Structural insights in cell-type specific evolution of intra-host diversity by SARS-CoV-2
| العنوان: | Structural insights in cell-type specific evolution of intra-host diversity by SARS-CoV-2 |
|---|---|
| المؤلفون: | Kapil Gupta, Christine Toelzer, Maia Kavanagh Williamson, Deborah K. Shoemark, A. Sofia F. Oliveira, David A. Matthews, Abdulaziz Almuqrin, Oskar Staufer, Sathish K. N. Yadav, Ufuk Borucu, Frederic Garzoni, Daniel Fitzgerald, Joachim Spatz, Adrian J. Mulholland, Andrew D. Davidson, Christiane Schaffitzel, Imre Berger |
| المصدر: | Nature Communications Gupta, K, Toelzer, C, Kavanagh Williamson, M, Shoemark, D K, Oliveira, A, Davidson, A D, Almuqrin, A M, Staufer, O, Yadav Kadapalakere, S, Borucu, U, Garzoni, F, Fitzgerald, D J, Spatz, J P, Mulholland, A J, Davidson, A D, Berger-Schaffitzel, C H & Berger, I 2022, ' Structural insights in cell-type specific evolution of intra-host diversity by SARS-CoV-2 ', Nature Communications, vol. 13, no. 1, 222 . https://doi.org/10.1038/s41467-021-27881-6Test Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022) |
| سنة النشر: | 2022 |
| مصطلحات موضوعية: | Protein Conformation, Science, viruses, UNCOVER, General Physics and Astronomy, Molecular Dynamics Simulation, General Biochemistry, Genetics and Molecular Biology, Article, Cell Line, Evolution, Molecular, Linoleic Acid, Max Planck Bristol, Animals, Humans, Furin, Multidisciplinary, SARS-CoV-2, Bristol BioDesign Institute, Cryoelectron Microscopy, virus diseases, COVID-19, Covid19, General Chemistry, Virus Internalization, Viral proteins, Viral Tropism, Mutation, Spike Glycoprotein, Coronavirus, Molecular modelling, Protein Binding |
| الوصف: | As the global burden of SARS-CoV-2 infections escalates, so does the evolution of viral variants with increased transmissibility and pathology. In addition to this entrenched diversity, RNA viruses can also display genetic diversity within single infected hosts with co-existing viral variants evolving differently in distinct cell types. The BriSΔ variant, originally identified as a viral subpopulation from SARS-CoV-2 isolate hCoV-19/England/02/2020, comprises in the spike an eight amino-acid deletion encompassing a furin recognition motif and S1/S2 cleavage site. We elucidate the structure, function and molecular dynamics of this spike providing mechanistic insight into how the deletion correlates to viral cell tropism, ACE2 receptor binding and infectivity of this SARS-CoV-2 variant. Our results reveal long-range allosteric communication between functional domains that differ in the wild-type and the deletion variant and support a view of SARS-CoV-2 probing multiple evolutionary trajectories in distinct cell types within the same infected host. BriSΔ, a SARS-CoV-2 variant from clinical isolate hCoV/England/02/2020, comprises a deletion in a spike cleavage site. The structure and molecular dynamics of this spike provides mechanistic insights into how the deletion modulates virus infectivity. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::419085f7658a502362a30c9d43b5b890Test https://hdl.handle.net/21.11116/0000-0009-CA25-A21.11116/0000-0009-CA2A-521.11116/0000-0009-CA2B-421.11116/0000-0009-CA2C-321.11116/0000-0009-CA27-821.11116/0000-0009-CA28-721.11116/0000-0009-CA29-6Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....419085f7658a502362a30c9d43b5b890 |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |