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Emerging Microbes & Infections Volume 11, 2022 - Issue 1
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Coronaviruses

Pathogen-host adhesion between SARS-CoV-2 spike proteins from different variants and human ACE2 studied at single-molecule and single-cell levels

Xiaoxu Zhanga Beijing Advanced Innovation Center for Soft Matter Science and Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, People’s Republic of ChinaORCID Iconhttps://orcid.org/0000-0003-2724-9896View further author information
ORCID Icon,
Bixia Honga Beijing Advanced Innovation Center for Soft Matter Science and Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, People’s Republic of ChinaView further author information
,
Peng Weib School of Traditional Chinese Medicine, Beijing University of Chinese Medicine, Beijing, People’s Republic of ChinaORCID Iconhttps://orcid.org/0000-0002-3721-7014View further author information
ORCID Icon,
Pengfei Peia Beijing Advanced Innovation Center for Soft Matter Science and Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, People’s Republic of ChinaView further author information
,
Haifeng Xuc Beijing Laboratory of Biomedical Materials, College of Materials Science and Engineering, Beijing University of Chemical Technology, Beijing, People’s Republic of ChinaView further author information
,
Long Chena Beijing Advanced Innovation Center for Soft Matter Science and Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, People’s Republic of ChinaORCID Iconhttps://orcid.org/0000-0002-3812-1815View further author information
ORCID Icon,
Yigang Tonga Beijing Advanced Innovation Center for Soft Matter Science and Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, People’s Republic of ChinaORCID Iconhttps://orcid.org/0000-0002-8503-8045View further author information
ORCID Icon,
Jialin Chend State Key Laboratory for Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, People’s Republic of China;e The Key Laboratory of Chemistry for Natural Products of Guizhou Province and Chinese Academy of Sciences, Guiyang, People’s Republic of ChinaCorrespondence[email protected]
ORCID Iconhttps://orcid.org/0000-0001-6294-876XView further author information
ORCID Icon,
Shi-Zhong Luoa Beijing Advanced Innovation Center for Soft Matter Science and Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, People’s Republic of ChinaCorrespondence[email protected]
ORCID Iconhttps://orcid.org/0000-0002-4880-5962View further author information
ORCID Icon,
Huahao Fana Beijing Advanced Innovation Center for Soft Matter Science and Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, People’s Republic of ChinaCorrespondence[email protected]
ORCID Iconhttps://orcid.org/0000-0001-5007-2158View further author information
ORCID Icon &
Chengzhi Hea Beijing Advanced Innovation Center for Soft Matter Science and Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, People’s Republic of ChinaCorrespondence[email protected]
ORCID Iconhttps://orcid.org/0000-0001-5013-0207View further author information
ORCID Icon show all
Pages 2658-2669 | Received 19 Jun 2022, Accepted 21 Sep 2022, Published online: 04 Nov 2022

References

  • Liang K-H, Shih-Han Ko PYC, Chou Y-C, et al. Antibody cocktail effective against variants of SARS-CoV-2. J Biomed Sci. 2021;28:80, doi:10.1186/s12929-021-00777-9.
  • Yang J, Petitjean SJL, Koehler M, et al. Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor. Nat Commun. 2020;11:4541, doi:10.1038/s41467-020-18319-6.
  • Li M, Lou F, Fan H. SARS-CoV-2 variants of concern Delta: a great challenge to prevention and control of COVID-19. Signal Transduct Target Ther. 2021;6:349, doi:10.1038/s41392-021-00767-1.
  • Pei P, Qin H, Chen J, et al. Computational design of ultrashort peptide inhibitors of the receptor-binding domain of the SARS-CoV-2 S protein. Brief Bioinform. 2021;22; doi:10.1093/bib/bbab243.
  • Zumla A, Chan JFW, Azhar EI, et al. Coronaviruses – drug discovery and therapeutic options. Nat Rev Drug Discov. 2016;15:327–347.
