journal article·2024-11Open access

Broad Adaptability of Coronavirus Adhesion Revealed from the Complementary Surface Affinity of Membrane and Spikes

Aritz B. García‐Arribas, Pablo Ibáñez‐Freire, Diego Carlero, Pablo Palacios‐Alonso, Miguel Cantero‐Reviejo, Pablo Ares, Guillermo López‐Polín, Han Yan, Yan Wang, Soumya Sarkar, Manish Chhowalla, Hanna M. Oksanen, Jaime Martín‐Benito, Pedro J. de Pablo, Rafael Delgado‐Buscalioni

Advanced Science· Volume 11· Issue 41

Abstract

Abstract Coronavirus stands for a large family of viruses characterized by protruding spikes surrounding a lipidic membrane adorned with proteins. The present study explores the adhesion of transmissible gastroenteritis coronavirus (TGEV) particles on a variety of reference solid surfaces that emulate typical virus‐surface interactions. Atomic force microscopy informs about trapping effectivity and the shape of the virus envelope on each surface, revealing that the deformation of TGEV particles spans from 20% to 50% in diameter. Given this large deformation range, experimental Langmuir isotherms convey an unexpectedly moderate variation in the adsorption‐free energy, indicating a viral adhesion adaptability which goes beyond the membrane. The combination of an extended Helfrich theory and coarse‐grained simulations reveals that, in fact, the envelope and the spikes present complementary adsorption affinities. While strong membrane‐surface interaction lead to highly deformed TGEV particles, surfaces with strong spike attraction yield smaller deformations with similar or even larger adsorption‐free energies.
Source: crossref · Quality: baseline

Research context

OpenAlex topics: Bacteriophages and microbial interactions · SARS-CoV-2 and COVID-19 Research · Lipid Membrane Structure and Behavior

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Departamento de Física de la Materia Condensada Universidad Autónoma de Madrid Madrid 28049 Spain

Departamento de Física Teórica de la Materia Condensada Universidad Autónoma de Madrid Madrid 28049 Spain

Departamento de Estructura de Macromoléculas Centro Nacional de Biotecnología CSIC Madrid 28049 Spain

Department of Materials Science and Metallurgy University of Cambridge Cambridge CB3 0FS UK

Faculty of Biological and Environmental Sciences Vijkki Biocenter University of Helsinki Helsinki 00014 Finland

Instituto de Física de la Materia Condensada IFIMAC Universidad Autónoma de Madrid Madrid 28049 Spain

Funding

Ministerio de Asuntos Económicos y Transformación Digital, Gobierno de España · Ministerio de Ciencia e Innovación · Comunidad de Madrid · Human Frontier Science Program · Fundación Banco Santander · Fundación General CSIC

References (85)

