Structures of Ebola virus GP and sGP in complex with therapeutic antibodies
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2016
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| author | Pallesen, Jesper Murin, Charles D. De Val, Natalia Cottrell, Christopher A. Hastie, Kathryn M. Turner, Hannah L. Fusco, Marnie L. Flyak, Andrew I. Zeitlin, Larry Crowe, James E. Andersen, Kristian G. Saphire, Erica Ollmann Ward, Andrew B. |
| author_facet | Pallesen, Jesper Murin, Charles D. De Val, Natalia Cottrell, Christopher A. Hastie, Kathryn M. Turner, Hannah L. Fusco, Marnie L. Flyak, Andrew I. Zeitlin, Larry Crowe, James E. Andersen, Kristian G. Saphire, Erica Ollmann Ward, Andrew B. |
| contents | (Uploaded by Plazi for the Bat Literature Project) Zaire Ebola virus (EBOV) and related viruses of the family Filoviridae are highly lethal and have caused numerous outbreaks since emerging in 1967, including a sustained epidemic in West Africa from 2013–2015 (www.cdc.gov). No vaccines or therapeutics against EBOV are yet approved, although several have shown promise in animal models and have moved forward to human clinical trials1–3. The main target of these candidate vaccines and treatments is the viral-surface trimeric GP, which includes GP1 (receptor binding) and GP2 (viral fusion) subunits4,5. However, the major product of the GP gene is not viral-surface GP, but instead a secreted, dimeric glycoprotein termed sGP6. GP and sGP share 295 N-terminal amino acids, but have distinct C-terminal regions as a result of transcriptional editing6. The unique C terminus of sGP contains 65 amino acids and includes a Cys at position 306 that is critical for sGP dimerization7. In contrast, the unique C terminus of viral-surface GP contains 381 amino acids that assemble a large, heavily glycosylated mucin-like domain (MLD), the viral fusion machinery and a transmembrane domain8. Antibodies elicited during infection that cross-react to sGP and GP9 can potentially be absorbed by sGP, although the consequences of such are unclear10. |
| format | Recurso digital |
| id | zenodo_https___doi_org_10_5281_zenodo_13533097 |
| institution | Zenodo |
| language | |
| publishDate | 2016 |
| publisher | Zenodo |
| record_format | zenodo |
| spellingShingle | Structures of Ebola virus GP and sGP in complex with therapeutic antibodies Pallesen, Jesper Murin, Charles D. De Val, Natalia Cottrell, Christopher A. Hastie, Kathryn M. Turner, Hannah L. Fusco, Marnie L. Flyak, Andrew I. Zeitlin, Larry Crowe, James E. Andersen, Kristian G. Saphire, Erica Ollmann Ward, Andrew B. Biodiversity Mammalia Chiroptera Chordata Animalia bats bat (Uploaded by Plazi for the Bat Literature Project) Zaire Ebola virus (EBOV) and related viruses of the family Filoviridae are highly lethal and have caused numerous outbreaks since emerging in 1967, including a sustained epidemic in West Africa from 2013–2015 (www.cdc.gov). No vaccines or therapeutics against EBOV are yet approved, although several have shown promise in animal models and have moved forward to human clinical trials1–3. The main target of these candidate vaccines and treatments is the viral-surface trimeric GP, which includes GP1 (receptor binding) and GP2 (viral fusion) subunits4,5. However, the major product of the GP gene is not viral-surface GP, but instead a secreted, dimeric glycoprotein termed sGP6. GP and sGP share 295 N-terminal amino acids, but have distinct C-terminal regions as a result of transcriptional editing6. The unique C terminus of sGP contains 65 amino acids and includes a Cys at position 306 that is critical for sGP dimerization7. In contrast, the unique C terminus of viral-surface GP contains 381 amino acids that assemble a large, heavily glycosylated mucin-like domain (MLD), the viral fusion machinery and a transmembrane domain8. Antibodies elicited during infection that cross-react to sGP and GP9 can potentially be absorbed by sGP, although the consequences of such are unclear10. |
| title | Structures of Ebola virus GP and sGP in complex with therapeutic antibodies |
| topic | Biodiversity Mammalia Chiroptera Chordata Animalia bats bat |
| url | https://doi.org/10.5281/zenodo.13533097 |