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Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Arch+Virol 2021 ; 166 (3): 697-714 Nephropedia Template TP
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A comparative study of human betacoronavirus spike proteins: structure, function and therapeutics #MMPMID33483791
Verma J; Subbarao N
Arch Virol 2021[Mar]; 166 (3): 697-714 PMID33483791show ga
Coronaviruses are the paradigm of emerging 21(st) century zoonotic viruses, triggering numerous outbreaks and a severe global health crisis. The current COVID-19 pandemic caused by SARS-CoV-2 has affected more than 51 million people across the globe as of 12 November 2020. The crown-like spikes on the surface of the virion are the unique structural feature of viruses in the family Coronaviridae. The spike (S) protein adopts distinct conformations while mediating entry of the virus into the host. This multifunctional protein mediates the entry process by recognizing its receptor on the host cell, followed by the fusion of the viral membrane with the host cell membrane. This review article focuses on the structural and functional comparison of S proteins of the human betacoronaviruses, severe acute respiratory syndrome coronavirus (SARS-CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Here, we review the current state of knowledge about receptor recognition, the membrane fusion mechanism, structural epitopes, and glycosylation sites of the S proteins of these viruses. We further discuss various vaccines and other therapeutics such as monoclonal antibodies, peptides, and small molecules based on the S protein of these three viruses.
|*Virus Attachment[MESH]
|Angiotensin-Converting Enzyme 2/metabolism[MESH]
|Antiviral Agents/therapeutic use[MESH]
|COVID-19 Drug Treatment[MESH]
|COVID-19 Vaccines/immunology[MESH]
|COVID-19/pathology/*transmission[MESH]
|Crystallography, X-Ray[MESH]
|Glycosylation[MESH]
|Humans[MESH]
|Middle East Respiratory Syndrome Coronavirus/*ultrastructure[MESH]