Article: Mutations in the SARS-CoV-2 spike RBD are responsible for stronger ACE2 binding and poor anti-SARS-CoV mAbs cross-neutralization.
Computational and structural biotechnology journal
2020 Volume 18, Page(s) 3402–3414
Abstract: ... questions on spike-ACE2 binding affinity and its neutralization by anti-SARS-CoV monoclonal antibodies (mAbs ... Here, we observed Val-to-Lys417 mutation in the receptor-binding domains (RBD) of SARS-CoV-2 ... angiotensin-converting enzyme 2 (ACE2) and ensure cell recognition. High infectivity of SARS-CoV-2 raises ...
| Abstract | Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which causes coronavirus disease 2019 (COVID-19), is a novel beta coronavirus. SARS-CoV-2 uses spike glycoprotein to interact with host angiotensin-converting enzyme 2 (ACE2) and ensure cell recognition. High infectivity of SARS-CoV-2 raises questions on spike-ACE2 binding affinity and its neutralization by anti-SARS-CoV monoclonal antibodies (mAbs). Here, we observed Val-to-Lys417 mutation in the receptor-binding domains (RBD) of SARS-CoV-2, which established a Lys-Asp electrostatic interaction enhancing its ACE2-binding. Pro-to-Ala475 substitution and Gly482 insertion in the |
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| Keywords | covid19 |
| Language | English |
| Publishing date | 2020-11-12 |
| Publishing country | Netherlands |
| Document type | Journal Article |
| ZDB-ID | 2694435-2 |
| ISSN | 2001-0370 |
| ISSN | 2001-0370 |
| DOI | 10.1016/j.csbj.2020.11.002 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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