Structures and Receptor Binding of Hemagglutinins from Human-Infecting H7N9 Influenza Viruses

An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor-binding properties of two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature residue Gln²²⁶) and A/Anhui/1/2013 (AH-H7N9) (co...

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Published inScience (American Association for the Advancement of Science) Vol. 342; no. 6155; pp. 243 - 247
Main Authors Shi, Yi, Zhang, Wei, Wang, Fei, Qi, Jianxun, Wu, Ying, Song, Hao, Gao, Feng, Bi, Yuhai, Zhang, Yanfang, Fan, Zheng, Qin, Chengfeng, Sun, Honglei, Liu, Jinhua, Haywood, Joel, Liu, Wenjun, Gong, Weimin, Wang, Dayan, Shu, Yuelong, Wang, Yu, Yan, Jinghua, Gao, George F.
Format Journal Article
LanguageEnglish
Published United States American Association for the Advancement of Science 11.10.2013
The American Association for the Advancement of Science
Subjects
Affinity
amino acid sequences
Amino acids
Animals
Avian flu
avian influenza
Binding
binding sites
Birds
China
Crystallography, X-Ray
Glycine - chemistry
Glycine - genetics
Glycine - metabolism
Hemagglutinin Glycoproteins, Influenza Virus - chemistry
Hemagglutinin Glycoproteins, Influenza Virus - metabolism
hemagglutinins
Human
human diseases
Humans
hydrophobicity
Hydroxyapatite
Influenza
Influenza A virus
Influenza A virus - metabolism
Influenza in Birds - virology
Influenza, Human - virology
mutants
mutation
polysaccharides
Protein Conformation
Receptors
Receptors, Cell Surface - chemistry
Receptors, Cell Surface - genetics
Receptors, Cell Surface - metabolism
virion
Virology
Viruses
China
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Abstract An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor-binding properties of two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature residue Gln²²⁶) and A/Anhui/1/2013 (AH-H7N9) (containing the mammalian-signature residue Leu²²⁶). We found that SH-H7N9 HA preferentially binds the avian receptor analog, whereas AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9 mutant HA (Leu²²⁶ → Gln) was found to exhibit dual receptor-binding property, indicating that other amino acid substitutions contribute to the receptor-binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with either avian or human receptor analogs show how AH-H7N9 can bind human receptors while still retaining the avian receptor-binding property.
AbstractList Two Viruses to BindStructural studies of two different H7N9 influenza viruses isolated from humans-A/Shanghai/1/2013 and A/Anhui/1/2013-which have different amino acid sequences in the receptor binding site, provide data indicating that the virus is in transition with respect to host adaptation. The Shanghai virus was one of the first isolated in humans that binds avian receptor glycans with high affinity, but binds poorly to human receptors. However, the later Anhui isolates can bind both avian and human receptors at high affinity. Shi et al. (p. 243, published online 5 September) show that four hydrophobic mutations contribute to acquisition of affinity for the human receptor by the virus hemagglutinin (HA) and confirm this effect in binding studies with virus particles. Further comparison of a mutant H7N9 A/Anhui/1/2013 HA with the bird flu H5N1 virus revealed the significance of some of the naturally occurring changes observed in circulating H7N9 viruses, which helps to explain how these viruses have been able to cause many severe human infections in a short time.
Two Viruses to Bind Structural studies of two different H7N9 influenza viruses isolated from humans—A/Shanghai/1/2013 and A/Anhui/1/2013—which have different amino acid sequences in the receptor binding site, provide data indicating that the virus is in transition with respect to host adaptation. The Shanghai virus was one of the first isolated in humans that binds avian receptor glycans with high affinity, but binds poorly to human receptors. However, the later Anhui isolates can bind both avian and human receptors at high affinity. Shi et al. (p. 243, published online 5 September) show that four hydrophobic mutations contribute to acquisition of affinity for the human receptor by the virus hemagglutinin (HA) and confirm this effect in binding studies with virus particles. Further comparison of a mutant H7N9 A/Anhui/1/2013 HA with the bird flu H5N1 virus revealed the significance of some of the naturally occurring changes observed in circulating H7N9 viruses, which helps to explain how these viruses have been able to cause many severe human infections in a short time.
