Author Correction: Multivalent 9-O-Acetylated-sialic acid glycoclusters as potent inhibitors for SARS-CoV-2 infection

Simon J.L. Petitjean, Wenzhang Chen, Melanie Koehler, Ravikumar Jimmidi, Jinsung Yang, Danahe Mohammed, Blinera Juniku, Megan L. Stanifer, Steeve Boulant, Stéphane P. Vincent, David Alsteens

Research output: Contribution to journalComment/debatepeer-review

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Abstract

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. The deleted text is reproduced below: 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.

Original languageEnglish
Article number3611
JournalNature Communications
Volume13
Issue number1
DOIs
Publication statusPublished - Dec 2022

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