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Review
. 2020 Sep 10;25(18):4133.
doi: 10.3390/molecules25184133.

Mass Spectrometry and Structural Biology Techniques in the Studies on the Coronavirus-Receptor Interaction

Danuta Witkowska  1
Affiliations
Review

Mass Spectrometry and Structural Biology Techniques in the Studies on the Coronavirus-Receptor Interaction

Danuta Witkowska. Molecules. .

Abstract

Mass spectrometry and some other biophysical methods, have made substantial contributions to the studies on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and human proteins interactions. The most interesting feature of SARS-CoV-2 seems to be the structure of its spike (S) protein and its interaction with the human cell receptor. Mass spectrometry of spike S protein revealed how the glycoforms are distributed across the S protein surface. X-ray crystallography and cryo-electron microscopy made huge impact on the studies on the S protein and ACE2 receptor protein interaction, by elucidating the three-dimensional structures of these proteins and their conformational changes. The findings of the most recent studies in the scope of SARS-CoV-2-Human protein-protein interactions are described here.

Keywords: MS; SARS coronavirus; glycosylation; spike protein-ACE2 interaction; structural techniques.

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Conflict of interest statement

The author declares no conflict of interest.

Figures

Figure 1
Figure 1
Overall structure of the S protein protomer of SARS-CoV-2. (A) Each monomer of the S protein protomer is represented by a different color. (B) Receptor-binding sites of the chains A, B, and C of the S protein are highlighted in blue, purple and green color, respectively. Glycan ligands have been omitted for simplicity. (C) Monomer of the SARS-CoV2 spike protein during the receptor-accessible conformation. The receptor binding domain (RBD) is shown in cyan. Visualized by USCF Chimera [80]. PDB ID: 6VSB.
Figure 1
Figure 1
Overall structure of the S protein protomer of SARS-CoV-2. (A) Each monomer of the S protein protomer is represented by a different color. (B) Receptor-binding sites of the chains A, B, and C of the S protein are highlighted in blue, purple and green color, respectively. Glycan ligands have been omitted for simplicity. (C) Monomer of the SARS-CoV2 spike protein during the receptor-accessible conformation. The receptor binding domain (RBD) is shown in cyan. Visualized by USCF Chimera [80]. PDB ID: 6VSB.
Figure 2
Figure 2
Interactions between SARS-CoV-2 RBD (in orange) and ACE2 (the main interacting α1 helix in dark green, the α2 helix also contributing to the interaction in green), visualized by USCF Chimera. PDB ID: 6M0J.
Figure 3
Figure 3
Comparison of the SARS-CoV-RBD/hACE2 and SARS-CoV-2 RBD/hACE2 binding sites. The most prominent substitutions are highlighted in yellow. 2AJF stands for PDB ID of the receptor binding domain of SARS-CoV; below the RBD sequences of the SARS-CoV-2 S1 protein (PDB IDs: 6LZG and 6M0J).
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