New England harbor seal H3N8 influenza virus retains avian-like receptor specificity
An influenza H3N8 virus, carrying mammalian adaptation mutations, was isolated from New England harbor seals in 2011. We sought to assess the risk of its human transmissibility using two complementary approaches. First, we tested the binding of recombinant hemagglutinin (HA) proteins of seal H3N8 an...
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| Format: | Article |
| Language: | en_US |
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Nature Publishing Group
2016
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| Online Access: | http://hdl.handle.net/1721.1/101878 https://orcid.org/0000-0002-1288-9965 https://orcid.org/0000-0002-2085-7840 https://orcid.org/0000-0002-6747-7765 https://orcid.org/0000-0003-0041-5989 https://orcid.org/0000-0002-6528-0125 https://orcid.org/0000-0002-6977-7403 |
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| author | Krammer, Florian Estrin, Michael Viswanathan, Karthik Stebbins, Nathan W. Sasisekharan, Ram Runstadler, Jonathan Hussein, Islam Ma, Eric Jinglong Quinlan, Devin Scott |
| author2 | Massachusetts Institute of Technology. Department of Biological Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Biological Engineering Krammer, Florian Estrin, Michael Viswanathan, Karthik Stebbins, Nathan W. Sasisekharan, Ram Runstadler, Jonathan Hussein, Islam Ma, Eric Jinglong Quinlan, Devin Scott |
| author_sort | Krammer, Florian |
| collection | MIT |
| description | An influenza H3N8 virus, carrying mammalian adaptation mutations, was isolated from New England harbor seals in 2011. We sought to assess the risk of its human transmissibility using two complementary approaches. First, we tested the binding of recombinant hemagglutinin (HA) proteins of seal H3N8 and human-adapted H3N2 viruses to respiratory tissues of humans and ferrets. For human tissues, we observed strong tendency of the seal H3 to bind to lung alveoli, which was in direct contrast to the human-adapted H3 that bound mainly to the trachea. This staining pattern was also consistent in ferrets, the primary animal model for human influenza pathogenesis. Second, we compared the binding of the recombinant HAs to a library of 610 glycans. In contrast to the human H3, which bound almost exclusively to α-2,6 sialylated glycans, the seal H3 bound preferentially to α-2,3 sialylated glycans. Additionally, the seal H3N8 virus replicated in human lung carcinoma cells. Our data suggest that the seal H3N8 virus has retained its avian-like receptor binding specificity, but could potentially establish infection in human lungs. |
| first_indexed | 2024-09-23T10:20:13Z |
| format | Article |
| id | mit-1721.1/101878 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T10:20:13Z |
| publishDate | 2016 |
| publisher | Nature Publishing Group |
| record_format | dspace |
| spelling | mit-1721.1/1018782022-09-26T17:19:05Z New England harbor seal H3N8 influenza virus retains avian-like receptor specificity Krammer, Florian Estrin, Michael Viswanathan, Karthik Stebbins, Nathan W. Sasisekharan, Ram Runstadler, Jonathan Hussein, Islam Ma, Eric Jinglong Quinlan, Devin Scott Massachusetts Institute of Technology. Department of Biological Engineering Massachusetts Institute of Technology. Division of Comparative Medicine Massachusetts Institute of Technology. School of Engineering Koch Institute for Integrative Cancer Research at MIT Hussein, Islam Ma, Eric Jinglong Estrin, Michael Viswanathan, Karthik Stebbins, Nathan W. Quinlan, Devin Scott Sasisekharan, Ram Runstadler, Jonathan An influenza H3N8 virus, carrying mammalian adaptation mutations, was isolated from New England harbor seals in 2011. We sought to assess the risk of its human transmissibility using two complementary approaches. First, we tested the binding of recombinant hemagglutinin (HA) proteins of seal H3N8 and human-adapted H3N2 viruses to respiratory tissues of humans and ferrets. For human tissues, we observed strong tendency of the seal H3 to bind to lung alveoli, which was in direct contrast to the human-adapted H3 that bound mainly to the trachea. This staining pattern was also consistent in ferrets, the primary animal model for human influenza pathogenesis. Second, we compared the binding of the recombinant HAs to a library of 610 glycans. In contrast to the human H3, which bound almost exclusively to α-2,6 sialylated glycans, the seal H3 bound preferentially to α-2,3 sialylated glycans. Additionally, the seal H3N8 virus replicated in human lung carcinoma cells. Our data suggest that the seal H3N8 virus has retained its avian-like receptor binding specificity, but could potentially establish infection in human lungs. National Institute of Allergy and Infectious Diseases (U.S.). Centers of Excellence for Influenza Research and Surveillance and Research on Influenza Pathogenesis (NIAID HHSN266200700010C) 2016-03-28T14:09:42Z 2016-03-28T14:09:42Z 2016-02 2015-05 Article http://purl.org/eprint/type/JournalArticle 2045-2322 http://hdl.handle.net/1721.1/101878 Hussein, Islam T. M., Florian Krammer, Eric Ma, Michael Estrin, Karthik Viswanathan, Nathan W. Stebbins, Devin S. Quinlan, Ram Sasisekharan, and Jonathan Runstadler. “New England Harbor Seal H3N8 Influenza Virus Retains Avian-Like Receptor Specificity.” Scientific Reports 6 (February 18, 2016): 21428. https://orcid.org/0000-0002-1288-9965 https://orcid.org/0000-0002-2085-7840 https://orcid.org/0000-0002-6747-7765 https://orcid.org/0000-0003-0041-5989 https://orcid.org/0000-0002-6528-0125 https://orcid.org/0000-0002-6977-7403 en_US http://dx.doi.org/10.1038/srep21428 Scientific Reports Creative Commons Attribution http://creativecommons.org/licenses/by/4.0/ application/pdf Nature Publishing Group Nature Publishing Group |
| spellingShingle | Krammer, Florian Estrin, Michael Viswanathan, Karthik Stebbins, Nathan W. Sasisekharan, Ram Runstadler, Jonathan Hussein, Islam Ma, Eric Jinglong Quinlan, Devin Scott New England harbor seal H3N8 influenza virus retains avian-like receptor specificity |
| title | New England harbor seal H3N8 influenza virus retains avian-like receptor specificity |
| title_full | New England harbor seal H3N8 influenza virus retains avian-like receptor specificity |
| title_fullStr | New England harbor seal H3N8 influenza virus retains avian-like receptor specificity |
| title_full_unstemmed | New England harbor seal H3N8 influenza virus retains avian-like receptor specificity |
| title_short | New England harbor seal H3N8 influenza virus retains avian-like receptor specificity |
| title_sort | new england harbor seal h3n8 influenza virus retains avian like receptor specificity |
| url | http://hdl.handle.net/1721.1/101878 https://orcid.org/0000-0002-1288-9965 https://orcid.org/0000-0002-2085-7840 https://orcid.org/0000-0002-6747-7765 https://orcid.org/0000-0003-0041-5989 https://orcid.org/0000-0002-6528-0125 https://orcid.org/0000-0002-6977-7403 |
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