Special Issue "Advances in Antibody Design and Antigenic Peptide Targeting"
Deadline for manuscript submissions: 15 February 2019
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
Manuscript Submission Information
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- epitope mapping
- therapeutic antibodies
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.
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.