An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor-binding properties of two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature residue Gln(226)) and A/Anhui/1/2013 (AH-H7N9) (containing the mammalian-signature residue Leu(226)). We found that SH-H7N9 HA preferentially binds the avian receptor analog, whereas AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9 mutant HA (Leu(226) → Gln) was found to exhibit dual receptor-binding property, indicating that other amino acid substitutions contribute to the receptor-binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with either avian or human receptor analogs show how AH-H7N9 can bind human receptors while still retaining the avian receptor-binding property.
Structural studies of two different H7N9 influenza viruses isolated from humans—A/Shanghai/1/2013 and A/Anhui/1/2013—which have different amino acid sequences in the receptor binding site, provide data indicating that the virus is in transition with respect to host adaptation. The Shanghai virus was one of the first isolated in humans that binds avian receptor glycans with high affinity, but binds poorly to human receptors. However, the later Anhui isolates can bind both avian and human receptors at high affinity. Shi et al. (p. 243 , published online 5 September) show that four hydrophobic mutations contribute to acquisition of affinity for the human receptor by the virus hemagglutinin (HA) and confirm this effect in binding studies with virus particles. Further comparison of a mutant H7N9 A/Anhui/1/2013 HA with the bird flu H5N1 virus revealed the significance of some of the naturally occurring changes observed in circulating H7N9 viruses, which helps to explain how these viruses have been able to cause many severe human infections in a short time. Four amino acids in the H7N9 influenza virus binding site provide a hydrophobic environment for human receptors. An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor–binding properties of two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature residue Gln 226 ) and A/Anhui/1/2013 (AH-H7N9) (containing the mammalian-signature residue Leu 226 ). We found that SH-H7N9 HA preferentially binds the avian receptor analog, whereas AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9 mutant HA (Leu 226 → Gln) was found to exhibit dual receptor-binding property, indicating that other amino acid substitutions contribute to the receptor-binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with either avian or human receptor analogs show how AH-H7N9 can bind human receptors while still retaining the avian receptor–binding property.
Structural studies of two different H7N9 influenza viruses isolated from humans--A/Shanghai/1/2013 and A/Anhui/1/2013--which have different amino acid sequences in the receptor binding site, provide data indicating that the virus is in transition with respect to host adaptation. The Shanghai virus was one of the first isolated in humans that binds avian receptor glycans with high affinity, but binds poorly to human receptors. However, the later Anhui isolates can bind both avian and human receptors at high affinity. Shi et al. (p. 243, published online 5 September) show that four hydrophobic mutations contribute to acquisition of affinity for the human receptor by the virus hemagglutinin (HA) and confirm this effect in binding studies with virus particles. Further comparison of a mutant H7N9 A/Anhui/1/2013 HA with the bird flu H5N1 virus revealed the significance of some of the naturally occurring changes observed in circulating H7N9 viruses, which helps to explain how these viruses have been able to cause many severe human infections in a short time. [PUBLICATION ABSTRACT] An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor-binding properties of two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature residue Gln226) and A/Anhui/1/2013 (AH-H7N9) (containing the mammalian-signature residue Leu226). We found that SH-H7N9 HA preferentially binds the avian receptor analog, whereas AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9 mutant HA (Leu226 [arrow right] Gln) was found to exhibit dual receptor-binding property, indicating that other amino acid substitutions contribute to the receptor-binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with either avian or human receptor analogs show how AH-H7N9 can bind human receptors while still retaining the avian receptor-binding property. [PUBLICATION ABSTRACT]
An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor-binding properties of two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature residue Gln²²⁶) and A/Anhui/1/2013 (AH-H7N9) (containing the mammalian-signature residue Leu²²⁶). We found that SH-H7N9 HA preferentially binds the avian receptor analog, whereas AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9 mutant HA (Leu²²⁶ → Gln) was found to exhibit dual receptor-binding property, indicating that other amino acid substitutions contribute to the receptor-binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with either avian or human receptor analogs show how AH-H7N9 can bind human receptors while still retaining the avian receptor-binding property.
