TY - JOUR
T1 - Author Correction
T2 - Multivalent 9-O-Acetylated-sialic acid glycoclusters as potent inhibitors for SARS-CoV-2 infection
AU - Petitjean, Simon J.L.
AU - Chen, Wenzhang
AU - Koehler, Melanie
AU - Jimmidi, Ravikumar
AU - Yang, Jinsung
AU - Mohammed, Danahe
AU - Juniku, Blinera
AU - Stanifer, Megan L.
AU - Boulant, Steeve
AU - Vincent, Stéphane P.
AU - Alsteens, David
N1 - Publisher Copyright:
© The Author(s) 2022.
PY - 2022/12
Y1 - 2022/12
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85132919043&partnerID=8YFLogxK
U2 - 10.1038/s41467-022-31290-8
DO - 10.1038/s41467-022-31290-8
M3 - Comment/debate
C2 - 35750667
AN - SCOPUS:85132919043
SN - 2041-1723
VL - 13
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 3611
ER -