Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution
Differential interactions between influenza A virus protein hemagglutinin (HA) and α2→3 (avian) or α2→6 (human) sialylated glycan receptors play an important role in governing host specificity and adaptation of the virus. Previous analysis of HA–glycan interactions with trisaccharides showed that, i...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | en_US |
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American Chemical Society (ACS)
2015
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| Online Access: | http://hdl.handle.net/1721.1/99521 https://orcid.org/0000-0001-9344-0205 https://orcid.org/0000-0002-2085-7840 |
| _version_ | 1811082323935887360 |
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| author | Sassaki, Guilherme L. Elli, Stefano Rudd, Timothy R. Macchi, Eleonora Yates, Edwin A. Naggi, Annamaria Raman, Rahul Torri, Giangiacomo Guerrini, Marco 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 Sassaki, Guilherme L. Elli, Stefano Rudd, Timothy R. Macchi, Eleonora Yates, Edwin A. Naggi, Annamaria Raman, Rahul Torri, Giangiacomo Guerrini, Marco Shriver, Zachary H. Sasisekharan, Ram |
| author_sort | Sassaki, Guilherme L. |
| collection | MIT |
| description | Differential interactions between influenza A virus protein hemagglutinin (HA) and α2→3 (avian) or α2→6 (human) sialylated glycan receptors play an important role in governing host specificity and adaptation of the virus. Previous analysis of HA–glycan interactions with trisaccharides showed that, in addition to the terminal sialic acid linkage, the conformation and topology of the glycans, while they are bound to HA, are key factors in regulating these interactions. Here, the solution conformation and dynamics of two representative avian and human glycan pentasaccharide receptors [LSTa, Neu5Ac-α(2→3)-Gal-β(1→3)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc; LSTc, (Neu5Ac-α(2→6)-Gal-β(1→4)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc] have been explored using nuclear magnetic resonance and molecular dynamics simulation. Analyses demonstrate that, in solution, human and avian receptors sample distinct conformations, topologies, and dynamics. These unique features of avian and human receptors in solution could represent distinct molecular characteristics for recognition by HA, thereby providing the HA–glycan interaction specificity in influenza. |
| first_indexed | 2024-09-23T12:01:19Z |
| format | Article |
| id | mit-1721.1/99521 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T12:01:19Z |
| publishDate | 2015 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/995212022-09-27T23:33:12Z Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution Sassaki, Guilherme L. Elli, Stefano Rudd, Timothy R. Macchi, Eleonora Yates, Edwin A. Naggi, Annamaria Raman, Rahul Torri, Giangiacomo Guerrini, Marco 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 Shriver, Zachary H. Raman, Rahul Sasisekharan, Ram Differential interactions between influenza A virus protein hemagglutinin (HA) and α2→3 (avian) or α2→6 (human) sialylated glycan receptors play an important role in governing host specificity and adaptation of the virus. Previous analysis of HA–glycan interactions with trisaccharides showed that, in addition to the terminal sialic acid linkage, the conformation and topology of the glycans, while they are bound to HA, are key factors in regulating these interactions. Here, the solution conformation and dynamics of two representative avian and human glycan pentasaccharide receptors [LSTa, Neu5Ac-α(2→3)-Gal-β(1→3)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc; LSTc, (Neu5Ac-α(2→6)-Gal-β(1→4)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc] have been explored using nuclear magnetic resonance and molecular dynamics simulation. Analyses demonstrate that, in solution, human and avian receptors sample distinct conformations, topologies, and dynamics. These unique features of avian and human receptors in solution could represent distinct molecular characteristics for recognition by HA, thereby providing the HA–glycan interaction specificity in influenza. Finlombardia SPA Conselho Nacional de Pesquisas (Brazil) National Institutes of Health (U.S.) (R37 GM057073-13) Singapore. National Research Foundation (Singapore-MIT Alliance for Research and Technology) 2015-10-29T18:47:00Z 2015-10-29T18:47:00Z 2013-09 2013-09 Article http://purl.org/eprint/type/JournalArticle 0006-2960 1520-4995 http://hdl.handle.net/1721.1/99521 Sassaki, Guilherme L., Stefano Elli, Timothy R. Rudd, Eleonora Macchi, Edwin A. Yates, Annamaria Naggi, Zachary Shriver, et al. “Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution.” Biochemistry 52, no. 41 (October 15, 2013): 7217–7230. https://orcid.org/0000-0001-9344-0205 https://orcid.org/0000-0002-2085-7840 en_US http://dx.doi.org/10.1021/bi400677n Biochemistry 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 American Chemical Society (ACS) PMC |
| spellingShingle | Sassaki, Guilherme L. Elli, Stefano Rudd, Timothy R. Macchi, Eleonora Yates, Edwin A. Naggi, Annamaria Raman, Rahul Torri, Giangiacomo Guerrini, Marco Shriver, Zachary H. Sasisekharan, Ram Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution |
| title | Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution |
| title_full | Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution |
| title_fullStr | Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution |
| title_full_unstemmed | Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution |
| title_short | Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution |
| title_sort | human α2 6 and avian α2 3 sialylated receptors of influenza a virus show distinct conformations and dynamics in solution |
| url | http://hdl.handle.net/1721.1/99521 https://orcid.org/0000-0001-9344-0205 https://orcid.org/0000-0002-2085-7840 |
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