PreprintArticleVersion 1Preserved in Portico This version is not peer-reviewed
Structural Identification of the Electrostatic Hot Spots for Severe Acute Respiratory Syndrome Coronavirus Spike Protein to Be Complexed with Its Receptor ACE2 and Its Neutralizing Antibodies
Version 1
: Received: 17 February 2020 / Approved: 18 February 2020 / Online: 18 February 2020 (11:03:10 CET)
How to cite:
Li, W. Structural Identification of the Electrostatic Hot Spots for Severe Acute Respiratory Syndrome Coronavirus Spike Protein to Be Complexed with Its Receptor ACE2 and Its Neutralizing Antibodies. Preprints2020, 2020020265. https://doi.org/10.20944/preprints202002.0265.v1
Li, W. Structural Identification of the Electrostatic Hot Spots for Severe Acute Respiratory Syndrome Coronavirus Spike Protein to Be Complexed with Its Receptor ACE2 and Its Neutralizing Antibodies. Preprints 2020, 2020020265. https://doi.org/10.20944/preprints202002.0265.v1
Li, W. Structural Identification of the Electrostatic Hot Spots for Severe Acute Respiratory Syndrome Coronavirus Spike Protein to Be Complexed with Its Receptor ACE2 and Its Neutralizing Antibodies. Preprints2020, 2020020265. https://doi.org/10.20944/preprints202002.0265.v1
APA Style
Li, W. (2020). Structural Identification of the Electrostatic Hot Spots for Severe Acute Respiratory Syndrome Coronavirus Spike Protein to Be Complexed with Its Receptor ACE2 and Its Neutralizing Antibodies. Preprints. https://doi.org/10.20944/preprints202002.0265.v1
Chicago/Turabian Style
Li, W. 2020 "Structural Identification of the Electrostatic Hot Spots for Severe Acute Respiratory Syndrome Coronavirus Spike Protein to Be Complexed with Its Receptor ACE2 and Its Neutralizing Antibodies" Preprints. https://doi.org/10.20944/preprints202002.0265.v1
Abstract
The spike protein of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2), which is mediated by the receptor binding domain (RBD) of the spike protein. Recently, an analysis based on decade-long structural studies of SARS was reported to illustrate with atomic-level details receptor recognition by the novel coronavirus from Wuhan, i.e., 2019-nCoV. Here, this article reports a comprehensive set of structural electrostatic analysis of all SARS-CoV spike protein RBD-related structures as of February 13, 2020, aiming at identifying the electrostatic hot spots for SARS-CoV spike protein to be complexed with ACE2 and its neutralizing antibodies. First, this article identified a structural action mechanism of the F26G19 antibody (of SARS-CoV spike protein), where its Asp56 residue binds to the Arg426 of the SARS-CoV spike protein RBD against the formation of the interfacial Arg426-Glu329 salt bridges between ACE2 and the SARS-CoV spike protein RBD. Second, a hypothesis is reported that a pair of electrostatic clips exist at the interface between ACE2 and the SARS-CoV spike protein RBD, including both Arg426-Glu329 and His445-Glu23-Lys447 salt bridges. Last, this article reports a structurally identified interfacial Glu35-Arg479 salt bridge which helps stabilize the complex structure of ACE2 and the SARS-CoV spike protein RBD. Overall, the structurally identified electrostatic hot spots reported here may be useful for the design of SARS-CoV-neutralizing antibodies in future.
Medicine and Pharmacology, Pulmonary and Respiratory Medicine
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
