glycosylation; lipid anchors
Dr. William Leenders

E-Mail Website
Guest Editor
Department of Pathology, Radboud University Medical Center, PO Box 9101, 6500 HB Nijmegen, The Netherlands
Interests: cameloid antibody discovery; antibody-mediated targeting; nanobody-conjugation methodologies; (molecular) imaging; personalized medicine; nanomedicine.

Special Issue Information

Dear Colleagues,

The discovery of heavy chain-only antibodies in sera from camelids, nurse sharks and some other exotic species has initiated large research efforts in the field of antibody engineering. The antigen-binding fragments of these antibodies can be easily cloned and expressed as small single domain antibodies (called Nanobodies® by Ablynx [1]) with binding properties similar to that of the originating antibody. The advantages of high water solubility, thermostability, favorable pharmacokinetics, low immunogenicity in humans, ease of library generation for selection purposes and possibilities for relatively cheap expression in E. coli or yeast make single domain antibodies highly interesting emerging alternatives to conventional antibodies.

This special issue on Nanobodies will consider contributions in the field of nanobody discovery, expression, modification and conjugation technologies. In particular, we invite contributions that deal with in vivo applications of therapeutic and/or diagnostic nanobodies for disease.

Dr. William Leenders
Prof. Dr. Friedrich Koch-Nolte
Guest Editors

[1] Gibbs, W.W. Nanobodies. Scientific American Magazine. August 2005. http://www.scientificamerican.com/article/nanobodies/.

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

  • camelid antibodies
  • single domain antibodies
  • expression systems
  • library screening
  • antibody conjugation
  • nanomedicine
  • targeting

Published Papers (2 papers)

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Article
Pre-Clinical Intravenous Serum Pharmacokinetics of Albumin Binding and Non-Half-Life Extended Nanobodies®
by Sven Hoefman, Ingrid Ottevaere, Judith Baumeister and Maria Laura Sargentini-Maier
Antibodies 2015, 4(3), 141-156; https://0-doi-org.brum.beds.ac.uk/10.3390/antib4030141 - 10 Jul 2015
Cited by 73 | Viewed by 16103
Abstract
Nanobodies are antigen-binding, single variable domain proteins derived from naturally-occurring, heavy chain only antibodies. They are highly soluble, stable, and can be linked to build multi-specific formats. Several Nanobodies are currently in clinical development in different therapeutic areas, for both chronic and acute [...] Read more.
Nanobodies are antigen-binding, single variable domain proteins derived from naturally-occurring, heavy chain only antibodies. They are highly soluble, stable, and can be linked to build multi-specific formats. Several Nanobodies are currently in clinical development in different therapeutic areas, for both chronic and acute applications. For the former, prolonged exposure is achieved by half-life extending moieties that target endogenous albumin, while for the latter, non-half-life extended constructs are preferable. To demonstrate the general pharmacokinetic behavior of both formats, serum levels of seven intravenously administered Nanobodies were analyzed in cynomolgus monkeys, mice or rabbits. In monkeys, the total clearance of a monomeric irrelevant Nanobody was rapid (2.0 mL/(min*kg)) and approximated the species glomerular filtration rate, indirectly suggesting that the Nanobody was mainly eliminated via the kidneys. When linked to an anti-albumin Nanobody, a 376-fold decrease in clearance was observed, resulting in a terminal half-life of 4.9 days, corresponding to the expected species albumin half-life. Similar conclusions were drawn for (non-) half-life extended mono-, bi- and trimeric Nanobodies in mice or rabbits, suggesting that these kinetic principles apply across species. Applying this knowledge to species translation and study design is crucial for successful pre-clinical development of novel therapeutic Nanobody candidates. Full article
(This article belongs to the Special Issue Nanobodies)
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Review

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Review
VNARs: An Ancient and Unique Repertoire of Molecules That Deliver Small, Soluble, Stable and High Affinity Binders of Proteins
by Caroline Barelle and Andy Porter
Antibodies 2015, 4(3), 240-258; https://0-doi-org.brum.beds.ac.uk/10.3390/antib4030240 - 01 Sep 2015
Cited by 32 | Viewed by 11297
Abstract
At 420 million years, the variable domain of New Antigen Receptors or VNARs are undoubtedly the oldest (and smallest) antigen binding single domains identified in the vertebrate kingdom. Their role as an integral part of the adaptive immune system of sharks has been [...] Read more.
At 420 million years, the variable domain of New Antigen Receptors or VNARs are undoubtedly the oldest (and smallest) antigen binding single domains identified in the vertebrate kingdom. Their role as an integral part of the adaptive immune system of sharks has been well established and has served to provide a greater understanding of the evolution of humoral immunity; their cellular components and processes as well as the underlying genetic organization and molecular control mechanisms. Intriguingly, unlike the variable domain of the camelid heavy chain antibodies or VHH, VNARs do not conform to all of the characteristic properties of classical antibodies with an ancestral origin that clearly distinguishes them from true immunoglobulin antibodies. However, this uniqueness of their origin only adds to their potential as next generation therapeutic biologics with their structural and functional attributes and commercial freedom all enhancing their profile and current success. In fact their small size, remarkable stability, molecular flexibility and solubility, together with their high affinity and selectivity for target, all reinforce the potential of these domains as drug candidates. The purpose of this review is to provide an overview of the existing basic biology of these unique domains, to highlight the drug-like properties of VNARs and describe current progress in their journey towards the clinic. Full article
(This article belongs to the Special Issue Nanobodies)
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