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Spike Proteins of SARS-CoV and SARS-CoV-2 Utilize Different Mechanisms to Bind With Human ACE2.
Xie, Yixin; Karki, Chitra B; Du, Dan; Li, Haotian; Wang, Jun; Sobitan, Adebiyi; Teng, Shaolei; Tang, Qiyi; Li, Lin.
  • Xie Y; Computational Science Program, University of Texas at El Paso, El Paso, TX, United States.
  • Karki CB; Computational Science Program, University of Texas at El Paso, El Paso, TX, United States.
  • Du D; Computational Science Program, University of Texas at El Paso, El Paso, TX, United States.
  • Li H; Department of Physics, University of Texas at El Paso, El Paso, TX, United States.
  • Wang J; Department of Physics, University of Texas at El Paso, El Paso, TX, United States.
  • Sobitan A; Department of Biology, Howard University, Washington, DC, United States.
  • Teng S; Department of Biology, Howard University, Washington, DC, United States.
  • Tang Q; Department of Biology, Howard University, Washington, DC, United States.
  • Li L; Computational Science Program, University of Texas at El Paso, El Paso, TX, United States.
Front Mol Biosci ; 7: 591873, 2020.
Article in English | MEDLINE | ID: covidwho-1000111
ABSTRACT
The ongoing outbreak of COVID-19 has been a serious threat to human health worldwide. The virus SARS-CoV-2 initiates its infection to the human body via the interaction of its spike (S) protein with the human Angiotensin-Converting Enzyme 2 (ACE2) of the host cells. Therefore, understanding the fundamental mechanisms of how SARS-CoV-2 S protein receptor binding domain (RBD) binds to ACE2 is highly demanded for developing treatments for COVID-19. Here we implemented multi-scale computational approaches to study the binding mechanisms of human ACE2 and S proteins of both SARS-CoV and SARS-CoV-2. Electrostatic features, including electrostatic potential, electric field lines, and electrostatic forces of SARS-CoV and SARS-CoV-2 were calculated and compared in detail. The results demonstrate that SARS-CoV and SARS-CoV-2 S proteins are both attractive to ACE2 by electrostatic forces even at different distances. However, the residues contributing to the electrostatic features are quite different due to the mutations between SARS-CoV S protein and SARS-CoV-2 S protein. Such differences are analyzed comprehensively. Compared to SARS-CoV, the SARS-CoV-2 binds with ACE2 using a more robust strategy The electric field line related residues are distributed quite differently, which results in a more robust binding strategy of SARS-CoV-2. Also, SARS-CoV-2 has a higher electric field line density than that of SARS-CoV, which indicates stronger interaction between SARS-CoV-2 and ACE2, compared to that of SARS-CoV. Key residues involved in salt bridges and hydrogen bonds are identified in this study, which may help the future drug design against COVID-19.
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Full text: Available Collection: International databases Database: MEDLINE Language: English Journal: Front Mol Biosci Year: 2020 Document Type: Article Affiliation country: Fmolb.2020.591873

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Full text: Available Collection: International databases Database: MEDLINE Language: English Journal: Front Mol Biosci Year: 2020 Document Type: Article Affiliation country: Fmolb.2020.591873