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Spike Glycoprotein-Mediated Entry of SARS Coronaviruses
- Source :
- Viruses, Viruses, Vol 12, Iss 1289, p 1289 (2020)
- Publication Year :
- 2020
- Publisher :
- MDPI AG, 2020.
-
Abstract
- Severe acute respiratory syndrome coronavirus (SARS-CoV) and SARS-CoV-2 are enveloped, positive-sense, single-stranded RNA viruses and causes of epidemic diseases that have resulted in public health emergencies worldwide. Angiotensin-converting enzyme 2 (ACE2) is the receptor that allows the entry of these two viruses into host cells, a key step in the life cycle of the pathogens. The characterization of the interactions of ACE2 with the viral spike glycoproteins and structural studies of the ACE2-binding-induced conformational changes in the viral spike glycoproteins have furthered our understanding of the entry processes of these two viruses, and these studies provide useful information that will facilitate the development of antiviral agents and vaccines to control the diseases.
- Subjects :
- 0301 basic medicine
2019-20 coronavirus outbreak
receptor binding
viruses
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
membrane fusion
lcsh:QR1-502
Review
Plasma protein binding
Biology
lcsh:Microbiology
03 medical and health sciences
conformational change
0302 clinical medicine
Protein Domains
Virology
Humans
spike glycoprotein
chemistry.chemical_classification
SARS-CoV-2
SARS coronaviruses
COVID-19
RNA
Lipid bilayer fusion
Virus Internalization
Antibodies, Neutralizing
030104 developmental biology
Infectious Diseases
Severe acute respiratory syndrome-related coronavirus
chemistry
030220 oncology & carcinogenesis
Spike Glycoprotein, Coronavirus
entry
Spike (software development)
Angiotensin-Converting Enzyme 2
Severe acute respiratory syndrome coronavirus
Coronavirus Infections
Glycoprotein
hormones, hormone substitutes, and hormone antagonists
Protein Binding
Subjects
Details
- ISSN :
- 19994915
- Volume :
- 12
- Database :
- OpenAIRE
- Journal :
- Viruses
- Accession number :
- edsair.doi.dedup.....42f1ed1695a81118de738d8eb8ab193c
- Full Text :
- https://doi.org/10.3390/v12111289