Structural insights into the human metapneumovirus glycoprotein ectodomain.
Human metapneumovirus is a major cause of respiratory tract infections worldwide. Previous reports have shown that the viral attachment glycoprotein (G) modulates innate and adaptive immune responses, leading to incomplete immunity and promoting reinfection. Using bioinformatics analyses, static lig...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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American Society for Microbiology
2014
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| _version_ | 1826266431229001728 |
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| author | Leyrat, C Paesen, G Charleston, J Renner, M Grimes, J |
| author_facet | Leyrat, C Paesen, G Charleston, J Renner, M Grimes, J |
| author_sort | Leyrat, C |
| collection | OXFORD |
| description | Human metapneumovirus is a major cause of respiratory tract infections worldwide. Previous reports have shown that the viral attachment glycoprotein (G) modulates innate and adaptive immune responses, leading to incomplete immunity and promoting reinfection. Using bioinformatics analyses, static light scattering, and small-angle X-ray scattering, we show that the extracellular region of G behaves as a heavily glycosylated, intrinsically disordered polymer. We discuss potential implications of these findings for the modulation of immune responses by G. |
| first_indexed | 2024-03-06T20:38:51Z |
| format | Journal article |
| id | oxford-uuid:3392025f-7f9b-44cf-b7c8-880278c5c0c0 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:38:51Z |
| publishDate | 2014 |
| publisher | American Society for Microbiology |
| record_format | dspace |
| spelling | oxford-uuid:3392025f-7f9b-44cf-b7c8-880278c5c0c02022-03-26T13:20:57ZStructural insights into the human metapneumovirus glycoprotein ectodomain.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3392025f-7f9b-44cf-b7c8-880278c5c0c0EnglishSymplectic Elements at OxfordAmerican Society for Microbiology2014Leyrat, CPaesen, GCharleston, JRenner, MGrimes, JHuman metapneumovirus is a major cause of respiratory tract infections worldwide. Previous reports have shown that the viral attachment glycoprotein (G) modulates innate and adaptive immune responses, leading to incomplete immunity and promoting reinfection. Using bioinformatics analyses, static light scattering, and small-angle X-ray scattering, we show that the extracellular region of G behaves as a heavily glycosylated, intrinsically disordered polymer. We discuss potential implications of these findings for the modulation of immune responses by G. |
| spellingShingle | Leyrat, C Paesen, G Charleston, J Renner, M Grimes, J Structural insights into the human metapneumovirus glycoprotein ectodomain. |
| title | Structural insights into the human metapneumovirus glycoprotein ectodomain. |
| title_full | Structural insights into the human metapneumovirus glycoprotein ectodomain. |
| title_fullStr | Structural insights into the human metapneumovirus glycoprotein ectodomain. |
| title_full_unstemmed | Structural insights into the human metapneumovirus glycoprotein ectodomain. |
| title_short | Structural insights into the human metapneumovirus glycoprotein ectodomain. |
| title_sort | structural insights into the human metapneumovirus glycoprotein ectodomain |
| work_keys_str_mv | AT leyratc structuralinsightsintothehumanmetapneumovirusglycoproteinectodomain AT paeseng structuralinsightsintothehumanmetapneumovirusglycoproteinectodomain AT charlestonj structuralinsightsintothehumanmetapneumovirusglycoproteinectodomain AT rennerm structuralinsightsintothehumanmetapneumovirusglycoproteinectodomain AT grimesj structuralinsightsintothehumanmetapneumovirusglycoproteinectodomain |