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Structural basis of severe acute respiratory syndrome coronavirus 2 infection.
Curr Opin HIV AIDS. 2021 Jan; 16(1):74-81.CO

Abstract

PURPOSE OF REVIEW

The spike glycoprotein plays a critical role in severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection by recognizing the angiotensin converting enzyme 2 (ACE2) receptor and mediating fusion of the viral envelope with the cell membrane. It is also the major target for neutralizing antibodies and vaccines. This review summarizes recent studies on the structure and function of spike glycoprotein, which revealed the structural basis of SARS-CoV-2 infection.

RECENT FINDINGS

SARS-CoV-2 spike glycoprotein, similar to those of SARS-CoV and Middle East respiratory syndrome coronavirus, spontaneously samples different prefusion states with the receptor-binding domain (RBD) adopting 'up' or 'down' conformations, and the RBD 'down' to 'up' conformational change is required for ACE2 binding. Receptor binding and spike glycoprotein priming by host proteases such as furin and transmembrane protease serine 2 induce pre to postfusion conformational changes of the spike trimer that enable membrane fusion. Interactions between SARS-CoV-2 RBD and ACE2 were elucidated at atomic resolution using high-resolution crystal structures. These structures, together with adapted and remodeled SARS-CoV-2 strains, further revealed critical residues of the spike glycoprotein for SARS-CoV-2 infection and cross-species transmission.

SUMMARY

Recent studies on SARS-CoV-2 spike glycoprotein provide important structural knowledge for a better understanding of the molecular mechanisms of SARS-CoV-2 infection and cross-species transmission.

Authors+Show Affiliations

The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, Beijing, China.The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, Beijing, China.Center for Global Health and Infectious Diseases, Comprehensive AIDS Research Center, Beijing Advanced Innovation Center for Structural Biology, School of Medicine, Tsinghua University, Beijing, China.The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, Beijing, China.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

33186231

Citation

Ge, Jiwan, et al. "Structural Basis of Severe Acute Respiratory Syndrome Coronavirus 2 Infection." Current Opinion in HIV and AIDS, vol. 16, no. 1, 2021, pp. 74-81.
Ge J, Zhang S, Zhang L, et al. Structural basis of severe acute respiratory syndrome coronavirus 2 infection. Curr Opin HIV AIDS. 2021;16(1):74-81.
Ge, J., Zhang, S., Zhang, L., & Wang, X. (2021). Structural basis of severe acute respiratory syndrome coronavirus 2 infection. Current Opinion in HIV and AIDS, 16(1), 74-81. https://doi.org/10.1097/COH.0000000000000658
Ge J, et al. Structural Basis of Severe Acute Respiratory Syndrome Coronavirus 2 Infection. Curr Opin HIV AIDS. 2021;16(1):74-81. PubMed PMID: 33186231.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural basis of severe acute respiratory syndrome coronavirus 2 infection. AU - Ge,Jiwan, AU - Zhang,Senyan, AU - Zhang,Linqi, AU - Wang,Xinquan, PY - 2020/11/14/pubmed PY - 2021/1/5/medline PY - 2020/11/13/entrez SP - 74 EP - 81 JF - Current opinion in HIV and AIDS JO - Curr Opin HIV AIDS VL - 16 IS - 1 N2 - PURPOSE OF REVIEW: The spike glycoprotein plays a critical role in severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection by recognizing the angiotensin converting enzyme 2 (ACE2) receptor and mediating fusion of the viral envelope with the cell membrane. It is also the major target for neutralizing antibodies and vaccines. This review summarizes recent studies on the structure and function of spike glycoprotein, which revealed the structural basis of SARS-CoV-2 infection. RECENT FINDINGS: SARS-CoV-2 spike glycoprotein, similar to those of SARS-CoV and Middle East respiratory syndrome coronavirus, spontaneously samples different prefusion states with the receptor-binding domain (RBD) adopting 'up' or 'down' conformations, and the RBD 'down' to 'up' conformational change is required for ACE2 binding. Receptor binding and spike glycoprotein priming by host proteases such as furin and transmembrane protease serine 2 induce pre to postfusion conformational changes of the spike trimer that enable membrane fusion. Interactions between SARS-CoV-2 RBD and ACE2 were elucidated at atomic resolution using high-resolution crystal structures. These structures, together with adapted and remodeled SARS-CoV-2 strains, further revealed critical residues of the spike glycoprotein for SARS-CoV-2 infection and cross-species transmission. SUMMARY: Recent studies on SARS-CoV-2 spike glycoprotein provide important structural knowledge for a better understanding of the molecular mechanisms of SARS-CoV-2 infection and cross-species transmission. SN - 1746-6318 UR - https://www.unboundmedicine.com/medline/citation/33186231/Structural_basis_of_severe_acute_respiratory_syndrome_coronavirus_2_infection_ DB - PRIME DP - Unbound Medicine ER -