Glycosylation at Asn[supscript 91] of H1N1 haemagglutinin affects binding to glycan receptors
The glycoprotein HA (haemagglutinin) on the surface of influenza A virus plays a central role in recognition and binding to specific host cell-surface glycan receptors and in fusion of viral membrane to the host nuclear membrane during viral replication. Given the abundance of HA on the viral surfac...
| Main Authors: | , , , , , , |
|---|---|
| Other Authors: | |
| Format: | Article |
| Language: | en_US |
| Published: |
Portland Press
2013
|
| Online Access: | http://hdl.handle.net/1721.1/76307 https://orcid.org/0000-0002-1288-9965 https://orcid.org/0000-0001-9344-0205 https://orcid.org/0000-0002-2085-7840 |
| _version_ | 1826213139597754368 |
|---|---|
| author | Jayaraman, Akila Koh, Xiaoying Li, Jing Raman, Rahul Viswanathan, Karthik Shriver, Zachary H. Sasisekharan, Ram |
| author2 | Harvard University--MIT Division of Health Sciences and Technology |
| author_facet | Harvard University--MIT Division of Health Sciences and Technology Jayaraman, Akila Koh, Xiaoying Li, Jing Raman, Rahul Viswanathan, Karthik Shriver, Zachary H. Sasisekharan, Ram |
| author_sort | Jayaraman, Akila |
| collection | MIT |
| description | The glycoprotein HA (haemagglutinin) on the surface of influenza A virus plays a central role in recognition and binding to specific host cell-surface glycan receptors and in fusion of viral membrane to the host nuclear membrane during viral replication. Given the abundance of HA on the viral surface, this protein is also the primary target for host innate and adaptive immune responses. Although addition of glycosylation sites on HA are a part of viral evolution to evade the host immune responses, there are specific glycosylation sites that are conserved during most of the evolution of the virus. In the present study, it was demonstrated that one such conserved glycosylation site at Asn[superscript 91] in H1N1 HA critically governs the glycan receptor-binding specificity and hence would potentially impinge on the host adaptation of the virus. |
| first_indexed | 2024-09-23T15:43:58Z |
| format | Article |
| id | mit-1721.1/76307 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T15:43:58Z |
| publishDate | 2013 |
| publisher | Portland Press |
| record_format | dspace |
| spelling | mit-1721.1/763072022-09-29T15:47:11Z Glycosylation at Asn[supscript 91] of H1N1 haemagglutinin affects binding to glycan receptors Jayaraman, Akila Koh, Xiaoying Li, Jing Raman, Rahul Viswanathan, Karthik Shriver, Zachary H. Sasisekharan, Ram Harvard University--MIT Division of Health Sciences and Technology Massachusetts Institute of Technology. Department of Biological Engineering Massachusetts Institute of Technology. School of Engineering Koch Institute for Integrative Cancer Research at MIT Jayaraman, Akila Li, Jing Raman, Rahul Viswanathan, Karthik Shriver, Zachary H. Sasisekharan, Ram The glycoprotein HA (haemagglutinin) on the surface of influenza A virus plays a central role in recognition and binding to specific host cell-surface glycan receptors and in fusion of viral membrane to the host nuclear membrane during viral replication. Given the abundance of HA on the viral surface, this protein is also the primary target for host innate and adaptive immune responses. Although addition of glycosylation sites on HA are a part of viral evolution to evade the host immune responses, there are specific glycosylation sites that are conserved during most of the evolution of the virus. In the present study, it was demonstrated that one such conserved glycosylation site at Asn[superscript 91] in H1N1 HA critically governs the glycan receptor-binding specificity and hence would potentially impinge on the host adaptation of the virus. National Institutes of Health (U.S.) (Grant GM R37 GM057073-1) 2013-01-18T16:40:28Z 2013-01-18T16:40:28Z 2012-05 2011-11 Article http://purl.org/eprint/type/JournalArticle 0264-6021 1470-8728 http://hdl.handle.net/1721.1/76307 Jayaraman, Akila et al. “Glycosylation at Asn [superscript 91] of H1N1 Haemagglutinin Affects Binding to Glycan Receptors.” Biochemical Journal 444.3 (2012). https://orcid.org/0000-0002-1288-9965 https://orcid.org/0000-0001-9344-0205 https://orcid.org/0000-0002-2085-7840 en_US http://dx.doi.org/10.1042/BJ20112101 Biochemical Journal Creative Commons Attribution Non-Commercial License http://creativecommons.org/licenses/by-nc/2.5/ application/pdf Portland Press PMC |
| spellingShingle | Jayaraman, Akila Koh, Xiaoying Li, Jing Raman, Rahul Viswanathan, Karthik Shriver, Zachary H. Sasisekharan, Ram Glycosylation at Asn[supscript 91] of H1N1 haemagglutinin affects binding to glycan receptors |
| title | Glycosylation at Asn[supscript 91] of H1N1 haemagglutinin affects binding to glycan receptors |
| title_full | Glycosylation at Asn[supscript 91] of H1N1 haemagglutinin affects binding to glycan receptors |
| title_fullStr | Glycosylation at Asn[supscript 91] of H1N1 haemagglutinin affects binding to glycan receptors |
| title_full_unstemmed | Glycosylation at Asn[supscript 91] of H1N1 haemagglutinin affects binding to glycan receptors |
| title_short | Glycosylation at Asn[supscript 91] of H1N1 haemagglutinin affects binding to glycan receptors |
| title_sort | glycosylation at asn supscript 91 of h1n1 haemagglutinin affects binding to glycan receptors |
| url | http://hdl.handle.net/1721.1/76307 https://orcid.org/0000-0002-1288-9965 https://orcid.org/0000-0001-9344-0205 https://orcid.org/0000-0002-2085-7840 |
| work_keys_str_mv | AT jayaramanakila glycosylationatasnsupscript91ofh1n1haemagglutininaffectsbindingtoglycanreceptors AT kohxiaoying glycosylationatasnsupscript91ofh1n1haemagglutininaffectsbindingtoglycanreceptors AT lijing glycosylationatasnsupscript91ofh1n1haemagglutininaffectsbindingtoglycanreceptors AT ramanrahul glycosylationatasnsupscript91ofh1n1haemagglutininaffectsbindingtoglycanreceptors AT viswanathankarthik glycosylationatasnsupscript91ofh1n1haemagglutininaffectsbindingtoglycanreceptors AT shriverzacharyh glycosylationatasnsupscript91ofh1n1haemagglutininaffectsbindingtoglycanreceptors AT sasisekharanram glycosylationatasnsupscript91ofh1n1haemagglutininaffectsbindingtoglycanreceptors |