Correction: Complementary recognition of the receptor-binding site of highly pathogenic H5N1 influenza viruses by two human neutralizing antibodies. [Additions and Corrections] (Journal of Biological Chemistry)

VOLUME 293 (2018) PAGES 16503-16517Leu-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...