Structural basis of severe acute respiratory syndrome coronavirus 2 infection. Issue 1 (January 2021)
- Record Type:
- Journal Article
- Title:
- Structural basis of severe acute respiratory syndrome coronavirus 2 infection. Issue 1 (January 2021)
- Main Title:
- Structural basis of severe acute respiratory syndrome coronavirus 2 infection
- Authors:
- Ge, Jiwan
Zhang, Senyan
Zhang, Linqi
Wang, Xinquan - Abstract:
- 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 theAbstract : 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. … (more)
- Is Part Of:
- Current opinion in HIV & AIDS. Volume 16:Issue 1(2021)
- Journal:
- Current opinion in HIV & AIDS
- Issue:
- Volume 16:Issue 1(2021)
- Issue Display:
- Volume 16, Issue 1 (2021)
- Year:
- 2021
- Volume:
- 16
- Issue:
- 1
- Issue Sort Value:
- 2021-0016-0001-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-01
- Subjects:
- angiotensin converting enzyme 2 -- receptor-binding domain -- severe acute respiratory syndrome coronavirus 2 -- spike glycoprotein -- virus–receptor interaction
AIDS (Disease) -- Periodicals
HIV infections -- Periodicals
HIV Infections -- Periodicals
Acquired Immunodeficiency Syndrome -- Periodicals
Infections à VIH -- Périodiques
Sida -- Périodiques
AIDS (Disease)
HIV infections
Periodicals
616.9792005 - Journal URLs:
- http://gateway.ovid.com/ovidweb.cgi?T=JS&MODE=ovid&NEWS=n&PAGE=toc&D=ovft&AN=01222929-000000000-00000 ↗
http://journals.lww.com/pages/default.aspx ↗ - DOI:
- 10.1097/COH.0000000000000658 ↗
- Languages:
- English
- ISSNs:
- 1746-630X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3500.775250
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 15734.xml