Abstract
The ongoing pandemic of coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), poses a grave threat to global public health and imposes a severe burden on the entire human society. Like other coronaviruses, the SARS-CoV-2 genome encodes spike (S) glycoproteins, which protrude from the surface of mature virions. The S glycoprotein plays essential roles in virus attachment, fusion and entry into the host cell. Surface location of the S glycoprotein renders it a direct target for host immune responses, making it the main target of neutralizing antibodies. In the light of its crucial roles in viral infection and adaptive immunity, the S protein is the focus of most vaccine strategies as well as therapeutic interventions. In this review, we highlight and describe the recent progress that has been made in the biosynthesis, structure, function, and antigenicity of the SARS-CoV-2 S glycoprotein, aiming to provide valuable insights into the design and development of the S protein-based vaccines as well as therapeutics.
Highlights
The coronavirus disease 2019 (COVID-19) global pandemic represents an unprecedented public health, social and economic challenge [1, 2]
SARSCoV-2 evades immune surveillance through conformational masking, which is well-documented for human immunodeficiency virus (HIV)-1 [43, 44]; while at the same time, the S protein could transiently sample the functional state to engage angiotensinconverting enzyme 2 (ACE2), consistent with the notion that the fusion glycoprotein of highly pathogenic viruses have evolved to perform its functions while evading host neutralizing antibody responses
No vaccines for any of the known human CoVs have been licensed [143, 144], several potential SARS-CoV and MERS-CoV vaccines have advanced into human clinical trials for years [117, 145], suggesting the development of effective vaccines against human CoVs has always been challenging
Summary
The coronavirus disease 2019 (COVID-19) global pandemic represents an unprecedented public health, social and economic challenge [1, 2]. Prefusion structures of human coronavirus HKU1 (HCoVHKU1) and mouse hepatitis virus S protein ectodomains without two consecutive proline mutations reveal only fully closed conformation [37, 42], similar to that observed for a full-length, wild-type prefusion form of the SARS-CoV-2 S glycoprotein [41].
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