33SD
Immune complex comprising the HRSV preF trimer (SC-DM) and the monoclonal antibody Lor69 - Obtained by cryo-EM
This is a non-PDB format compatible entry.
Summary for 33SD
| Entry DOI | 10.2210/pdb33sd/pdb |
| EMDB information | 59533 |
| Descriptor | Fusion glycoprotein F0, Lor69 Heavy Chain, Lor69 Light Chain, ... (4 entities in total) |
| Functional Keywords | antigen, antibody, complex, rsv, viral protein |
| Biological source | Respiratory syncytial virus More |
| Total number of polymer chains | 9 |
| Total formula weight | 248785.95 |
| Authors | Ols, S.,Cerveira, R.A.,Borst, A.J.,Bermudez-Mendez, E.,Gegenfurtner, F.,Eray, E.,Weidle, C.,Miranda, M.C.,Peng, Z.,Carr, K.D.,Skotheim, R.,Kochmann, J.,Brunette, N.,Lenart, K.,Hanke, L.,Karlsson Hedestam, G.B.,Perez, L.,Antanasijevic, A.,King, N.P.,Lore, K. (deposition date: 2026-08-21, release date: 2026-10-14) |
| Primary citation | Ols, S.,Arcoverde Cerveira, R.,Borst, A.J.,Bermudez-Mendez, E.,Gegenfurtner, F.,Eray, E.,Weidle, C.,Miranda, M.C.,Peng, Z.,Carr, K.D.,Skotheim, R.,Kochmann, J.,Brunette, N.,Lenart, K.,Hanke, L.,Karlsson Hedestam, G.B.,Perez, L.,Antanasijevic, A.,King, N.P.,Lore, K. Distinct mechanisms of neutralization by antibodies targeting a conserved pneumovirus F epitope. Biorxiv, 2026 Cited by PubMed Abstract: Pneumoviruses cause seasonal outbreaks leading to hospitalizations of vulnerable populations such as infants and the elderly. Cross-neutralizing antibodies targeting viral fusion have been isolated from infected individuals, but their elicitation and mechanisms of action remain understudied. Here, we describe two vaccine-elicited antibody classes, LOR24 and LOR69, that bind an overlapping epitope, and identify the somatic mutations that endow their breadth and potency, respectively. Cryo-electron microscopy structures of both antibodies bound to the HRSV fusion (F) protein show binding modes distinct from each other and from the previously described cross-neutralizing antibody MPE8, yet they all use similar motifs for binding. Complementary and electron microscopy experiments show that these antibodies either lock prefusion F as a trimer, arrest F in a monomeric or intermediate state, or promote the transition to the postfusion conformation. This work sheds light on mechanisms of pneumovirus neutralization and the elicitation of cross-neutralizing antibody responses. PubMed: 42818254DOI: 10.64898/2026.09.21.749132 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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