8U0T
PRD-0038 RBD bound to Rhinolophus alcyone ACE2 (local refinement)
Summary for 8U0T
| Entry DOI | 10.2210/pdb8u0t/pdb |
| EMDB information | 41784 41786 |
| Descriptor | Angiotensin-converting enzyme, PRD-0038, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | sarbecoviruses, spike glycoprotein, fusion protein, neutralizing antibodies, structural genomics, seattle structural genomics center for infectious disease, ssgcid, inhibitor, viral protein |
| Biological source | Rhinolophus alcyone (Halcyon horseshoe bat) More |
| Total number of polymer chains | 2 |
| Total formula weight | 119716.01 |
| Authors | Park, Y.J.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2023-08-29, release date: 2023-12-06, Last modification date: 2024-10-23) |
| Primary citation | Lee, J.,Zepeda, S.K.,Park, Y.J.,Taylor, A.L.,Quispe, J.,Stewart, C.,Leaf, E.M.,Treichel, C.,Corti, D.,King, N.P.,Starr, T.N.,Veesler, D. Broad receptor tropism and immunogenicity of a clade 3 sarbecovirus. Cell Host Microbe, 31:1961-1973.e11, 2023 Cited by PubMed Abstract: Although Rhinolophus bats harbor diverse clade 3 sarbecoviruses, the structural determinants of receptor tropism along with the antigenicity of their spike (S) glycoproteins remain uncharacterized. Here, we show that the African Rhinolophus bat clade 3 sarbecovirus PRD-0038 S has a broad angiotensin-converting enzyme 2 (ACE2) usage and that receptor-binding domain (RBD) mutations further expand receptor promiscuity and enable human ACE2 utilization. We determine a cryo-EM structure of the PRD-0038 RBD bound to Rhinolophus alcyone ACE2, explaining receptor tropism and highlighting differences with SARS-CoV-1 and SARS-CoV-2. Characterization of PRD-0038 S using cryo-EM and monoclonal antibody reactivity reveals its distinct antigenicity relative to SARS-CoV-2 and identifies PRD-0038 cross-neutralizing antibodies for pandemic preparedness. PRD-0038 S vaccination elicits greater titers of antibodies cross-reacting with vaccine-mismatched clade 2 and clade 1a sarbecoviruses compared with SARS-CoV-2 S due to broader antigenic targeting, motivating the inclusion of clade 3 antigens in next-generation vaccines for enhanced resilience to viral evolution. PubMed: 37989312DOI: 10.1016/j.chom.2023.10.018 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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