Author: Yasunori Watanabe; Joel D. Allen; Daniel Wrapp; Jason S. McLellan; Max Crispin
Title: Site-specific analysis of the SARS-CoV-2 glycan shield Document date: 2020_3_28
ID: 63j4qc7d_1
Snippet: Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative pathogen of COVID-19 1,2 , induces fever, severe respiratory illness and pneumonia. SARS-CoV-2 utilizes an extensively glycosylated spike (S) protein that protrudes from the viral surface to bind to angiotensin-converting enzyme 2 (ACE2), the host cell receptor, to mediate cell entry 3 . The S protein is a trimeric class I fusion protein that is composed of two functional.....
Document: Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative pathogen of COVID-19 1,2 , induces fever, severe respiratory illness and pneumonia. SARS-CoV-2 utilizes an extensively glycosylated spike (S) protein that protrudes from the viral surface to bind to angiotensin-converting enzyme 2 (ACE2), the host cell receptor, to mediate cell entry 3 . The S protein is a trimeric class I fusion protein that is composed of two functional subunits responsible for receptor binding (S1 subunit) and membrane fusion (S2 subunit). Remarkably, the surface of the virally encoded envelope spike is dominated by an array of host-derived glycans with each trimer displaying 66 N-linked glycosylation sites. This extensive glycosylation has important implications for vaccine design.
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