Your browser doesn't support javascript.
Mutations on RBD of SARS-CoV-2 Omicron variant result in stronger binding to human ACE2 receptor.
Lupala, Cecylia S; Ye, Yongjin; Chen, Hong; Su, Xiao-Dong; Liu, Haiguang.
  • Lupala CS; Complex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China.
  • Ye Y; Complex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China.
  • Chen H; School of Life Sciences, State Key Laboratory of Protein and Plant Gene Research and Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, 100871, People's Republic of China.
  • Su XD; School of Life Sciences, State Key Laboratory of Protein and Plant Gene Research and Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, 100871, People's Republic of China. Electronic address: xdsu@pku.edu.cn.
  • Liu H; Complex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China; Physics Department, Beijing Normal University, Haidian, Beijing, 100875, People's Republic of China. Electronic address: hgliu@csrc.ac.cn.
Biochem Biophys Res Commun ; 590: 34-41, 2022 01 29.
Article in English | MEDLINE | ID: covidwho-1588232
ABSTRACT
The COVID-19 pandemic caused by the SARS-CoV-2 virus has led to more than 270 million infections and 5.3 million of deaths worldwide. Several major variants of SARS-CoV-2 have emerged and posed challenges in controlling the pandemic. The recently occurred Omicron variant raised serious concerns about reducing the efficacy of vaccines and neutralization antibodies due to its vast mutations. We have modelled the complex structure of the human ACE2 protein and the receptor binding domain (RBD) of Omicron Spike protein (S-protein), and conducted atomistic molecular dynamics simulations to study the binding interactions. The analysis shows that the Omicron RBD binds more strongly to the human ACE2 protein than the original strain. The mutations at the ACE2-RBD interface enhance the tight binding by increasing hydrogen bonding interaction and enlarging buried solvent accessible surface area.
Subject(s)
Keywords

Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / COVID-19 Topics: Vaccines / Variants Limits: Humans Language: English Journal: Biochem Biophys Res Commun Year: 2022 Document Type: Article

Similar

MEDLINE

...
LILACS

LIS


Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / COVID-19 Topics: Vaccines / Variants Limits: Humans Language: English Journal: Biochem Biophys Res Commun Year: 2022 Document Type: Article