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The Journal of Biological Chemistry logoLink to The Journal of Biological Chemistry
. 2019 Apr 5;294(14):5735. doi: 10.1074/jbc.AAC119.008421

Correction: Complementary recognition of the receptor-binding site of highly pathogenic H5N1 influenza viruses by two human neutralizing antibodies.

Yanan Zuo, Pengfei Wang, Jianfeng Sun, Shichun Guo, Guiqin Wang, Teng Zuo, Shilong Fan, Paul Zhou, Mifang Liang, Xuanling Shi, Xinquan Wang, Linqi Zhang
PMCID: PMC6462513  PMID: 30952830

VOLUME 293 (2018) PAGES 16503–16517

Leu-194 was mistakenly written as Leu-104.

“Another hydrophobic residue, Pro-106, and the aromatic residue Tyr-107 of FLD21.140 interacted with HA residues Trp-153 and Leu-104 through hydrophobic and van der Waals interactions, respectively. Furthermore, residue Pro-106 inserted its side chain into the hydrophobic receptor-binding pocket surrounded by residues Trp-153 and Leu-104 in the 190-helix of RBS (Fig. 1D and Table S3). Both residues were highly conserved, being present in 99.9 and 95.7% of 3758 influenza H5 HA sequences currently available in the Influenza Virus Database at the National Center for Biotechnology Information, respectively (Table S4). As shown previously (50), the contact residues Val-135, Ser-137, Trp-153, and Leu-104 were also involved in the interaction with the sialoglycan receptor analog, suggesting that FLD21.140 and AVFluIgG03 exert their neutralizing activities through direct competition with the sialic acid receptor (Fig. 1, D–F, and Table S3).”

should read as

“Another hydrophobic residue, Pro-106, and the aromatic residue Tyr-107 of FLD21.140 interacted with HA residues Trp-153 and Leu-194 through hydrophobic and van der Waals interactions, respectively. Furthermore, residue Pro-106 inserted its side chain into the hydrophobic receptor-binding pocket surrounded by residues Trp-153 and Leu-194 in the 190-helix of RBS (Fig. 1D and Table S3). Both residues were highly conserved, being present in 99.9 and 95.7% of 3758 influenza H5 HA sequences currently available in the Influenza Virus Database at the National Center for Biotechnology Information, respectively (Table S4). As shown previously (50), the contact residues Val-135, Ser-137, Trp-153, and Leu-194 were also involved in the interaction with the sialoglycan receptor analog, suggesting that FLD21.140 and AVFluIgG03 exert their neutralizing activities through direct competition with the sialic acid receptor (Fig. 1, D–F, and Table S3).”

This error has now been corrected and does not affect the results or conclusions of this work.


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