An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor-binding properties of two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature residue Gln(226)) and A/Anhui/1/2013 (AH-H7N9) (containing the mammalian-signature residue Leu(226)). We found that SH-H7N9 HA preferentially binds the avian receptor analog, whereas AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9 mutant HA (Leu(226) → Gln) was found to exhibit dual receptor-binding property, indicating that other amino acid substitutions contribute to the receptor-binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with either avian or human receptor analogs show how AH-H7N9 can bind human receptors while still retaining the avian receptor-binding property.An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor-binding properties of two human H7N9 isolates, A/Shanghai/1/2013 (SH-H7N9) (containing the avian-signature residue Gln(226)) and A/Anhui/1/2013 (AH-H7N9) (containing the mammalian-signature residue Leu(226)). We found that SH-H7N9 HA preferentially binds the avian receptor analog, whereas AH-H7N9 HA binds both avian and human receptor analogs. Furthermore, an AH-H7N9 mutant HA (Leu(226) → Gln) was found to exhibit dual receptor-binding property, indicating that other amino acid substitutions contribute to the receptor-binding switch. The structures of SH-H7N9 HA, AH-H7N9 HA, and its mutant in complex with either avian or human receptor analogs show how AH-H7N9 can bind human receptors while still retaining the avian receptor-binding property.
Author Shi, Yi
Qin, Chengfeng
Wang, Yu
Zhang, Wei
Sun, Honglei
Qi, Jianxun
Zhang, Yanfang
Liu, Wenjun
Wang, Fei
Song, Hao
Bi, Yuhai
Haywood, Joel
Gao, George F.
Wang, Dayan
Liu, Jinhua
Wu, Ying
Gao, Feng
Gong, Weimin
Yan, Jinghua
Fan, Zheng
Shu, Yuelong
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  surname: Gao
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/24009358$$D View this record in MEDLINE/PubMed
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Snippet An avian-origin human-infecting influenza (H7N9) virus was recently identified in China. We have evaluated the viral hemagglutinin (HA) receptor-binding...
Structural studies of two different H7N9 influenza viruses isolated from humans—A/Shanghai/1/2013 and A/Anhui/1/2013—which have different amino acid sequences...
Structural studies of two different H7N9 influenza viruses isolated from humans--A/Shanghai/1/2013 and A/Anhui/1/2013--which have different amino acid...
Two Viruses to BindStructural studies of two different H7N9 influenza viruses isolated from humans-A/Shanghai/1/2013 and A/Anhui/1/2013-which have different...
Two Viruses to Bind Structural studies of two different H7N9 influenza viruses isolated from humans—A/Shanghai/1/2013 and A/Anhui/1/2013—which have different...
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SubjectTerms Affinity
amino acid sequences
Amino acids
Animals
Avian flu
avian influenza
Binding
binding sites
Birds
China
Crystallography, X-Ray
Glycine - chemistry
Glycine - genetics
Glycine - metabolism
Hemagglutinin Glycoproteins, Influenza Virus - chemistry
Hemagglutinin Glycoproteins, Influenza Virus - metabolism
hemagglutinins
Human
human diseases
Humans
hydrophobicity
Hydroxyapatite
Influenza
Influenza A virus
Influenza A virus - metabolism
Influenza in Birds - virology
Influenza, Human - virology
mutants
mutation
polysaccharides
Protein Conformation
Receptors
Receptors, Cell Surface - chemistry
Receptors, Cell Surface - genetics
Receptors, Cell Surface - metabolism
virion
Virology
Viruses
Title Structures and Receptor Binding of Hemagglutinins from Human-Infecting H7N9 Influenza Viruses
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