  • Tian F, Liang Sun BT, Shi S, et al. N501y mutation of spike protein in SARS-CoV-2 strengthens its 2 binding to receptor ACE2. Elife. 2021;10:e69091.
  • Yan R, Yuanyuan Z, Li Y, et al. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science. 2020;367:1444–1448.
  • Millet JK, Whittaker GR. Host cell proteases: critical determinants of coronavirus tropism and pathogenesis. Virus Res. 2015;202:120–134.
  • Gu H, Chen Q, Yang G, et al. Adaptation of SARS-CoV-2 in BALB/c mice for testing vaccine efficacy. Science. 2020;369:1603–1607.
  • Yuan M, Huang D, Lee C-CD, et al. Structural and functional ramifcations of antigenic drift in recent SARS-CoV-2 variants. Science. 2021;373:818–823.
  • Motozono C, Toyoda M, Zahradnik J, et al. SARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity. Cell Host Microbe. 2021;29:1124–1136.e11.
  • Liu Z, Van Blargan LA, Bloyet LM, et al. Identifcation of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization. Cell Host Microbe. 2021;29:477–488.e4.
  • Chen Y, Chen L, Yin S, et al. The third dose of CoronVac vaccination induces broad and potent adaptive immune responses that recognize SARS-CoV-2 Delta and Omicron variants. Emerg Microbes Infect. 2022;11:1524–1536. doi:10.1080/22221751.2022.2081614.
  • Espenhain L, Funk T, Overvad M, et al. Epidemiological characterisation of the first 785 SARS-CoV-2 Omicron variant cases in Denmark, December 2021. Eurosurveillance. 2021;26; doi:10.2807/1560-7917.Es.2021.26.50.2101146.
  • Tuekprakhon A, Nutalai R, Dijokaite-Guraliuc A, et al. Antibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1 serum. Cell. 2022;185:2422–2433.e13. doi:10.1016/j.cell.2022.06.005.
  • Dejnirattisai W, Huo J, Zhou D, et al. SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses. Cell. 2022;185:467–484.e15. doi:10.1016/j.cell.2021.12.046.
  • Han P, Li L, Liu S, et al. Receptor binding and complex structures of human ACE2 to spike RBD from Omicron and Delta SARS-CoV-2. Cell. 2022;185:630–640.e10. doi:10.1016/j.cell.2022.01.001.
  • Ravichandran S, Coyle EM, Klenow L, et al. Antibody signature induced by SARS-CoV-2 spike protein immunogens in rabbits. Sci Transl Med. 2020;12:eabc3539.
  • Koehler M, Ray A, Moreira RA, et al. Molecular insights into receptor binding energetics and neutralization of SARS-CoV-2 variants. Nat Commun. 2021;12:6977. doi:10.1038/s41467-021-27325-1.
  • Petitjean SJL, Chen W, Koehler M, et al. Multivalent 9-O-acetylated-sialic acid glycoclusters as potent inhibitors for SARS-CoV-2 infection. Nat Commun. 2022;13:2564, doi:10.1038/s41467-022-30313-8.
  • Wang Y, Liu C, Zhang C, et al. Structural basis for SARS-CoV-2 Delta variant recognition of ACE2 receptor and broadly neutralizing antibodies. Nat Commun. 2022;13:871. doi:10.1038/s41467-022-28528-w.
  • Tai L, Zhu G, Yang M, et al. Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein. Proc Natl Acad Sci. 2021;118:e2112703118. doi:10.1073/pnas.2112703118.
  • Lv Z, Deng Y-Q, Ye Q, et al. Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody. Science. 2020;369:1505–1509. doi:10.1126/science.abc5881.
  • Zhang X, Kou X, Zhang W, et al. Identification of the new type of G-Quadruplex with multiple vacant sites in human telomeric DNA. CCS Chemistry. 2022;4:3023–3035. doi:10.31635/ccschem.021.202101436.
