Role of Spike Protein Endodomains in Regulating Coronavirus Entry *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 284, Issue: 47, Page: 32725-32734
2009
- 57Citations
- 75Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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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
- Citations57
- Citation Indexes57
- 57
- CrossRef49
- Captures75
- Readers75
- 75
Article Description
Enveloped viruses enter cells by viral glycoprotein-mediated binding to host cells and subsequent fusion of virus and host cell membranes. For the coronaviruses, viral spike (S) proteins execute these cell entry functions. The S proteins are set apart from other viral and cellular membrane fusion proteins by their extensively palmitoylated membrane-associated tails. Palmitate adducts are generally required for protein-mediated fusions, but their precise roles in the process are unclear. To obtain additional insights into the S-mediated membrane fusion process, we focused on these acylated carboxyl-terminal intravirion tails. Substituting alanines for the cysteines that are subject to palmitoylation had effects on both S incorporation into virions and S-mediated membrane fusions. In specifically dissecting the effects of endodomain mutations on the fusion process, we used antiviral heptad repeat peptides that bind only to folding intermediates in the S-mediated fusion process and found that mutants lacking three palmitoylated cysteines remained in transitional folding states nearly 10 times longer than native S proteins. This slower refolding was also reflected in the paucity of postfusion six-helix bundle configurations among the mutant S proteins. Viruses with fewer palmitoylated S protein cysteines entered cells slowly and had reduced specific infectivities. These findings indicate that lipid adducts anchoring S proteins into virus membranes are necessary for the rapid, productive S protein refolding events that culminate in membrane fusions. These studies reveal a previously unappreciated role for covalently attached lipids on the endodomains of viral proteins eliciting membrane fusion reactions.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820378662; http://dx.doi.org/10.1074/jbc.m109.043547; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=70450231625&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/19801669; http://www.jbc.org/lookup/doi/10.1074/jbc.M109.043547; https://syndication.highwire.org/content/doi/10.1074/jbc.M109.043547; https://linkinghub.elsevier.com/retrieve/pii/S0021925820378662; https://dx.doi.org/10.1074/jbc.m109.043547
American Society for Biochemistry & Molecular Biology (ASBMB)
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