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Special Issue "Advances in Antibody Design and Antigenic Peptide Targeting"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 15 February 2019

Special Issue Editors

Guest Editor
Prof. Gunnar Houen

Department of Autoimmunology and Biomarkers, Statens Serum Institut, Artillerivej 5, 2300, Copenhagen S, Denmark
Website | E-Mail
Phone: +4532683276
Co-Guest Editor
Dr. Nicole Hartwig Trier

Department of Autoimmunology and Biomarkers, Statens Serum Institut, Artillerivej 5, 2300, Copenhagen S, Denmark
Website | E-Mail

Special Issue Information

Dear Colleagues,

Peptides can be made synthetically in essentially unlimited amounts, with most post-translational modifications and with non-natural amino acid residues. This makes them valuable reagents for many purposes, e.g. T cell epitope mapping and (linear) B cell epitope mapping. However, they generally have very little defined structure unless they are heavily constrained by e.g. disulfide bridges, thus making them unsuitable as specific reagents for target recognition.

Antibodies are natural, large proteins with specific recognition properties and can undergo affinity maturation and class switching during immune responses (e.g., immunization) in vivo to achieve very high affinities and specific effector functions. Antibodies can be made in large amounts by recombinant technology and can be engineered in several ways to modify their properties, e.g., structure, immunogenicity and effector functions.

All antibodies recognize three-dimensional structures, but a distinction is usually made between epitopes containing residues far apart in the amino acid sequence and epitopes with residues close in the sequence. The latter are called linear epitopes and are mainly found in linker regions between protein domains, in non-structured parts of proteins and in N- and C-terminal sequences.

The use of synthetic peptides for production of antibodies (peptide antibodies) has been extremely rewarding in all areas of biology and biotechnology and continues to be of major importance. Peptide antibodies are particularly good at recognizing linear epitopes, post-translationally modified epitopes, and denatured proteins (e.g., Western immunoblotting). However, several goals remain to be achieved in relation to peptides and antibodies, including the design and synthesis of (constrained) peptides with specific recognition properties (peptibodies) and the use of peptides as therapeutic vaccines.

This issue of IJMS attempts to describe current knowledge about specially designed peptides and antibodies with a particular emphasis on sophisticated peptide antibodies.

Prof. Gunnar Houen
Dr. Nicole Trier
Guest Editors

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. International Journal of Molecular Sciences is an international peer-reviewed open access bimonthly 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.


  • antibodies
  • autoantibodies
  • diagnostics
  • epitope
  • epitope mapping
  • immunoassay
  • paratope
  • peptibodies
  • therapeutic antibodies

Published Papers (1 paper)

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Open AccessArticle Optimization of Sequence, Display, and Mode of Operation of IgG-Binding Peptide Ligands to Develop Robust, High-Capacity Affinity Adsorbents That Afford High IgG Product Quality
Int. J. Mol. Sci. 2019, 20(1), 161; https://doi.org/10.3390/ijms20010161
Received: 3 December 2018 / Revised: 20 December 2018 / Accepted: 26 December 2018 / Published: 4 January 2019
PDF Full-text (6761 KB) | HTML Full-text | XML Full-text
This work presents the use of peptide ligand HWRGWV and its cognate sequences to develop affinity adsorbents that compete with Protein A in terms of binding capacity and quality of the eluted product. First, the peptide ligand was conjugated to crosslinked agarose resins
[...] Read more.
This work presents the use of peptide ligand HWRGWV and its cognate sequences to develop affinity adsorbents that compete with Protein A in terms of binding capacity and quality of the eluted product. First, the peptide ligand was conjugated to crosslinked agarose resins (WorkBeads) at different densities and using different spacer arms. The optimization of ligand density and display resulted in values of static and dynamic binding capacity of 85 mg/mL and 65 mg/mL, respectively. A selected peptide-WorkBeads adsorbent was utilized for purifying Mabs from Chinese Hamster Ovary (CHO) cell culture supernatants. The peptide-WorkBeads adsorbent was found able to withstand sanitization with strong alkaline solutions (0.5 M NaOH). The purity of the eluted product was consistently higher than 95%, with logarithmic removal value (LRV) of 1.5 for host cell proteins (HCPs) and 4.0 for DNA. HCP clearance was significantly improved by adding a post-load washing step with either 0.1 M Tris HCl pH 9 or 1 M NaCl. The cognate peptide of HWRGWV, constructed by replacing arginine (R) with citrulline, further increased the HCP LRV to 2.15. The peptide-based adsorbent also showed a remarkable performance in terms of removal of Mab aggregates; unlike Protein A, in fact, HWRGWV was found to bind only monomeric IgG. Collectively, these results demonstrate the potential of peptide-based adsorbents as alternative to Protein A for the purification of therapeutic antibodies. Full article
(This article belongs to the Special Issue Advances in Antibody Design and Antigenic Peptide Targeting)

Graphical abstract

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.

Title: Advances in Antigenic Peptide Targeting in the Design of Vaccines against Viruses Causing Hand, Foot and Mouth Disease (HFMD)
Authors: Mohd Ishtiaq Anasir1, Pinn Tsin Isabel Yee1 and Chit Laa Poh1, *
1 Centre for Virus and Vaccine Research, School of Science and Technology, Sunway University, Bandar Sunway, Kuala Lumpur, Selangor 47500, Malaysia
Abstract: The hand, foot, and mouth disease (HFMD) commonly produces herpangina but fatal neurological complications have been observed in children. Enterovirus 71 (EV-A71) and Coxsackievirus CV-A16 are the predominant viruses causing HFMD worldwide. With rising concern about HFMD outbreaks, there is a need for an effective vaccine against EV-A71 and CV-A16. Although an inactivated vaccine (IV) has been developed against EV-A71 in China, the inability of the IV to confer protection against CVA-16 infection necessitates the exploration of other vaccine platforms. A diphtheria toxoid-conjugated synthetic peptide comprising the EV-A71 SP70 neutralizing epitope was able to confer 80% passive protection in mice upon lethal challenge, and elicited cross protective neutralizing antibodies (1:32) against EV-A71 sub-genotypes B2, B5, C2 and C4. Subsequently, another recombinant sub-unit vaccine was designed containing multiple tandem linear neutralizing epitopes (mTLNE) by sequential linking VP1-SP55, VP1-SP70 and VP2-SP28 with a Gly-Ser linker. After immunization, the passive transfer of anti-mTLNE sera was able to confer 100% protection in neonatal mice against lethal EV-A71 challenge (10 LD50). This shows that advances in antigenic peptide targeting can facilitate the development of novel peptide based vaccine against EV-A71. As both EV-A71 and CVA-16 are major pathogens causing HFMD, an ideal vaccine should be bivalent against both. Chimeric EV-A71 virus like-particles (ChiEV-A71 VLPs) were produced with the EV-A71 SP70 epitope being replaced with the CV-A16 SP70 epitope. The ChiEV-A71 VLPs were able to elicit neutralizing antibodies against both EV-A71 and CV-A16. The passive immunization with anti-ChiEV-A71 VLP sera also conferred full protection against lethal challenge against both EV-A71 and CV-A16 infections in mice. Overall, the findings discussed in this review highlight the importance of antigenic peptide targeting as an indispensable tool to develop novel vaccines.
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
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