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TitleIsolation and escape mapping of broadly neutralizing antibodies against emerging delta-coronaviruses.
Journal, issue, pagesImmunity, Vol. 57, Issue 12, Page 2914-22927.e7, Year 2024
Publish dateDec 10, 2024
AuthorsMegi Rexhepaj / Daniel Asarnow / Lisa Perruzza / Young-Jun Park / Barbara Guarino / Mathew Mccallum / Katja Culap / Christian Saliba / Giada Leoni / Alessio Balmelli / Courtney N Yoshiyama / Miles S Dickinson / Joel Quispe / Jack T Brown / M Alejandra Tortorici / Kaitlin R Sprouse / Ashley L Taylor / Davide Corti / Tyler N Starr / Fabio Benigni / David Veesler /
PubMed AbstractPorcine delta-coronavirus (PDCoV) spillovers were recently detected in febrile children, underscoring the recurrent zoonoses of divergent CoVs. To date, no vaccines or specific therapeutics are ...Porcine delta-coronavirus (PDCoV) spillovers were recently detected in febrile children, underscoring the recurrent zoonoses of divergent CoVs. To date, no vaccines or specific therapeutics are approved for use in humans against PDCoV. To prepare for possible future PDCoV epidemics, we isolated PDCoV spike (S)-directed monoclonal antibodies (mAbs) from humanized mice and found that two, designated PD33 and PD41, broadly neutralized a panel of PDCoV variants. Cryoelectron microscopy (cryo-EM) structures of PD33 and PD41 in complex with the S receptor-binding domain (RBD) and ectodomain trimer revealed the epitopes recognized by these mAbs, rationalizing their broad inhibitory activity. We show that both mAbs competitively interfere with host aminopeptidase N binding to neutralize PDCoV and used deep-mutational scanning epitope mapping to associate RBD antigenic sites with mAb-mediated neutralization potency. Our results indicate a PD33-PD41 mAb cocktail may heighten the barrier to escape. PD33 and PD41 are candidates for clinical advancement against future PDCoV outbreaks.
External linksImmunity / PubMed:39488210 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.0 Å
Structure data

44103

9b2c

EMDB-44103, PDB-9b2c:
Structure of the Porcine deltacoronavirus (PDCoV) receptor-binding domain bound to the PD33 antibody Fab fragment and the Kappa light chain nanobody
Method: EM (single particle) / Resolution: 3.0 Å

46804

9dez

EMDB-46804, PDB-9dez:
PDCoV S trimer bound by three copies of PD41 Fab
Method: EM (single particle) / Resolution: 2.6 Å

46805

9df0

EMDB-46805, PDB-9df0:
PDCoV S RBD bound to PD41 Fab (local refinement)
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-46806: PDCoV S SD2018/300 Apo (Class I)
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-46814: PDCoV S SD2018/300 with one PD41 Fab bound (Class II)
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-46815: PDCoV S SD2018/300 with one PD41 Fab bound (Class III)
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-46816: PDCoV S SD2018/300 with two PD41 Fabs bound (Class IV)
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

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

ChemComp-PAM:
PALMITOLEIC ACID

Source
  • Homo sapiens (human)
  • porcine deltacoronavirus
  • mus sp. (mice)
  • lama glama (llama)
  • Deltacoronavirus PDCoV/USA/Illinois121/2014
  • mus musculus (house mouse)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Spike glycoprotein / fusion protein / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / viral neutralization / inhibitor / VIRAL PROTEIN-IMMUNE SYSTEM complex / VIRAL PROTEIN / coronavirus / spike / antibody / PDCoV / PD41 / complex / Fab / antigen

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