Structural Characterization of the Hemagglutinin Receptor Specificity from the 2009 H1N1 Influenza Pandemic

Xu, Rui; McBride, Ryan; Nycholat, Corwin M.; Paulson, James C.; Wilson, Ian A.

doi:10.1128/jvi.06322-11

Cited by 167 publications

(185 citation statements)

References 47 publications

(98 reference statements)

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“…We and others have shown that the D222G change increased virus binding to ␣2,3-linked sialic acid (10,28). However, the receptor binding assay using resialylated red blood cells showed that the viruses with N125D, D127E, or K209E changes remain predominantly bound to ␣2,6-linked sialic acid receptors, consistent with other glycan binding reports (23,29,30). Possibly, the current in vitro methods failed to detect the differences in the receptor binding caused by these changes.…”

Section: Discussionsupporting

confidence: 66%

Identification of Critical Residues in the Hemagglutinin and Neuraminidase of Influenza Virus H1N1pdm for Vaccine Virus Replication in Embryonated Chicken Eggs

Wang

Cotter

et al. 2013

J Virol

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Section: Discussionsupporting

confidence: 66%

Identification of Critical Residues in the Hemagglutinin and Neuraminidase of Influenza Virus H1N1pdm for Vaccine Virus Replication in Embryonated Chicken Eggs

Wang

Cotter

et al. 2013

J Virol

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“…5e), the hydrogen bond bridge could create an unfavourable hydrophilic environment for the exposed hydrophobic glycosidic linkage of the human receptor. Alternatively, as R137 forms a hydrogen bond with the 220-loop, it may stabilize the loop so that it favours binding to the avian receptor more than the human receptor 21,22 .…”

Section: Resultsmentioning

confidence: 99%

Structural basis for preferential avian receptor binding by the human-infecting H10N8 avian influenza virus

Wang

Zhang

et al. 2015

Nat Commun

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Since December 2013, at least three cases of human infections with H10N8 avian influenza virus have been reported in China, two of them being fatal. To investigate the epidemic potential of H10N8 viruses, we examined the receptor binding property of the first human isolate, A/Jiangxi-Donghu/346/2013 (JD-H10N8), and determined the structures of its haemagglutinin (HA) in complex with both avian and human receptor analogues. Our results suggest that JD-H10N8 preferentially binds the avian receptor and that residue R137-localized within the receptor-binding site of HA-plays a key role in this preferential binding. Compared with the H7N9 avian influenza viruses, JD-H10N8 did not exhibit the enhanced binding to human receptors observed with the prevalent H7N9 virus isolate Anhui-1, but resembled the receptor binding activity of the early-outbreak H7N9 isolate (Shanghai-1). We conclude that the H10N8 virus is a typical avian influenza virus.

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“…Similarly, in published HA-3=-SLN structures, it was also found that only the first two saccharides, Sia-1 and Gal-2, form hydrogen bonds with HA, but not with GlcNAc-3 (7). Avian-like glycans adopt a trans conformation of the ␣2-3 sialoside linkages (4), and it seems that only the first two saccharides, Sia-1 and Gal-2, are required for binding to NA, as found in HA-receptor complexes (reviewed in reference 7) and some recent structures (14,33,36).…”

Section: 60-å Resolution By Molecular Replacement (See Materials Andmentioning

confidence: 99%

Influenza Virus Neuraminidases with Reduced Enzymatic Activity That Avidly Bind Sialic Acid Receptors

Zhu

McBride

Nycholat

et al. 2012

J Virol

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Influenza virus neuraminidase (NA) cleaves off sialic acid from cellular receptors of hemagglutinin (HA) to enable progeny escape from infected cells. However, NA variants (D151G) of recent human H3N2 viruses have also been reported to bind receptors on red blood cells, but the nature of these receptors and the effect of the mutation on NA activity were not established. Here, we compare the functional and structural properties of a human H3N2 NA from A/Tanzania/205/2010 and its D151G mutant, which supports HA-independent receptor binding. While the wild-type NA efficiently cleaves sialic acid from both ␣2-6-and ␣2-3-linked glycans, the mutant exhibits much reduced enzymatic activity toward both types of sialosides. Conversely, while wild-type NA shows no detectable binding to sialosides, the D151G NA exhibits avid binding with broad specificity toward ␣2-3 sialosides. D151G NA binds the 3= sialyllactosamine (3=-SLN) and 6=-SLN sialosides with equilibrium dissociation constant (K D ) values of 30.0 M and 645 M, respectively, which correspond to much higher affinities than the corresponding affinities (low mM) of HA to these glycans. Crystal structures of wild-type and mutant NAs reveal the structural basis for glycan binding in the active site by exclusively impairing the glycosidic bond hydrolysis step. The general significance of D151 among influenza virus NAs was further explored by introducing the D151G mutation into three N1 NAs and one N2 NA, which all exhibited reduced enzymatic activity and preferential binding to ␣2-3 sialosides. Since the enzymatic and binding activities of NAs are not routinely assessed, the potential for NA receptor binding to contribute to influenza virus biology may be underappreciated.

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Structural Characterization of the Hemagglutinin Receptor Specificity from the 2009 H1N1 Influenza Pandemic

Cited by 167 publications

References 47 publications

Identification of Critical Residues in the Hemagglutinin and Neuraminidase of Influenza Virus H1N1pdm for Vaccine Virus Replication in Embryonated Chicken Eggs

Identification of Critical Residues in the Hemagglutinin and Neuraminidase of Influenza Virus H1N1pdm for Vaccine Virus Replication in Embryonated Chicken Eggs

Structural basis for preferential avian receptor binding by the human-infecting H10N8 avian influenza virus

Influenza Virus Neuraminidases with Reduced Enzymatic Activity That Avidly Bind Sialic Acid Receptors

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