Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer [PDF]
The tremendous pandemic potential of coronaviruses was demonstrated twice in the past few decades by two global outbreaks of deadly pneumonia. Entry of coronaviruses into cells is mediated by the transmembrane spike glycoprotein S, which forms a trimer carrying receptor-binding and membrane fusion functions.
Walls, Alexandra +7 more
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The recent outbreak of pneumonia-causing COVID-19 in China is an urgent global public health issue with an increase in mortality and morbidity. Here we report our modelled homo-trimer structure of COVID-19 spike glycoprotein in both closed (ligand-free ...
Naveen Vankadari, Jacqueline A. Wilce
doaj +3 more sources
Bat and pangolin coronavirus spike glycoprotein structures provide insights into SARS-CoV-2 evolution [PDF]
The spike glycoprotein in coronaviruses is a key viral protein for cross-species transmission and infection. Here, the authors present the cryo-EM structures of the spike ectodomains from bat and pangolin coronaviruses, compare them with the available ...
Shuyuan Zhang +8 more
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Cetacean coronavirus spikes highlight S glycoprotein structural plasticity. [PDF]
AbstractCoronaviruses (CoVs) exhibit a remarkable ability for spill-over infections into naive host populations. While much research has focused on the spike (S) glycoproteins of zoonotic alpha- and betacoronaviruses, the S proteins of gamma- and deltacoronaviruses, which predominantly infect avian hosts, remain poorly understood. Here, we present high-
Hulswit RJG +8 more
europepmc +2 more sources
Mutational heterogeneity in spike glycoproteins of severe acute respiratory syndrome coronavirus 2 [PDF]
The novel coronavirus SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) has led to a global crisis by infecting millions of people across the globe eventually causing multiple deaths. The prominent player of the virus has been known as the spike protein which enters the host system and leads to the infection.
Aanchal Mathur +5 more
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Closing coronavirus spike glycoproteins by structure-guided design [PDF]
The recent spillover of SARS-CoV-2 in the human population resulted in the ongoing COVID-19 pandemic which has already caused 4.9 million infections and more than 326,000 fatalities. To initiate infection the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface, determining host and tissue tropism, and fusion of the viral and ...
McCallum, Matthew +3 more
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Therapeutic targeting of coronavirus spike glycoprotein priming [PDF]
Abstract Processing of certain viral proteins and bacterial toxins by host serine proteases is a frequent and critical step in virulence. The coronavirus spike glycoprotein contains three (S1, S2, and S2’) cleavage sites that are processed by human host proteases.
Maurizio Pellecchia +5 more
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Expression of SARS-coronavirus spike glycoprotein in Pichia pastoris [PDF]
To establish a rapid and economical method for the expression of viral proteins in high yield and purity by Pichia pastoris, the S protein of the SARS-CoV was selected in this study. Six S glycoprotein fragments were expressed in Escherichia coli BL21 and yeast KM71H strains.
Chuck, Chi-Pang +5 more
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An Overview of Spike Surface Glycoprotein in Severe Acute Respiratory Syndrome–Coronavirus [PDF]
The novel coronavirus originated in December 2019 in Hubei, China. This contagious disease named as COVID-19 resulted in a massive expansion within 6 months by spreading to more than 213 countries. Despite the availability of antiviral drugs for the treatment of various viral infections, it was concluded by the WHO that there is no medicine to treat ...
Muthu Kumaradoss Kathiravan +5 more
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Incorporation of Spike and Membrane Glycoproteins into Coronavirus Virions [PDF]
The envelopes of coronaviruses (CoVs) contain primarily three proteins; the two major glycoproteins spike (S) and membrane (M), and envelope (E), a non-glycosylated protein. Unlike other enveloped viruses, CoVs bud and assemble at the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC).
Makoto Ujike, Fumihiro Taguchi
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