Virus-like particles in picornavirus vaccine development

Dong, Hu; Guo, Huichen; Sun, Shiqi

doi:10.1007/s00253-014-5639-1

Cited by 16 publications

(10 citation statements)

References 53 publications

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“…Virus-like particles (VLPs) are multi-protein structures that mimic the organization and conformation of authentic native viruses but lack the viral genome [53]. They are safe and effective tolls that are widely used in studying the pathogenic mechanisms of virus infection, efficacy evaluation of drugs and vaccines, and drug delivery [54]. For example, the corresponding VLPs have been already used to determine the neutralizing antibodies induced by SARS-CoV and H5N1 vaccines [55,56].…”

Section: Means Of Efficacy Evaluationmentioning

confidence: 99%

Progress and Prospects on Vaccine Development against SARS-CoV-2

et al. 2020

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In December 2019, the outbreak of pneumonia caused by a novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has led to a serious pandemic in China and other countries worldwide. So far, more than 460,000 confirmed cases were diagnosed in nearly 190 countries, causing globally over 20,000 deaths. Currently, the epidemic is still spreading and there is no effective means to prevent the infection. Vaccines are proved to be the most effective and economical means to prevent and control infectious diseases. Several countries, companies, and institutions announced their programs and progress on vaccine development against the virus. While most of the vaccines are under design and preparation, there are some that have entered efficacy evaluation in animals and initial clinical trials. This review mainly focused on the progress and our prospects on field of vaccine development against SARS-CoV-2.

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Section: Means Of Efficacy Evaluationmentioning

confidence: 99%

Progress and Prospects on Vaccine Development against SARS-CoV-2

et al. 2020

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“…47,48 VLPs is a potentially safe subunit vaccine that can induce immune responses similar to those prompted by natural viral infection. 49 VLPs present repetitive high-density displays of epitopes and exhibit excellent adjuvant properties capable of inducing strong immune responses. 50 It has been found that VLPs are more stable and considerably more immunogenic than purified protein antigens.…”

Section: Recombinant Protein Subunit Vaccinesmentioning

confidence: 99%

Recent advances in the production of recombinant subunit vaccines inPichia pastoris

2016

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Recombinant protein subunit vaccines are formulated using defined protein antigens that can be produced in heterologous expression systems. The methylotrophic yeast Pichia pastoris has become an important host system for the production of recombinant subunit vaccines. Although many basic elements of P. pastoris expression system are now well developed, there is still room for further optimization of protein production. Codon bias, gene dosage, endoplasmic reticulum protein folding and culture condition are important considerations for improved production of recombinant vaccine antigens. Here we comment on current advances in the application of P. pastoris for the synthesis of recombinant subunit vaccines.

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“…Novel vaccines based on recombinant FMDV empty capsids (Lewis et al, 1991;Abrams et al, 1995;Cao et al, 2009;Li et al, 2011;Gullberg et al, 2013;Guo et al, 2013;Porta et al, 2013aPorta et al, , 2013bDong et al, 2014) are also being investigated to avoid the risks of virus escape or deficient inactivation during vaccine production, while still preserving the full immunogenicity and antigenic spectrum of current vaccines. Such vaccines would also allow differentiation between infected and vaccinated animals (DIVA assays).…”

Section: Introductionmentioning

confidence: 99%

Identification of the Structural Basis of Thermal Lability of a Virus Provides a Rationale for Improved Vaccines

et al. 2014

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Virus stability and dynamics play critical roles during infection. Some viruses, including foot-and-mouth disease virus (FMDV), are surprisingly prone to thermal dissociation outside the cell. The structural bases and functional implications of this distinctive trait were essentially unknown. This study (1) uncovers the structural determinants of FMDV thermolability, (2) investigates the relationship between virus thermolability and infectivity, and (3) provides a structure-based rationale for engineering thermostable virus particles to develop improved vaccines and nanocontainers. The results reveal that negatively charged residues close to protein-protein interfaces exert electrostatic repulsions between capsid subunits and mediate the sensitivity of the virion to thermal dissociation, even at neutral pH. Based on these results, a series of fully infectious virions of increased thermostability were engineered by individually removing different carboxylates involved in intersubunit repulsions. The implications for virus biology and the design of thermostable vaccines are discussed.

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Virus-like particles in picornavirus vaccine development

Cited by 16 publications

References 53 publications

Progress and Prospects on Vaccine Development against SARS-CoV-2

Progress and Prospects on Vaccine Development against SARS-CoV-2

Recent advances in the production of recombinant subunit vaccines inPichia pastoris

Identification of the Structural Basis of Thermal Lability of a Virus Provides a Rationale for Improved Vaccines

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