Plant Viral Epitope Display Systems for Vaccine Development

2011 ◽  
pp. 47-59 ◽  
Author(s):  
Denis Leclerc
Keyword(s):  
Vaccine Development ◽  
Viral Epitope ◽  
Display Systems

scholarly journals Covalent protein display on Hepatitis B core-like particles in plants through the in vivo use of the SpyTag/SpyCatcher system

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Hadrien Peyret ◽  
Daniel Ponndorf ◽  
Yulia Meshcheriakova ◽  
Jake Richardson ◽  
George P. Lomonossoff
Keyword(s):  
Hepatitis B ◽  
Cost Saving ◽  
Capsid Protein ◽  
Recombinant Proteins ◽  
Nicotiana Benthamiana ◽  
Vaccine Development ◽  
Binding Partner ◽  
Gfp Fluorescence ◽  
Display Systems

Abstract Virus-like particles (VLPs) can be used as nano-carriers and antigen-display systems in vaccine development and therapeutic applications. Conjugation of peptides or whole proteins to VLPs can be achieved using different methods such as the SpyTag/SpyCatcher system. Here we investigate the conjugation of tandem Hepatitis B core (tHBcAg) VLPs and the model antigen GFP in vivo in Nicotiana benthamiana. We show that tHBcAg VLPs could be successfully conjugated with GFP in the cytosol and ER without altering VLP formation or GFP fluorescence. Conjugation in the cytosol was more efficient when SpyCatcher was displayed on tHBcAg VLPs instead of being fused to GFP. This effect was even more obvious in the ER, showing that it is optimal to display SpyCatcher on the tHBcAg VLPs and SpyTag on the binding partner. To test transferability of the GFP results to other antigens, we successfully conjugated tHBcAg VLPs to the HIV capsid protein P24 in the cytosol. This work presents an efficient strategy which can lead to time and cost saving post-translational, covalent conjugation of recombinant proteins in plants.

scholarly journals Crystal structure of the classical MHC-I molecule: insights into the MHC-I system in antiviral diseases in dogs

2021 ◽  
Author(s):  
Yujiao Sun ◽  
Lizhen Ma ◽  
Shen Li ◽  
Yawen Wang ◽  
Ruiqi Xiao ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Vaccine Development ◽  
3D Structure ◽  
Binding Motif ◽  
Mhc I ◽  
Viral Epitope ◽  
First Category ◽  
Viral Vaccine ◽  
Epitope Vaccines

AbstractOnly one classical MHC-I locus (aka DLA-88) evolved in dogs, and thus far, a total of 76 DLA-88 alleles can be divided into two categories. The first category consists of 60 alleles, and the second category consists of 16 alleles. The main difference between the two categories is the insertion of an amino acid in the α2 region of DLA-88 alleles. To elucidate the structure of the first category, in this study, the crystal structure of pDLA-88*001:01 was determined for the first time. The 3D structure and topological characteristics of the ABG of pDLA-88*001:01 with a CDV peptide were analyzed. The viral presentation profile and the binding motif of viruses presented by pDLA-88*001:01 were determined. Most importantly, there were no amino acid insertions in the α2 region of the first category, which changed the conformation of the D pocket and the docking of the TCR. The results suggest obvious differences between the two categories. Because of the variation in the α2 region, pDLA-88*001:01 showed distinctive features in the two categories. Due to the peptide-binding motif of pDLA-88*001:01, more than 320 high-affinity viral peptides were predicted from dog H7N9, CPV, CMV, CMV, and CDV strains. The results reveal that there are two kinds of structural MHC-I systems in dogs that are responsible for CTL immunity against viral diseases. The results provide knowledge for designing viral epitope vaccines in canines.ImportanceDLA plays an important role in the acquired immunity of organism. In previous study, the pMHC-I structure of dog was analyzed with DLA-88 self-peptide. In this study, we screened several viral peptides which can bind to DLA-88 and resolved the structure of the DLA-88 complex binding the CDV peptide. This study enriches the study of canine MHC-I molecular-presenting polypeptide-activated TCR, which is of great significance for the study of canine cellular immunity and anti-viral vaccine development.

