Correction to: Nature Communications https://doi.org/10.1038/s41467-022-30313-8, published online 10 May 2022.
The original version of this Article contained a factual error within the discussion section, which incorrectly stated that SARS-CoV-2 expresses a hemagglutinin esterase. This has been corrected in the PDF and HTML version of the Article by the removal of the corresponding text.
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Besides the spike glycoprotein, coronaviruses, including SARS-CoV-2, express at their surface the hemagglutinin esterase (HE) that often contains an active lectin domain that mediates glycan binding in several other viruses. However, the HE lectin domains of HCoV-OC43 and HCoV-HKU1 lost their glycan binding capacity due to mutations and deletion during adaptation to human host62. Our result also suggests that HE might not be directly involved in 9-AcSA binding, as binding kinetics to AcSA is similar on purified S1 and at the virion level. However, as their esterase activity is maintained, HE could be involved in the deacetylation during release of viral progeny from the host cell surface and possibly also for breaking decoy interactions of the S protein with O-AcSA carrying mucins63.
References
Bakkers, M. J. et al. Betacoronavirus adaptation to humans involved progressive loss of hemagglutinin-esterase lectin activity. Cell Host Microbe 21, 356–366 (2017).
Huang, X. et al. Human coronavirus HKU1 spike protein uses O-acetylated sialic acid as an attachment receptor determinant and employs hemagglutinin-esterase protein as a receptor-destroying enzyme. J. Virol. 89, 7202–7213 (2015).
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Petitjean, S.J.L., Chen, W., Koehler, M. et al. Author Correction: Multivalent 9-O-Acetylated-sialic acid glycoclusters as potent inhibitors for SARS-CoV-2 infection. Nat Commun 13, 3611 (2022). https://doi.org/10.1038/s41467-022-31290-8
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DOI: https://doi.org/10.1038/s41467-022-31290-8
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