Avian influenza A (H7N9) virus: from low pathogenic to highly pathogenic

doi:10.1007/s11684-020-0814-5

Front. Med.

2021, Vol. 15

Issue (4) : 507-527 https://doi.org/10.1007/s11684-020-0814-5

REVIEW

Avian influenza A (H7N9) virus: from low pathogenic to highly pathogenic

William J. Liu^1,²(

), Haixia Xiao³, Lianpan Dai⁴, Di Liu^5,^6,^7,⁸, Jianjun Chen^5,^6,^7,⁸, Xiaopeng Qi⁹, Yuhai Bi^1,^4,^7,⁸, Yi Shi^1,^4,^7,⁸, George F. Gao^2,^4,⁹, Yingxia Liu¹(

)

¹. Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People’s Hospital, Shenzhen 518114, China
². National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 102206, China
³. Laboratory of Protein Engineering and Vaccines, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences (CAS), Tianjin 300308, China
⁴. CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China
⁵. CAS Key Laboratory of Special Pathogens and Biosafety, Chinese Academy of Sciences, Wuhan 430071, China
⁶. National Virus Resource Center, Chinese Academy of Sciences, Wuhan 430071, China
⁷. University of Chinese Academy Sciences, Beijing 100049, China
⁸. Center for Influenza Research and Early Warning, Chinese Academy of Sciences, Beijing 100101, China
⁹. Chinese Center for Disease Control and Prevention, Beijing 102206, China

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Abstract

The avian influenza A (H7N9) virus is a zoonotic virus that is closely associated with live poultry markets. It has caused infections in humans in China since 2013. Five waves of the H7N9 influenza epidemic occurred in China between March 2013 and September 2017. H7N9 with low-pathogenicity dominated in the first four waves, whereas highly pathogenic H7N9 influenza emerged in poultry and spread to humans during the fifth wave, causing wide concern. Specialists and officials from China and other countries responded quickly, controlled the epidemic well thus far, and characterized the virus by using new technologies and surveillance tools that were made possible by their preparedness efforts. Here, we review the characteristics of the H7N9 viruses that were identified while controlling the spread of the disease. It was summarized and discussed from the perspectives of molecular epidemiology, clinical features, virulence and pathogenesis, receptor binding, T-cell responses, monoclonal antibody development, vaccine development, and disease burden. These data provide tools for minimizing the future threat of H7N9 and other emerging and re-emerging viruses, such as SARS-CoV-2.

Keywords H7N9 HPAIV epidemiology clinical features pathogenesis hemagglutinin immunity vaccine

Corresponding Author(s): William J. Liu,Yingxia Liu

Just Accepted Date: 03 December 2020 Online First Date: 15 April 2021 Issue Date: 23 September 2021

Cite this article:

William J. Liu,Haixia Xiao,Lianpan Dai, et al. Avian influenza A (H7N9) virus: from low pathogenic to highly pathogenic[J]. Front. Med., 2021, 15(4): 507-527.

URL:

https://academic.hep.com.cn/fmd/EN/10.1007/s11684-020-0814-5
https://academic.hep.com.cn/fmd/EN/Y2021/V15/I4/507

Fig.1 Origin and evolution of H7N9 viruses. (A) Schematic of the origin and dynamic reassortment of H7N9 viruses. The migratory birds, ducks, chickens, and humans involved in the emergence and outbreaks of H7N9 are shown. The dashed line arrow and circle of N9 represent the uncertain presence of N9 in ducks as indicated by a previous study [19]. Colored internal gene names in clouds represent diversified H9N2 gene pools. The specific reassortment of H7N9 with the H5N6 and H6N6 viruses is also shown. HP represents the highly pathogenic H7N9 viruses, which have also caused human infections. (B) Maximum likelihood (ML) trees of the surface genes of the H7N9 viruses in all human infections. Sequences of the surface genes of the H7N9 viruses in all human infections were downloaded from the NCBI Influenza Virus Database and Global Initiative on Sharing All Influenza Data for phylogenetic analysis. ML trees were inferred with the software RAxML under the GTRGAMMA model with 1000 bootstrap replicates by using A/Shanghai/02/2013 as the root. The background colors of the branches show the time at which the corresponding virus was isolated and are classified as waves 1 to 5 and after wave 5. Colored strips far from the tree indicate the regions from which the corresponding viruses were isolated. The Yangtze River Delta region, the Pearl River Delta region, and other regions are labeled in red, blue, and no-color, respectively. HP in the upper panel shows the cluster containing all HP H7N9 isolates.

Fig.2 Radiographic findings in A (H7N9) pneumonia. Chest radiograph (A) and computed tomography scan (B) showing bilateral ground-glass opacities and consolidation.

Tab.1 Clinical characteristics and laboratory results of subjects hospitalized for infection with low pathogenic and highly pathogenic H7N9 during the five waves of the H7N9 epidemic in China

Tab.2 Critical amino acid residues in H7N9 proteins associated with viral virulence in mammals

Fig.3 Diagram of the evolutionary routes of H7N9 HA. H7 HA with different residue combinations at receptor binding sites (G186/Q226, V186/L226, G186/L226, and V186/Q226) are represented by surface sheets and colored cyan, violet, wheat, and orange. SA receptor analogs are shown as sticks and colored on the basis of elements (carbon, yellow; oxygen, red; nitrogen, blue). The positions of residues 186 and 226 are highlighted in purple.

Fig.4 Molecular basis for cross-reactive T cell immunity and immune evasion between the H7N9 and 2009 pH1N1 influenza viruses. (A, B) 2009 pH1N1-derived T cell epitope peptide H1-P22 (PDB code: 4MJ5) and substitution peptide H7-P22 from H7N9 (PDB code: 4MJ6) presented by HLA-A*1101. The peptide-binding groove is shown as the vacuum electrostatic surface potential of the HLA-A*1101 H chain. (C) Alignment of peptides H1-P22 (green) and H7-P22 (yellow). The a1-helix of the HLA-A*1101 H chain is shown as a white spiral ribbon behind the peptide. (D, E) Peptide H1-P25 in pH1N1 (PDB code: 5WWU) and its substitution peptide in H7N9 H7-P25 (PDB code: 5WXD) presented by HLA-A*2402. The peptide binding groove is shown by the vacuum electrostatic surface potential of the HLA-A*2402 H chain. (F) Alignment of peptides H1-P25 (cyan) and H7-P25 (orange). The a1-helix of the HLA-A*2402 H chain is shown as a white spiral ribbon behind the peptide. The names and positions of the conserved residues in the peptides are denoted by black letters and numbers, respectively. Conserved residues are shown with colored sticks. Residue substitutions are shown in underlined bold text in colors corresponding to the peptides. Residue substitutions are shown with colored spheres and sticks.

Tab.3 H7N9 influenza vaccines in clinical development

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