scholarly journals Codon Usage and Adenovirus Fitness: Implications for Vaccine Development

2021 ◽  
Vol 12 ◽  
Author(s):  
Judit Giménez-Roig ◽  
Estela Núñez-Manchón ◽  
Ramon Alemany ◽  
Eneko Villanueva ◽  
Cristina Fillat
Keyword(s):  
Immune Response ◽  
Codon Usage ◽  
Viral Vectors ◽  
Vaccine Development ◽  
Health Hazard ◽  
Recombinant Vaccines ◽  
Viral Epitope ◽  
Naturally Occurring ◽  
Cellular Immune ◽  
Viral Attenuation

Vaccination is the most effective method to date to prevent viral diseases. It intends to mimic a naturally occurring infection while avoiding the disease, exposing our bodies to viral antigens to trigger an immune response that will protect us from future infections. Among different strategies for vaccine development, recombinant vaccines are one of the most efficient ones. Recombinant vaccines use safe viral vectors as vehicles and incorporate a transgenic antigen of the pathogen against which we intend to generate an immune response. These vaccines can be based on replication-deficient viruses or replication-competent viruses. While the most effective strategy involves replication-competent viruses, they must be attenuated to prevent any health hazard while guaranteeing a strong humoral and cellular immune response. Several attenuation strategies for adenoviral-based vaccine development have been contemplated over time. In this paper, we will review them and discuss novel approaches based on the principle that protein synthesis from individual genes can be modulated by codon usage bias manipulation. We will summarize vaccine approaches that consider recoding of viral proteins to produce adenoviral attenuation and recoding of the transgene antigens for both viral attenuation and efficient viral epitope expression.

scholarly journals Cryo-EM Studies of Virus-Antibody Immune Complexes

2020 ◽  
Vol 35 (1) ◽  
pp. 1-13
Author(s):  
Na Li ◽  
Zhiqiang Li ◽  
Yan Fu ◽  
Sheng Cao
Keyword(s):  
Immune Complexes ◽  
Molecular Mechanisms ◽  
Viral Infections ◽  
Vaccine Development ◽  
Diagnostic Tools ◽  
Virus Antibody ◽  
X Ray Crystallography ◽  
Road Map ◽  
Therapeutic Drugs ◽  
Viral Epitope

AbstractAntibodies play critical roles in neutralizing viral infections and are increasingly used as therapeutic drugs and diagnostic tools. Structural studies on virus-antibody immune complexes are important for better understanding the molecular mechanisms of antibody-mediated neutralization and also provide valuable information for structure-based vaccine design. Cryo-electron microscopy (cryo-EM) has recently matured as a powerful structural technique for studying bio-macromolecular complexes. When combined with X-ray crystallography, cryo-EM provides a routine approach for structurally characterizing the immune complexes formed between icosahedral viruses and their antibodies. In this review, recent advances in the structural understanding of virus-antibody interactions are outlined for whole virions with icosahedral T = pseudo 3 (picornaviruses) and T = 3 (flaviviruses) architectures, focusing on the dynamic nature of viral shells in different functional states. Glycoprotein complexes from pleomorphic enveloped viruses are also discussed as immune complex antigens. Improving our understanding of viral epitope structures using virus-based platforms would provide a fundamental road map for future vaccine development.

Aircraft Display Systems

2004 ◽  
Author(s):  
Malcolm Jukes
Keyword(s):  
Display Systems

Development of test/mission support data processing and display systems

1992 ◽  
Author(s):  
ARCHIE MOORE ◽  
DONALD RHEA ◽  
ROBERT DOWNING
Keyword(s):  
Data Processing ◽  
Display Systems

Advances and Challenges in HCV Vaccine Development

2020 ◽  
Author(s):  
Ivana Lazarevic
Keyword(s):  
Vaccine Development
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