Academic Journal

Single-Molecule Investigation of the Binding Interface Stability of SARS-CoV-2 Variants with ACE2.

التفاصيل البيبلوغرافية
العنوان: Single-Molecule Investigation of the Binding Interface Stability of SARS-CoV-2 Variants with ACE2.
المؤلفون: Ray, Ankita, Minh Tran, Thu Thi, Santos Natividade, Rita Dos, Moreira, Rodrigo A, Simpson, Joshua D, Mohammed, Danahe, Koehler, Melanie, L Petitjean, Simon J, Zhang, Qingrong, Bureau, Fabrice, Gillet, Laurent, Poma, Adolfo B, Alsteens, David
المصدر: ACS Nanoscience Au, 4 (2), 136 - 145 (2024-04-17)
بيانات النشر: American Chemical Society, 2024.
سنة النشر: 2024
مصطلحات موضوعية: ACE2, Atomic force microscopy, biolayer interferometry, convalescent patient sera, RBD, SARS-CoV-2, Steered molecular dynamics, Chemistry (miscellaneous), Materials Science (miscellaneous), Human health sciences, Immunology & infectious disease, Sciences de la santé humaine, Immunologie & maladie infectieuse
الوصف: The SARS-CoV-2 pandemic spurred numerous research endeavors to comprehend the virus and mitigate its global severity. Understanding the binding interface between the virus and human receptors is pivotal to these efforts and paramount to curbing infection and transmission. Here we employ atomic force microscopy and steered molecular dynamics simulation to explore SARS-CoV-2 receptor binding domain (RBD) variants and angiotensin-converting enzyme 2 (ACE2), examining the impact of mutations at key residues upon binding affinity. Our results show that the Omicron and Delta variants possess strengthened binding affinity in comparison to the Mu variant. Further, using sera from individuals either vaccinated or with acquired immunity following Delta strain infection, we assess the impact of immunity upon variant RBD/ACE2 complex formation. Single-molecule force spectroscopy analysis suggests that vaccination before infection may provide stronger protection across variants. These results underscore the need to monitor antigenic changes in order to continue developing innovative and effective SARS-CoV-2 abrogation strategies.
نوع الوثيقة: journal article
http://purl.org/coar/resource_type/c_6501
article
peer reviewed
اللغة: English
Relation: https://pubs.acs.org/doi/pdf/10.1021/acsnanoscienceau.3c00060; urn:issn:2694-2496
DOI: 10.1021/acsnanoscienceau.3c00060
URL الوصول: https://orbi.uliege.be/handle/2268/320928
Rights: open access
http://purl.org/coar/access_right/c_abf2
info:eu-repo/semantics/openAccess
رقم الانضمام: edsorb.320928
قاعدة البيانات: ORBi
الوصف
DOI:10.1021/acsnanoscienceau.3c00060