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Review
. 2021 Mar 4;17(3):644-653.
doi: 10.1080/21645515.2020.1804777. Epub 2020 Oct 29.

SARS-CoV-2 vaccine candidates in rapid development

Lifeng Li  1   2 , Pengbo Guo  1 , Xiaoman Zhang  1 , Zhidan Yu  1 , Wancun Zhang  1 , Huiqing Sun  2
Affiliations
Review

SARS-CoV-2 vaccine candidates in rapid development

Lifeng Li et al. Hum Vaccin Immunother. .

Abstract

The COVID-19 pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is still spreading globally. The scientific community is attempting to procure an effective treatment and prevention strategy for COVID-19. A rising number of vaccines for COVID-19 are being developed at an unprecedented speed. Development platforms include traditional inactivated or live attenuated virus vaccines, DNA or RNA vaccines, recombinant viral vector vaccines, and protein or peptide subunit vaccines. There are 23 vaccines in the clinical evaluation stage and at least 140 candidate vaccines in preclinical evaluation. In this review, we describe research regarding basic knowledge on the virus, updates on the animal models, current landscape of vaccines in clinical evaluation and updated research results on vaccine development. Safe and effective COVID-19 vaccines require further investigation.

Keywords: COVID-19 pandemic; SARS-CoV-2; animal models; coronavirus; vaccine development.

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Figures

Figure 1.
Figure 1.
Comparison of the similarity of structural proteins of SARS-CoV-2 with the corresponding proteins of SARS-CoV and MERS-CoV. (a) Percentage genetic similarity of the individual structural proteins of SARS‐CoV‐2 with those of SARS‐CoV and MERSCoV. (b) Circular phylogram of the phylogenetic trees of the four structural proteins. All trees were constructed based on the available unique sequences using PASTA and rooted with the out group Zaria Bat CoV strain (accession ID: HQ166910.1). Reprint from reference.16
Figure 2.
Figure 2.
Structure of 2019-nCoV S in the prefusion conformation. (a) Schematic of 2019-nCoV S primary structure colored by domain. Domains that were excluded from the ectodomain expression construct or could not be visualized in the final map are colored white. SS, signal sequence; S2′, S2′ protease cleavage site; FP, fusion peptide; HR1, heptad repeat 1; CH, central helix; CD, connector domain; HR2, heptad repeat 2; TM, transmembrane domain; CT, cytoplasmic tail. Arrows denote protease cleavage sites. (b) Side and top views of the prefusion structure of the 2019-nCoV S protein with a single RBD in the up conformation. The two RBD down protomers are shown as cryo-EM density in either white or gray and the RBD up protomer is shown in ribbons colored corresponding to the schematic in (a). Reprint from reference.20
Figure 3.
Figure 3.
Overall structure of the RBD-ACE2-B0AT1 complex. (a) Cryo-EM map of the RBD-ACE2-B0AT1 complex. The overall reconstruction of the ternary complex at 2.9 Å is shown on the left. The inset shows the focused refined map of RBD. Protomer A of ACE2 (cyan), protomer B of ACE2 (blue), protomer A of B0AT1 (pink) and protomer B of B0AT1 (gray) are shown. The red and gold color represent RBD protomers. (b) Overall structure of the RBD-ACE2-B0AT1 complex. The complex is colored by subunits, with the PD and CLD in one ACE2 protomer colored cyan and blue, respectively. The glycosylation moieties are shown as sticks. Reprint from reference.21
Figure 4.
Figure 4.
Timeline of the study progress related to the candidate vaccines against SARS-CoV-2
See this image and copyright information in PMC

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