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TitleDistinct mechanisms of neutralization by antibodies targeting a conserved pneumovirus F epitope.
Journal, issue, pagesbioRxiv, Year 2026
Publish dateSep 24, 2026
AuthorsSebastian Ols / Rodrigo Arcoverde Cerveira / Andrew J Borst / Erick Bermúdez-Méndez / Florian Gegenfurtner / Elise Eray / Connor Weidle / Marcos C Miranda / Zhitong Peng / Kenneth D Carr / Rebecca Skotheim / Jana Kochmann / Natalie Brunette / Klara Lenart / Leo Hanke / Gunilla B Karlsson Hedestam / Laurent Perez / Aleksandar Antanasijevic / Neil P King / Karin Loré /
PubMed AbstractPneumoviruses cause seasonal outbreaks leading to hospitalizations of vulnerable populations such as infants and the elderly. Cross-neutralizing antibodies targeting viral fusion have been isolated ...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.
External linksbioRxiv / PubMed:42818254 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

59533

33sd

EMDB-59533, PDB-33sd:
Immune complex comprising the HRSV preF trimer (SC-DM) and the monoclonal antibody Lor69 - Obtained by cryo-EM
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • respiratory syncytial virus
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / Antigen / antibody / complex / RSV

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