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- PDB-33sd: Immune complex comprising the HRSV preF trimer (SC-DM) and the mo... -

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Basic information

Entry
Database: PDB / ID: 33sd
TitleImmune complex comprising the HRSV preF trimer (SC-DM) and the monoclonal antibody Lor69 - Obtained by cryo-EM
Components
  • Fusion glycoprotein F0
  • Lor69 Heavy Chain
  • Lor69 Light Chain
KeywordsVIRAL PROTEIN / Antigen / antibody / complex / RSV
Function / homology
Function and homology information


symbiont-mediated induction of syncytium formation / Translation of respiratory syncytial virus mRNAs / RSV-host interactions / Assembly and release of respiratory syncytial virus (RSV) virions / Maturation of hRSV A proteins / Respiratory syncytial virus (RSV) attachment and entry / host cell Golgi membrane / entry receptor-mediated virion attachment to host cell / fusion of virus membrane with host plasma membrane / viral envelope ...symbiont-mediated induction of syncytium formation / Translation of respiratory syncytial virus mRNAs / RSV-host interactions / Assembly and release of respiratory syncytial virus (RSV) virions / Maturation of hRSV A proteins / Respiratory syncytial virus (RSV) attachment and entry / host cell Golgi membrane / entry receptor-mediated virion attachment to host cell / fusion of virus membrane with host plasma membrane / viral envelope / symbiont entry into host cell / host cell plasma membrane / virion membrane / identical protein binding / plasma membrane
Similarity search - Function
Precursor fusion glycoprotein F0, Paramyxoviridae / Fusion glycoprotein F0
Similarity search - Domain/homology
Fusion glycoprotein F0
Similarity search - Component
Biological speciesRespiratory syncytial virus
Homo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsOls, S. / Cerveira, R.A. / Borst, A.J. / Bermudez-Mendez, E. / Gegenfurtner, F. / Eray, E. / Weidle, C. / Miranda, M.C. / Peng, Z. / Carr, K.D. ...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.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI36621 United States
CitationJournal: bioRxiv / Year: 2026
Title: Distinct mechanisms of neutralization by antibodies targeting a conserved pneumovirus F epitope.
Authors: Sebastian Ols / Rodrigo Arcoverde Cerveira / Andrew J Borst / Erick Bermúdez-Méndez / Florian Gegenfurtner / Elise Eray / Connor Weidle / Marcos C Miranda / Zhitong Peng / Kenneth D Carr / ...Authors: Sebastian 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 /
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 ...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.
History
DepositionAug 21, 2026Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 14, 2026Provider: repository / Type: Initial release
Revision 1.0Oct 14, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Fusion glycoprotein F0
H: Lor69 Heavy Chain
L: Lor69 Light Chain
B: Fusion glycoprotein F0
D: Lor69 Heavy Chain
F: Lor69 Light Chain
C: Fusion glycoprotein F0
E: Lor69 Heavy Chain
G: Lor69 Light Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)248,78618
Polymers246,7959
Non-polymers1,9919
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein Fusion glycoprotein F0


Mass: 57338.434 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: SC-DM variant / Source: (gene. exp.) Respiratory syncytial virus / Cell line (production host): Expi293F / Production host: Homo sapiens (human) / References: UniProt: P03420
#2: Antibody Lor69 Heavy Chain


Mass: 13104.435 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: Heavy chain / Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): CHO / Production host: Homo sapiens (human)
#3: Antibody Lor69 Light Chain


Mass: 11822.156 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: Light chain / Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): CHO / Production host: Homo sapiens (human)
#4: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Monoclonal antibody Lor69 complex with HRSV preF trimer (SC-DM).
Type: COMPLEX / Entity ID: #1-#3 / Source: RECOMBINANT
Source (natural)Organism: Respiratory syncytial virus
Source (recombinant)Organism: Homo sapiens (human) / Cell: Expi293F
Buffer solutionpH: 7.4 / Details: PBS 1x
Buffer component
IDConc.NameFormulaBuffer-ID
1137 mMSodium ChlorideNaCl1
22.7 mMPotassium ChlorideKCl1
310 mMDisodium hydrigen phosphateNa2HPO41
41.8 mMPotassium dihydrogenKH2PO41
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 283 K
Details: Blot force of 0, wait time of 10s, blot time of 4-6s

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Electron microscopy imaging

MicroscopyModel: TFS GLACIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 150000 X / Nominal defocus max: 500 nm / Nominal defocus min: 250 nm
Specimen holderSpecimen holder model: OTHER
Image recordingElectron dose: 40 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 5373
Details: 2782 micrographs collected untilted and 2591 micrographs collected with a 30 degree tilt.

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
4CTFFIND4CTF correction
10RELION4initial Euler assignment
11RELION4final Euler assignment
12RELION4classification
13RELION43D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 361187
3D reconstructionResolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 128395 / Algorithm: BACK PROJECTION / Symmetry type: POINT

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