  • He C, Hu C, Hu X, et al. Direct observation of the reversible two-state unfolding and refolding of an α/β protein by single-molecule atomic force microscopy. Angew Chemie – Int Ed. 2015;54:9921–9925.
  • Moghaddar M, Radman R, Macreadie I. Severity, pathogenicity and transmissibility of Delta and Lambda variants of SARS-CoV-2, toxicity of spike protein and possibilities for future prevention of COVID-19. Microorganisms. 2021;9:2167; doi:10.3390/microorganisms9102167.
  • Müller DJ, Helenius J, Alsteens D, et al. Force probing surfaces of living cells to molecular resolution. Nat Chem Biol. 2009;5:383–390.
  • Maynard SA, Gelmi A, Stacey C, et al. Nanoscale molecular quantification of stem cell–hydrogel interactions. ACS Nano. 2020;14:17321–17332. doi:10.1021/acsnano.0c07428.
  • Helenius J, Heisenberg CP, Gaub HE, et al. Single-cell force spectroscopy. J Cell Sci. 2008;121:1785–1791.
  • Puckert C, Tomaskovik-Crook E, Gambhir S, et al. Molecular interactions and forces of adhesion between single human neural stem cells and gelatin methacrylate hydrogels of varying stiffness. Acta Biomater. 2020;106:156–169.
  • Bharadwaj M, Strohmeyer N, Colo GP, et al. αV-class integrins exert dual roles on α5β1 integrins to strengthen adhesion to fibronectin. Nat Commun. 2017;8:14348. doi:10.1038/ncomms14348.
  • Spoerri PM, Zhiqi Sun NS, Fässler R, et al. Protease-activated receptor signalling initiates α5β1-integrin-mediated adhesion in non-haematopoietic cells. Nat Mater. 2020;19:218–226. doi:10.1038/s41563-019-0580-4.
  • Klasse PJ, Moore JP. Antibodies to SARS-CoV-2 and their potential for therapeutic passive immunization. Elife. 2020;9. doi:10.7554/eLife.57877.
  • Prompetchara E, Tanapat Palaga CK. Immune responses in COVID-19 and potential vaccines lessons learned from SARS and MERS epidemic. Asian Pac J Allergy Immunol. 2020;38:1–9. doi:10.12932/AP-200220-0772.
  • Valdez-Cruz NA, Clara Espitia EGH, et al. Integrative overview of antibodies against SARS CoV 2 and their possible applications in COVID 19 prophylaxis and treatment. Microb Cell Factories. 2021;20:32. doi:10.1186/s12934-021-01526-1.
  • Jhun H, Park HY, Hisham Y, et al. SARS-CoV-2 Delta (B.1.617.2) variant: a unique T478K mutation in receptor binding motif (RBM) of Spike Gene. Immune Netw. 2021;21:e32, doi:10.4110/in.2021.21.e32.
  • Zhang JZ, Yeh H-W, Walls AC., et al. Thermodynamically coupled biosensors for detecting neutralizing antibodies against SARS-CoV-2 variants. Nat Biotechnol. 2022;40:1336–1340. doi:10.1038/s41587-022-01280-8.
  • Kozminsky M, Carey TR, Sohn LL. DNA-directed patterning for versatile validation and characterization of a lipid-based nanoparticle model of SARS-CoV-2. Adv Sci. 2021;8:2101166.
  • Ai J, Wang X, He X, et al. Antibody evasion of SARS-CoV-2 Omicron BA.1, BA.1.1, BA.2, and BA.3 sub-lineages. Cell Host Microbe. 2022;30:1077–1083.e4. doi:10.1016/j.chom.2022.05.001.
  • Hansen J, Baum A, Pascal KE, et al. Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail. Science. 2020;369:1010–1014. doi:10.1126/science.abd0827.