Show source-provided references
1. 10.1021/acsomega.0c0633510.1021/acsomega.0c06335 ↗
2. 10.1038/s41565-022-01177-210.1038/s41565-022-01177-2 ↗
3. 10.1016/j.chempr.2020.08.00110.1016/j.chempr.2020.08.001 ↗
4. 10.1103/PhysRevLett.119.03810210.1103/PhysRevLett.119.038102 ↗
5. 10.1080/0026894910803565610.1080/00268949108035656 ↗
6. 10.1016/bs.aivir.2016.08.00510.1016/bs.aivir.2016.08.005 ↗
7. 10.1038/s41586-020-2665-210.1038/s41586-020-2665-2 ↗
8. 10.1126/science.abd522310.1126/science.abd5223 ↗
9. 10.1021/acs.jcim.1c0124010.1021/acs.jcim.1c01240 ↗
10. Israelachvilii J. N. · 2011
11. 10.1209/epl/i2006-10249-710.1209/epl/i2006-10249-7 ↗
12. 10.1016/j.colcom.2020.10033810.1016/j.colcom.2020.100338 ↗
13. 10.1128/jvi.70.7.4773-4777.199610.1128/jvi.70.7.4773-4777.1996 ↗
14. 10.3390/cells1111175910.3390/cells11111759 ↗
15. 10.1016/j.watres.2009.02.00210.1016/j.watres.2009.02.002 ↗
16. 10.1021/acs.nanolett.0c0446510.1021/acs.nanolett.0c04465 ↗
17. 10.3390/pharmaceutics1412254910.3390/pharmaceutics14122549 ↗
18. 10.1016/j.foodcont.2022.10934010.1016/j.foodcont.2022.109340 ↗
19. Jiang C. · J. Virol. · 2022 · 96
20. 10.1073/pnas.080527010610.1073/pnas.0805270106 ↗
21. 10.1021/acs.est.3c0337610.1021/acs.est.3c03376 ↗
22. 10.1021/ba-1980-0189.ch00510.1021/ba-1980-0189.ch005 ↗
23. 10.1128/aem.49.1.91-95.198510.1128/aem.49.1.91-95.1985 ↗
24. 10.1128/aem.44.4.852-859.198210.1128/aem.44.4.852-859.1982 ↗
25. 10.1128/aem.46.3.673-682.198310.1128/aem.46.3.673-682.1983 ↗
26. 10.1021/acs.est.5b0464410.1021/acs.est.5b04644 ↗
27. 10.1016/j.mtbio.2022.10026510.1016/j.mtbio.2022.100265 ↗
28. 10.1021/acs.langmuir.3c0279210.1021/acs.langmuir.3c02792 ↗
29. 10.1021/acsami.2c2207810.1021/acsami.2c22078 ↗
30. 10.1016/S0169-7722(02)00087-610.1016/S0169-7722(02)00087-6 ↗
31. 10.1016/j.colsurfa.2013.02.04510.1016/j.colsurfa.2013.02.045 ↗
32. 10.1016/j.cplett.2014.07.04610.1016/j.cplett.2014.07.046 ↗
33. 10.1021/la950884d10.1021/la950884d ↗
34. 10.1039/C5NR04274G10.1039/C5NR04274G ↗
35. 10.1021/acsomega.0c0633510.1021/acsomega.0c06335 ↗
36. 10.1093/clinids/2.1.4010.1093/clinids/2.1.40 ↗
37. 10.1021/acs.jpcb.1c0605010.1021/acs.jpcb.1c06050 ↗
38. 10.1039/D1SM01026C10.1039/D1SM01026C ↗
39. 10.1101/pdb.top08047310.1101/pdb.top080473 ↗
40. 10.1016/S0006-3495(03)74722-510.1016/S0006-3495(03)74722-5 ↗
41. 10.1039/D2SM01181F10.1039/D2SM01181F ↗
42. 10.1016/j.bbrc.2022.01.10610.1016/j.bbrc.2022.01.106 ↗
43. 10.1128/mBio.00699-1610.1128/mBio.00699-16 ↗
44. 10.1038/s41467-019-08927-210.1038/s41467-019-08927-2 ↗
45. 10.1021/acs.analchem.9b0571610.1021/acs.analchem.9b05716 ↗
46. 10.1021/acsnano.6b0730210.1021/acsnano.6b07302 ↗
47. 10.1103/PhysRevE.65.04191210.1103/PhysRevE.65.041912 ↗
48. 10.1016/S1383-8121(06)80025-410.1016/S1383-8121(06)80025-4 ↗
49. 10.1021/la049302v10.1021/la049302v ↗
50. 10.1021/la990304310.1021/la9903043 ↗
51. 10.1016/S0006-3495(00)76611-210.1016/S0006-3495(00)76611-2 ↗
52. 10.3389/fphy.2021.68098310.3389/fphy.2021.680983 ↗
53. 10.1038/s41598-022-14884-610.1038/s41598-022-14884-6 ↗
54. 10.1103/PhysRevE.82.01190510.1103/PhysRevE.82.011905 ↗
55. 10.1016/j.matcom.2023.02.02010.1016/j.matcom.2023.02.020 ↗
56. Wang B. · J. Chem. Inf. Model. · 2021 · 62 · 12
57. 10.1016/j.str.2006.10.00310.1016/j.str.2006.10.003 ↗
58. 10.1126/science.abd522310.1126/science.abd5223 ↗
59. 10.1073/pnas.211270311810.1073/pnas.2112703118 ↗
60. 10.1103/PhysRevA.42.476810.1103/PhysRevA.42.4768 ↗
61. 10.1201/978113411158910.1201/9781134111589 ↗
62. 10.1002/jcc.2198910.1002/jcc.21989 ↗
63. 10.1007/BF0245220810.1007/BF02452208 ↗
64. 10.1186/s12985-019-1182-010.1186/s12985-019-1182-0 ↗
65. 10.1021/la204903710.1021/la2049037 ↗
66. 10.1021/acs.langmuir.1c0191010.1021/acs.langmuir.1c01910 ↗
67. 10.1039/D2SM00871H10.1039/D2SM00871H ↗
68. 10.1126/science.abb250710.1126/science.abb2507 ↗
69. 10.1016/j.cell.2020.02.05810.1016/j.cell.2020.02.058 ↗
70. 10.1021/acs.jpcb.0c0451110.1021/acs.jpcb.0c04511 ↗
71. 10.1021/acs.jpcb.2c0083310.1021/acs.jpcb.2c00833 ↗
72. 10.1016/j.virusres.2014.11.02110.1016/j.virusres.2014.11.021 ↗
73. 10.1039/D2SC06967A10.1039/D2SC06967A ↗
74. 10.1038/nphys285510.1038/nphys2855 ↗
75. 10.3390/covid104005410.3390/covid1040054 ↗
76. 10.1038/s41401-020-0485-410.1038/s41401-020-0485-4 ↗
77. 10.1371/journal.pone.001567410.1371/journal.pone.0015674 ↗
78. 10.1023/A:101114783258610.1023/A:1011147832586 ↗
79. 10.1016/j.ultramic.2012.01.00710.1016/j.ultramic.2012.01.007 ↗
80. 10.1063/1.115002110.1063/1.1150021 ↗
81. 10.1007/978-1-4939-8894-5_1510.1007/978-1-4939-8894-5_15 ↗
82. 10.1016/j.ultramic.2012.07.00210.1016/j.ultramic.2012.07.002 ↗
83. 10.1063/1.243241010.1063/1.2432410 ↗
84. 10.1103/PhysRevE.82.01190510.1103/PhysRevE.82.011905 ↗
85. 10.1063/1.297817710.1063/1.2978177 ↗