Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin
The advent of H7N9 in early 2013 is of concern for a number of reasons, including its capability to infect humans, the lack of clarity in the etiology of infection, and because the human population does not have pre-existing immunity to the H7 subtype. Earlier sequence analyses of H7N9 hemagglutinin...
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| Format: | Article |
| Language: | en_US |
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Elsevier B.V.
2014
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| Online Access: | http://hdl.handle.net/1721.1/89160 https://orcid.org/0000-0002-1288-9965 https://orcid.org/0000-0001-9344-0205 https://orcid.org/0000-0002-2085-7840 https://orcid.org/0000-0002-6528-0125 |
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| author | Tharakaraman, Kannan Jayaraman, Akila Raman, Rahul Viswanathan, Karthik Stebbins, Nathan W. Johnson, David Alan Shriver, Zachary H. Sasisekharan, Ram Stebbins, Nathan W. Sasisekharan, Viswanathan |
| author2 | Massachusetts Institute of Technology. Department of Biological Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Biological Engineering Tharakaraman, Kannan Jayaraman, Akila Raman, Rahul Viswanathan, Karthik Stebbins, Nathan W. Johnson, David Alan Shriver, Zachary H. Sasisekharan, Ram Stebbins, Nathan W. Sasisekharan, Viswanathan |
| author_sort | Tharakaraman, Kannan |
| collection | MIT |
| description | The advent of H7N9 in early 2013 is of concern for a number of reasons, including its capability to infect humans, the lack of clarity in the etiology of infection, and because the human population does not have pre-existing immunity to the H7 subtype. Earlier sequence analyses of H7N9 hemagglutinin (HA) point to amino acid changes that predicted human receptor binding and impinge on the antigenic characteristics of the HA. Here, we report that the H7N9 HA shows limited binding to human receptors; however, should a single amino acid mutation occur, this would result in structural changes within the receptor binding site that allow for extensive binding to human receptors present in the upper respiratory tract. Furthermore, a subset of the H7N9 HA sequences demarcating coevolving amino acids appears to be in the antigenic regions of H7, which, in turn, could impact effectiveness of the current WHO-recommended prepandemic H7 vaccines. |
| first_indexed | 2024-09-23T14:18:31Z |
| format | Article |
| id | mit-1721.1/89160 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T14:18:31Z |
| publishDate | 2014 |
| publisher | Elsevier B.V. |
| record_format | dspace |
| spelling | mit-1721.1/891602022-09-29T08:33:13Z Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin Tharakaraman, Kannan Jayaraman, Akila Raman, Rahul Viswanathan, Karthik Stebbins, Nathan W. Johnson, David Alan Shriver, Zachary H. Sasisekharan, Ram Stebbins, Nathan W. Sasisekharan, Viswanathan Massachusetts Institute of Technology. Department of Biological Engineering Singapore-MIT Alliance in Research and Technology (SMART) Koch Institute for Integrative Cancer Research at MIT Tharakaraman, Kannan Jayaraman, Akila Raman, Rahul Viswanathan, Karthik Stebbins, Nathan W. Johnson, David Alan Shriver, Zachary H. Sasisekharan, V. Sasisekharan, Ram The advent of H7N9 in early 2013 is of concern for a number of reasons, including its capability to infect humans, the lack of clarity in the etiology of infection, and because the human population does not have pre-existing immunity to the H7 subtype. Earlier sequence analyses of H7N9 hemagglutinin (HA) point to amino acid changes that predicted human receptor binding and impinge on the antigenic characteristics of the HA. Here, we report that the H7N9 HA shows limited binding to human receptors; however, should a single amino acid mutation occur, this would result in structural changes within the receptor binding site that allow for extensive binding to human receptors present in the upper respiratory tract. Furthermore, a subset of the H7N9 HA sequences demarcating coevolving amino acids appears to be in the antigenic regions of H7, which, in turn, could impact effectiveness of the current WHO-recommended prepandemic H7 vaccines. National Institutes of Health (U.S.) (grant R37 GM05707313) Singapore. National Research Foundation (Singapore MIT Alliance for Research and Technology, Infectious Disease IRG) 2014-09-03T19:10:22Z 2014-09-03T19:10:22Z 2013-06 2013-05 Article http://purl.org/eprint/type/JournalArticle 00928674 http://hdl.handle.net/1721.1/89160 Tharakaraman, Kannan, Akila Jayaraman, Rahul Raman, Karthik Viswanathan, Nathan W. Stebbins, David Johnson, Zachary Shriver, V. Sasisekharan, and Ram Sasisekharan. “Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin.” Cell 153, no. 7 (June 2013): 1486–1493. © 2013 Elsevier B.V. https://orcid.org/0000-0002-1288-9965 https://orcid.org/0000-0001-9344-0205 https://orcid.org/0000-0002-2085-7840 https://orcid.org/0000-0002-6528-0125 en_US http://dx.doi.org/10.1016/j.cell.2013.05.034 Cell Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf Elsevier B.V. Elsevier Open Archive |
| spellingShingle | Tharakaraman, Kannan Jayaraman, Akila Raman, Rahul Viswanathan, Karthik Stebbins, Nathan W. Johnson, David Alan Shriver, Zachary H. Sasisekharan, Ram Stebbins, Nathan W. Sasisekharan, Viswanathan Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin |
| title | Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin |
| title_full | Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin |
| title_fullStr | Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin |
| title_full_unstemmed | Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin |
| title_short | Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin |
| title_sort | glycan receptor binding of the influenza a virus h7n9 hemagglutinin |
| url | http://hdl.handle.net/1721.1/89160 https://orcid.org/0000-0002-1288-9965 https://orcid.org/0000-0001-9344-0205 https://orcid.org/0000-0002-2085-7840 https://orcid.org/0000-0002-6528-0125 |
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