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Review
. 2024 Jun 26:14:1406091.
doi: 10.3389/fcimb.2024.1406091. eCollection 2024.

Advances in virus-like particle-based SARS-CoV-2 vaccines

Xiaoting Hao #  1 , Feifei Yuan #  2 , Xuan Yao  3
Affiliations
Review

Advances in virus-like particle-based SARS-CoV-2 vaccines

Xiaoting Hao et al. Front Cell Infect Microbiol. .

Abstract

The Coronavirus Disease 2019 (COVID-19) pandemic, caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has incurred devastating human and economic losses. Vaccination remains the most effective approach for controlling the COVID-19 pandemic. Nonetheless, the sustained evolution of SARS-CoV-2 variants has provoked concerns among the scientific community regarding the development of next-generation COVID-19 vaccines. Among these, given their safety, immunogenicity, and flexibility to display varied and native epitopes, virus-like particle (VLP)-based vaccines represent one of the most promising next-generation vaccines. In this review, we summarize the advantages and characteristics of VLP platforms, strategies for antigen display, and current clinical trial progress of SARS-CoV-2 vaccines based on VLP platforms. Importantly, the experience and lessons learned from the development of SARS-CoV-2 VLP vaccines provide insights into the development of strategies based on VLP vaccines to prevent future coronavirus pandemics and other epidemics.

Keywords: COVID-19; SARS-CoV-2; immune response; receptor binding domain; spike protein; vaccines; virus-like particles.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
SARS-CoV-2 virion and the structure of its S protein. (A) A schematic diagram of SARS-CoV-2 virion. This figure was adapted from BioRender.com. (B) Structure of SARS-CoV-2 S protein. (left) The prefusion structure of the S protein with one RBD in the “up” conformation (PDB: 6VSB). (right) The post-fusion structure of the S protein (PDB: 6M3W). (C) Schematic domain structure of SARS-CoV-2 S protein. The S1 and S2 subunits are indicated, with the locations of furin cleavage sites. SP, signal peptide. NTD, N-terminal domain. RBD, receptor-binding domain. FP, fusion peptide. HR1 and HR2, heptad repeat 1 and 2. TM, transmembrane.
Figure 2
Figure 2
A range of different technologies for developing SARS-COV-2 vaccines. The figure was adapted from BioRender.com.
Figure 3
Figure 3
Structure of different VLPs. (A) Structure of I53–50 from EMDataResource (EMD-0350). (B) Structures from Protein Data Bank (PDB), PDB codes are the following: 3EGM (Ferritin), 7B3Y (mi3), and 5LQP (AP205).
Figure 4
Figure 4
The schematic representation of the immune response elicited by the VLPs. The figure was adapted from BioRender.com.
See this image and copyright information in PMC

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