Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor

@article{Li2005StructureOS,
  title={Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor},
  author={Fang Li and Wenhui Li and M. Farzan and Stephen C. Harrison},
  journal={Science},
  year={2005},
  volume={309},
  pages={1864 - 1868}
}
The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the… 
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
TLDR
High-resolution crystal structures of the receptor-binding domain of the spike protein of SARS-CoV-2 and SARS -CoV in complex with ACE2 provide insights into the binding mode of these coronaviruses and highlight essential ACE2-interacting residues.
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TLDR
It is proposed that blocking the hydrophobic surface of RBD via neutralizing antibodies could prove to be an effective strategy to inhibit S-ACE2 interactions.
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The role of the RBM is a bi-functional bioactive surface that can be demonstrated by antibodies such as the neutralizing human anti-SARS monoclonal antibody (mAb) 80R which targets the R BM and competes with the ACE2 receptor for binding.
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TLDR
The structure of the SARS-CoV RBD reveals in atomic detail the specific and high-affinity interactions between the virus and its receptor and sheds light on critical residue changes that dictate the species specificity of the virus.
Critical Interactions Between the SARS-CoV-2 Spike Glycoprotein and the Human ACE2 Receptor
TLDR
It is proposed that blocking the hydrophobic surface of RBD via neutralizing antibodies could prove an effective strategy to inhibit S-ACE2 interactions.
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TLDR
Computational simulations of interactions between three representative RBD mutants and four host species-specific receptors indicate that some viral prototypes might utilize the rat ACE2 while rats might serve as a vector or reservoir of SARS-CoV.
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TLDR
A variant of ACE2 based on deep mutagenesis far outcompetes the natural receptor in binding the SARS-CoV-2 spike protein and gives ACE2 variants with affinities that rival those of monoclonal antibodies.
Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2
TLDR
Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment, however, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S 1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition.
Prefusion conformation of SARS-CoV-2 receptor-binding domain favours interactions with human receptor ACE2
TLDR
Cryo-EM structures of SARS-CoV-2 and SARS, caused by Severe Acute Respiratory Syndrome coronavirus, report here that the homotrimer Sars-Cov-2 S receptor-binding domain (RBD) that binds with hACE2 has expanded in size, undergoing a large conformational change relative to SARs- coV-1 S protein.
The sequence of human ACE2 is suboptimal for binding the S spike protein of SARS coronavirus 2
  • E. Procko
  • Biology, Medicine
    bioRxiv : the preprint server for biology
  • 2020
TLDR
Using deep mutagenesis, variants of ACE2 are identified with increased binding to the receptor binding domain of S, and the mutational landscape offers a blueprint for engineering high affinity proteins and peptides that block receptor binding sites on S to meet this unprecedented challenge.
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