A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus
The emergent zoonotic henipaviruses, Hendra, and Nipah are responsible for frequent and fatal disease outbreaks in domestic animals and humans. Specificity of henipavirus attachment glycoproteins (G) for highly species-conserved ephrin ligands underpins their broad host range and is associated with...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Life Science Alliance
2019
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| _version_ | 1797069170450366464 |
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| author | Pryce, R Azarm, K Rissanen, I Harlos, K Bowden, TA Lee, B |
| author_facet | Pryce, R Azarm, K Rissanen, I Harlos, K Bowden, TA Lee, B |
| author_sort | Pryce, R |
| collection | OXFORD |
| description | The emergent zoonotic henipaviruses, Hendra, and Nipah are responsible for frequent and fatal disease outbreaks in domestic animals and humans. Specificity of henipavirus attachment glycoproteins (G) for highly species-conserved ephrin ligands underpins their broad host range and is associated with systemic and neurological disease pathologies. Here, we demonstrate that Cedar virus (CedV)—a related henipavirus that is ostensibly nonpathogenic—possesses an idiosyncratic entry receptor repertoire that includes the common henipaviral receptor, ephrin-B2, but, distinct from pathogenic henipaviruses, does not include ephrin-B3. Uniquely among known henipaviruses, CedV can use ephrin-B1 for cellular entry. Structural analyses of CedV-G reveal a key region of molecular specificity that directs ephrin-B1 utilization, while preserving a universal mode of ephrin-B2 recognition. The structural and functional insights presented uncover diversity within the known henipavirus receptor repertoire and suggest that only modest structural changes may be required to modulate receptor specificities within this group of lethal human pathogens. |
| first_indexed | 2024-03-06T22:20:30Z |
| format | Journal article |
| id | oxford-uuid:54e1c405-4e7e-4d7c-bbf8-4606d79ceb8f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:20:30Z |
| publishDate | 2019 |
| publisher | Life Science Alliance |
| record_format | dspace |
| spelling | oxford-uuid:54e1c405-4e7e-4d7c-bbf8-4606d79ceb8f2022-03-26T16:40:31ZA key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virusJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:54e1c405-4e7e-4d7c-bbf8-4606d79ceb8fEnglishSymplectic ElementsLife Science Alliance2019Pryce, RAzarm, KRissanen, IHarlos, KBowden, TALee, BThe emergent zoonotic henipaviruses, Hendra, and Nipah are responsible for frequent and fatal disease outbreaks in domestic animals and humans. Specificity of henipavirus attachment glycoproteins (G) for highly species-conserved ephrin ligands underpins their broad host range and is associated with systemic and neurological disease pathologies. Here, we demonstrate that Cedar virus (CedV)—a related henipavirus that is ostensibly nonpathogenic—possesses an idiosyncratic entry receptor repertoire that includes the common henipaviral receptor, ephrin-B2, but, distinct from pathogenic henipaviruses, does not include ephrin-B3. Uniquely among known henipaviruses, CedV can use ephrin-B1 for cellular entry. Structural analyses of CedV-G reveal a key region of molecular specificity that directs ephrin-B1 utilization, while preserving a universal mode of ephrin-B2 recognition. The structural and functional insights presented uncover diversity within the known henipavirus receptor repertoire and suggest that only modest structural changes may be required to modulate receptor specificities within this group of lethal human pathogens. |
| spellingShingle | Pryce, R Azarm, K Rissanen, I Harlos, K Bowden, TA Lee, B A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus |
| title | A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus |
| title_full | A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus |
| title_fullStr | A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus |
| title_full_unstemmed | A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus |
| title_short | A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus |
| title_sort | key region of molecular specificity orchestrates unique ephrin b1 utilization by cedar virus |
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