7A57
La Crosse Virus Envelope Glycoprotein Gc W1066H Mutant Fusion Domains in Postfusion Conformation
Summary for 7A57
| Entry DOI | 10.2210/pdb7a57/pdb |
| Descriptor | Envelopment polyprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | virus entry, class ii membrane fusion protein, viral protein |
| Biological source | La Crosse virus L78 |
| Total number of polymer chains | 3 |
| Total formula weight | 154546.59 |
| Authors | Hellert, J.,Guardado-Calvo, P.,Rey, F.A. (deposition date: 2020-08-20, release date: 2021-09-01, Last modification date: 2024-10-16) |
| Primary citation | Hellert, J.,Aebischer, A.,Haouz, A.,Guardado-Calvo, P.,Reiche, S.,Beer, M.,Rey, F.A. Structure, function, and evolution of the Orthobunyavirus membrane fusion glycoprotein. Cell Rep, 42:112142-112142, 2023 Cited by PubMed Abstract: La Crosse virus, responsible for pediatric encephalitis in the United States, and Schmallenberg virus, a highly teratogenic veterinary virus in Europe, belong to the large Orthobunyavirus genus of zoonotic arthropod-borne pathogens distributed worldwide. Viruses in this under-studied genus cause CNS infections or fever with debilitating arthralgia/myalgia syndromes, with no effective treatment. The main surface antigen, glycoprotein Gc (∼1,000 residues), has a variable N-terminal half (Gc) targeted by the patients' antibody response and a conserved C-terminal moiety (Gc) responsible for membrane fusion during cell entry. Here, we report the X-ray structure of post-fusion La Crosse and Schmallenberg virus Gc, revealing the molecular determinants for hairpin formation and trimerization required to drive membrane fusion. We further experimentally confirm the role of residues in the fusion loops and in a vestigial endoplasmic reticulum (ER) translocation sequence at the Gc-Gc junction. The resulting knowledge provides essential molecular underpinnings for future development of potential therapeutic treatments and vaccines. PubMed: 36827185DOI: 10.1016/j.celrep.2023.112142 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.155 Å) |
Structure validation
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