Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses.
In 2012, cases of lethal pneumonia among Chinese miners prompted the isolation of a rat-borne henipavirus (HNV), Mòjiāng virus (MojV). Although MojV is genetically related to highly pathogenic bat-borne henipaviruses, the absence of a conserved ephrin receptor-binding motif in the MojV attachment gl...
| Main Authors: | , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Nature Publishing Group
2017
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| _version_ | 1797105114022936576 |
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| author | Rissanen, AI Ahmed, AA Azarm, K Beaty, S Hong, P Nambulli, S Duprex, WP Lee, B Bowden, TA |
| author_facet | Rissanen, AI Ahmed, AA Azarm, K Beaty, S Hong, P Nambulli, S Duprex, WP Lee, B Bowden, TA |
| author_sort | Rissanen, AI |
| collection | OXFORD |
| description | In 2012, cases of lethal pneumonia among Chinese miners prompted the isolation of a rat-borne henipavirus (HNV), Mòjiāng virus (MojV). Although MojV is genetically related to highly pathogenic bat-borne henipaviruses, the absence of a conserved ephrin receptor-binding motif in the MojV attachment glycoprotein (MojV-G) indicates a differing host-cell recognition mechanism. Here we find that MojV-G displays a six-bladed β-propeller fold bearing limited similarity to known paramyxoviral attachment glycoproteins, in particular at host receptor-binding surfaces. We confirm the inability of MojV-G to interact with known paramyxoviral receptors in vitro, indicating an independence from well-characterized ephrinB2/B3, sialic acid and CD150-mediated entry pathways. Furthermore, we find that MojV-G is antigenically distinct, indicating that MojV would less likely be detected in existing large-scale serological screening studies focused on well-established HNVs. Altogether, these data indicate a unique host-cell entry pathway for this emerging and potentially pathogenic HNV. |
| first_indexed | 2024-03-07T06:42:54Z |
| format | Journal article |
| id | oxford-uuid:f9e491ef-4905-4ce9-9951-bea998f617a1 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T06:42:54Z |
| publishDate | 2017 |
| publisher | Nature Publishing Group |
| record_format | dspace |
| spelling | oxford-uuid:f9e491ef-4905-4ce9-9951-bea998f617a12022-03-27T13:01:34ZIdiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f9e491ef-4905-4ce9-9951-bea998f617a1EnglishSymplectic Elements at OxfordNature Publishing Group2017Rissanen, AIAhmed, AAAzarm, KBeaty, SHong, PNambulli, SDuprex, WPLee, BBowden, TAIn 2012, cases of lethal pneumonia among Chinese miners prompted the isolation of a rat-borne henipavirus (HNV), Mòjiāng virus (MojV). Although MojV is genetically related to highly pathogenic bat-borne henipaviruses, the absence of a conserved ephrin receptor-binding motif in the MojV attachment glycoprotein (MojV-G) indicates a differing host-cell recognition mechanism. Here we find that MojV-G displays a six-bladed β-propeller fold bearing limited similarity to known paramyxoviral attachment glycoproteins, in particular at host receptor-binding surfaces. We confirm the inability of MojV-G to interact with known paramyxoviral receptors in vitro, indicating an independence from well-characterized ephrinB2/B3, sialic acid and CD150-mediated entry pathways. Furthermore, we find that MojV-G is antigenically distinct, indicating that MojV would less likely be detected in existing large-scale serological screening studies focused on well-established HNVs. Altogether, these data indicate a unique host-cell entry pathway for this emerging and potentially pathogenic HNV. |
| spellingShingle | Rissanen, AI Ahmed, AA Azarm, K Beaty, S Hong, P Nambulli, S Duprex, WP Lee, B Bowden, TA Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses. |
| title | Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses. |
| title_full | Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses. |
| title_fullStr | Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses. |
| title_full_unstemmed | Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses. |
| title_short | Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses. |
| title_sort | idiosyncratic mojiang virus attachment glycoprotein directs a host cell entry pathway distinct from genetically related henipaviruses |
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