  • Omotuyi O, Olubiyi O, Nash O, et al. SARS-CoV-2 Omicron spike glycoprotein receptor binding domain exhibits super-binder ability with ACE2 but not convalescent monoclonal antibody. Comput Biol Med. 2022;142:105226. doi:10.1016/j.compbiomed.2022.105226.
  • Wang X, Zhao X, Song J, et al. Homologous or heterologous booster of inactivated vaccine reduces SARS-CoV-2 Omicron variant escape from neutralizing antibodies. Emerg Microbes Infect. 2022;11:477–481. doi:10.1080/22221751.2022.2030200.
  • Bertoglio F, Fühner V, Ruschig M, et al. A SARS-CoV-2 neutralizing antibody selected from COVID-19 patients binds to the ACE2-RBD interface and is tolerant to most known RBD mutations. Cell Reports. 2021;36:109433. doi:10.1016/j.celrep.2021.109433.
  • Zhou T, Wang L, Misasi J, et al. Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529. Science. 2022;376:eabn8897. doi:10.1126/science.abn8897.
  • Wang P, Nair MS, Liu L, et al. Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7. Nature. 2021;593:130–135. doi:10.1038/s41586-021-03398-2.
  • Goher SS, Ali F, Amin M. The Delta variant mutations in the receptor binding domain of SARS-CoV-2 show enhanced electrostatic interactions with the ACE2. Med Drug Discov. 2022;13:100114, doi:10.1016/j.medidd.2021.100114.
  • Rankl C, Kienberger F, Wildling L, et al. Multiple receptors involved in human rhinovirus attachment to live cells. Proc Natl Acad Sci. 2008;105:17778–17783. doi:10.1073/pnas.0806451105.
  • Qiao B, Olvera de la Cruz M. Enhanced binding of SARS-CoV-2 spike protein to receptor by distal polybasic cleavage sites. ACS Nano. 2020;14:10616–10623. doi:10.1021/acsnano.0c04798.
  • Gurung AB, Ali MA, Lee J, et al. Structural and functional insights into the major mutations of SARS-CoV-2 spike RBD and its interaction with human ACE2 receptor. J King Saud Univ – Sci. 2022;34:101773, doi:10.1016/j.jksus.2021.101773.
  • Kim S, Liu Y, Lei Z, et al. Differential interactions between human ACE2 and spike RBD of SARS-CoV-2 variants of concern. bioRxiv: The Preprint Server for Biology. 2021; doi:10.1101/2021.07.23.453598.
  • Shi S, Wang Z, Deng Y, et al. Combination of click chemistry and enzymatic ligation for stable and efficient protein immobilization for single-molecule force spectroscopy. CCS Chem. 2022;4:598–604. doi:10.31635/ccschem.021.202100779.
  • Zhang X, Chen J, Li E, et al. Ultrahigh adhesion force between silica-binding peptide SB7 and glass substrate studied by single-molecule force spectroscopy and molecular dynamic simulation. Front Chem. 2020;8:600918, doi:10.3389/fchem.2020.600918.
  • Bell GI. Models for the specific adhesion of cells to cells. Science. 1978;200:618–627. doi:10.1126/science.347575.
  • Abraham MJ, Murtola T, Schulz R, et al. GROMACS: high performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX. 2015;1–2:19–25.
  • Huang J, Rauscher S, Nawrocki G, et al. CHARMM36m: an improved force field for folded and intrinsically disordered proteins. Nat Methods. 2017;14:71–73. doi:10.1038/nmeth.4067.
  • Lee J, Cheng X, Swails JM, et al. CHARMM-GUI input generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM/OpenMM simulations using the CHARMM36 additive force field. J Chem Theory Comput. 2016;12:405–413.
  • Lemkul JA, Bevan DR. Assessing the stability of Alzheimer’s amyloid protofibrils using molecular dynamics. J Phys Chem B. 2010;114:1652–1660.

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