Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4
Summary: Low-pathogenicity avian influenza viruses (LPAIVs) have caused a global concern to public health since the first novel LPAIV H7N9 outbreak occurred. The receptor-binding properties of the viral hemagglutinin are one key factor for efficient transmission and infection in humans. Recent evide...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2017-08-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124717309944 |
| _version_ | 1819026766412382208 |
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| author | Hao Song Jianxun Qi Haixia Xiao Yuhai Bi Wei Zhang Ying Xu Fei Wang Yi Shi George F. Gao |
| author_facet | Hao Song Jianxun Qi Haixia Xiao Yuhai Bi Wei Zhang Ying Xu Fei Wang Yi Shi George F. Gao |
| author_sort | Hao Song |
| collection | DOAJ |
| description | Summary: Low-pathogenicity avian influenza viruses (LPAIVs) have caused a global concern to public health since the first novel LPAIV H7N9 outbreak occurred. The receptor-binding properties of the viral hemagglutinin are one key factor for efficient transmission and infection in humans. Recent evidence shows that H4 subtype viruses have been widely circulating in domestic poultry and human asymptomatic infections might have occurred. Here, we evaluated the receptor-binding properties of two representative isolates, avian H4N6 (containing Q226 and G228) and swine H4N6 (containing L226 and S228), and found that the avian isolate preferentially binds to avian receptors, whereas the swine isolate preferentially binds to human receptors. The Q226L and G228S substitutions are pivotal for the receptor-binding switch, which resulted in similar human receptor-binding features to the pandemic H2 and H3, implying that H4 has the potential to cause human infections. This early-warning study calls for future extensive surveillance. : The shift in the receptor-binding specificity of avian influenza virus is critical for the jump from avian to human hosts. Based on receptor-binding analysis and structural studies, Song et al. report the mechanisms behind the avian-to-human receptor-binding adaptation by influenza A virus hemagglutinin H4. Keywords: H4 hemagglutinin, influenza virus, receptor binding, crystal structure, host jump, transmission, H4N6 |
| first_indexed | 2024-12-21T05:31:47Z |
| format | Article |
| id | doaj.art-890b5cd0915c4845ab809b9ee05bab42 |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-12-21T05:31:47Z |
| publishDate | 2017-08-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-890b5cd0915c4845ab809b9ee05bab422022-12-21T19:14:31ZengElsevierCell Reports2211-12472017-08-0120512011214Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4Hao Song0Jianxun Qi1Haixia Xiao2Yuhai Bi3Wei Zhang4Ying Xu5Fei Wang6Yi Shi7George F. Gao8Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China; CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, ChinaCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, ChinaLaboratory of Protein Engineering and Vaccines, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China; Center for Influenza Research and Early-Warning (CASCIRE), Chinese Academy of Sciences, Beijing 100101, ChinaCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Center for Influenza Research and Early-Warning (CASCIRE), Chinese Academy of Sciences, Beijing 100101, ChinaCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, ChinaCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, ChinaCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, ChinaCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Center for Influenza Research and Early-Warning (CASCIRE), Chinese Academy of Sciences, Beijing 100101, China; Savaid Medical School, University of Chinese Academy of Sciences, Beijing 101408, ChinaResearch Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China; CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Laboratory of Protein Engineering and Vaccines, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China; Center for Influenza Research and Early-Warning (CASCIRE), Chinese Academy of Sciences, Beijing 100101, China; School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China; Savaid Medical School, University of Chinese Academy of Sciences, Beijing 101408, China; National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China; Corresponding authorSummary: Low-pathogenicity avian influenza viruses (LPAIVs) have caused a global concern to public health since the first novel LPAIV H7N9 outbreak occurred. The receptor-binding properties of the viral hemagglutinin are one key factor for efficient transmission and infection in humans. Recent evidence shows that H4 subtype viruses have been widely circulating in domestic poultry and human asymptomatic infections might have occurred. Here, we evaluated the receptor-binding properties of two representative isolates, avian H4N6 (containing Q226 and G228) and swine H4N6 (containing L226 and S228), and found that the avian isolate preferentially binds to avian receptors, whereas the swine isolate preferentially binds to human receptors. The Q226L and G228S substitutions are pivotal for the receptor-binding switch, which resulted in similar human receptor-binding features to the pandemic H2 and H3, implying that H4 has the potential to cause human infections. This early-warning study calls for future extensive surveillance. : The shift in the receptor-binding specificity of avian influenza virus is critical for the jump from avian to human hosts. Based on receptor-binding analysis and structural studies, Song et al. report the mechanisms behind the avian-to-human receptor-binding adaptation by influenza A virus hemagglutinin H4. Keywords: H4 hemagglutinin, influenza virus, receptor binding, crystal structure, host jump, transmission, H4N6http://www.sciencedirect.com/science/article/pii/S2211124717309944 |
| spellingShingle | Hao Song Jianxun Qi Haixia Xiao Yuhai Bi Wei Zhang Ying Xu Fei Wang Yi Shi George F. Gao Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4 Cell Reports |
| title | Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4 |
| title_full | Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4 |
| title_fullStr | Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4 |
| title_full_unstemmed | Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4 |
| title_short | Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4 |
| title_sort | avian to human receptor binding adaptation by influenza a virus hemagglutinin h4 |
| url | http://www.sciencedirect.com/science/article/pii/S2211124717309944 |
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