Glycans of SARS-CoV-2 Spike Protein in Virus Infection and Antibody Production
Frontiers in Molecular Biosciences, ISSN: 2296-889X, Vol: 8, Page: 629873
2021
- 75Citations
- 151Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations75
- Citation Indexes70
- 70
- Patent Family Citations5
- Patent Families5
- Captures151
- Readers151
- 151
Review Description
Viral protein glycosylation represents a successful strategy employed by the parasite to take advantage of host–cell machinery for modification of its own proteins. The resulting glycans have unneglectable roles in viral infection and immune response. The spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which presents on the surface of matured virion and mediates viral entry into the host, also undergoes extensive glycosylation to shield it from the human defense system. It is believed that the ongoing COVID-19 pandemic with more than 90,000,000 infections and 1,900,000 deaths is partly due to its successful glycosylation strategy. On the other hand, while glycan patches on S protein have been reported to shield the host immune response by masking “nonself” viral peptides with “self-glycans,” the epitopes are also important in eliciting neutralizing antibodies. In this review, we will summarize the roles of S protein glycans in mediating virus–receptor interactions, and in antibody production, as well as indications for vaccine development.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85104999138&origin=inward; http://dx.doi.org/10.3389/fmolb.2021.629873; http://www.ncbi.nlm.nih.gov/pubmed/33928117; https://www.frontiersin.org/articles/10.3389/fmolb.2021.629873/full; https://dx.doi.org/10.3389/fmolb.2021.629873; https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2021.629873/full
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