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- Ariane Sternberg and Cord Naujokat.
- Center and Network for Targeted Oncology, Muehlackerweg 8, D-69239 Heidelberg, Germany.
- Life Sci. 2020 Sep 15; 257: 118056.
AbstractVarious human pathogenic viruses employ envelope glycoproteins for host cell receptor recognition and binding, membrane fusion and viral entry. The spike (S) glycoprotein of betacoronavirus SARS-CoV-2 is a homotrimeric class I fusion protein that exists in a metastable conformation for cleavage by host cell proteases furin and TMPRSS2, thereby undergoing substantial structural rearrangement for ACE2 host cell receptor binding and subsequent viral entry by membrane fusion. The S protein is densely decorated with N-linked glycans protruding from the trimer surface that affect S protein folding, processing by host cell proteases and the elicitation of humoral immune response. Deep insight into the sophisticated structure of SARS-CoV-2 S protein may provide a blueprint for vaccination strategies, as reviewed herein.Copyright © 2020 Elsevier Inc. All rights reserved.
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