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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/8058| Evolving spike-protein N-glycosylation in SARS-CoV-2 variants | |
| Bhavya Singh Patrick Garrett Sabyasachi Baboo Jolene Diedrich Jonathan Torres Jeffrey Copps Andrew Ward James Paulson John Yates | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| https://doi.org/10.1101/2023.05.08.539897 | |
| https://www.biorxiv.org/content/10.1101/2023.05.08.539897v1 | |
| Abstract It has been three years since SARS-CoV-2 emerged and the world plunged into a “once in a century” pandemic. Since then, multiple waves of infection have swept through the human population, led by variants that were able to evade any acquired immunity. The co-evolution of SARS-CoV-2 variants with human immunity provides an excellent opportunity to study the interaction between viral pathogens and their human hosts. The heavily N-glycosylated spike-protein of SARS-CoV-2 plays a pivotal role in initiating infection and is the target for host immune response, both of which are impacted by host-installed N-glycans. We compared the N-glycan landscape of recombinantly expressed, stabilized, soluble spike-protein trimers representing seven of the most prominent SARS-CoV-2 variants and found that N-glycan processing is conserved at most sites. However, in multiple variants, processing of N-glycans from high mannose-to complex-type is reduced at sites N165, N343 and N616, implicated in spike-protein function. | |
| bioRxiv | |
| 09-05-2023 | |
| Preimpreso | |
| Inglés | |
| Público en general | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Materiales de Consulta y Comunicados Técnicos |
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| Fichero | Tamaño | Formato | |
|---|---|---|---|
| Evolving spike-protein N-glycosylation in SARS-CoV-2 variants.pdf | 1.35 MB | Adobe PDF | Visualizar/Abrir |