9BSU
EBOV GP/Nanosota-EB1
Summary for 9BSU
| Entry DOI | 10.2210/pdb9bsu/pdb |
| EMDB information | 44872 |
| Descriptor | Envelope glycoprotein, Nanosota-EB1, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | ebov glycoprotein, nanobody, viral protein |
| Biological source | Ebola virus More |
| Total number of polymer chains | 5 |
| Total formula weight | 267517.32 |
| Authors | |
| Primary citation | Bu, F.,Ye, G.,Morsheimer, K.,Mendoza, A.,Turner-Hubbard, H.,Herbst, M.,Spiller, B.,Wadzinski, B.E.,Eaton, B.,Anantpadma, M.,Yang, G.,Liu, B.,Davey, R.,Li, F. Discovery of Nanosota-EB1 and -EB2 as Novel Nanobody Inhibitors Against Ebola Virus Infection. Plos Pathog., 20:e1012817-e1012817, 2024 Cited by PubMed Abstract: The Ebola filovirus (EBOV) poses a serious threat to global health and national security. Nanobodies, a type of single-domain antibody, have demonstrated promising therapeutic potential. We identified two anti-EBOV nanobodies, Nanosota-EB1 and Nanosota-EB2, which specifically target the EBOV glycoprotein (GP). Cryo-EM and biochemical data revealed that Nanosota-EB1 binds to the glycan cap of GP1, preventing its protease cleavage, while Nanosota-EB2 binds to critical membrane-fusion elements in GP2, stabilizing it in the pre-fusion state. Nanosota-EB2 is a potent neutralizer of EBOV infection in vitro and offers excellent protection in a mouse model of EBOV challenge, while Nanosota-EB1 provides moderate neutralization and protection. Nanosota-EB1 and Nanosota-EB2 are the first nanobodies shown to inhibit authentic EBOV. Combined with our newly developed structure-guided in vitro evolution approach, they lay the foundation for nanobody-based therapies against EBOV and other viruses within the ebolavirus genus. PubMed: 39715280DOI: 10.1371/journal.ppat.1012817 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.36 Å) |
Structure validation
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