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TitleHuman Coronavirus HKU1 Neutralizing Monoclonal Antibodies Target Diverse Epitopes Within and Around the TMPRSS2 Receptor Binding Site.
Journal, issue, pagesBiorxiv, Year 2025
Publish dateSep 29, 2025 (structure data deposition date)
AuthorsLingshu Wang / Jeswin Joseph / Sheena Vasquez / Daniel Wrapp / Timothy P Sheahan / Christian K O Dzuvor / Osnat Rosen / Robert N Kirchdoerfer / Olubukola M Abiona / Catherine Hammond / Wei Shi / Sydney P Moak / Wing-Pui Kong / Yi Zhang / Michael R Eso / Ariane J Brown / Andrew B Ward / Ralph Baric / Jason S McLellan / Theodore C Pierson / John Mascola / Barney S Graham / Hadi M Yassine / Christopher O Barnes / Kizzmekia S Corbett-Helaire /
PubMed AbstractEndemic human coronaviruses (HCoVs), like HCoV-HKU1, account for ~30% of common cold/year and can cause serious upper and lower respiratory infections, yet no licensed vaccines target HCoVs. In fact, ...Endemic human coronaviruses (HCoVs), like HCoV-HKU1, account for ~30% of common cold/year and can cause serious upper and lower respiratory infections, yet no licensed vaccines target HCoVs. In fact, little is known about HCoV-HKU1's antigenic landscape. Thus, we characterized key interactions between HCoV-HKU1 spike (S) with monoclonal antibodies (mAbs) isolated from pre-pandemic HCoV-HKU1 convalescent PBMCs. We isolated 14 mAbs, which bound distinct S regions: receptor binding domain (RBD), N-terminal domain (NTD), and S2 subunit. Structural and functional studies revealed three groups of RBD-specific mAbs targeting diverse footprints within and around the TMPRSS2 receptor binding site, exemplified by: (1) The most potently neutralizing mAb, H501-022 (IC = 0.01 μg/mL), which recognizes the TMPRSS2 binding motif, thereby blocking receptor engagement; (2) mAb H501-008 (IC = 0.05 μg/mL) that binds a conserved, cross-reactive epitope outside of the TMPRSS2 binding site that is shared with HCoV-OC43; and (3) H501-018 (IC = 0.28 μg/mL) that recognizes both "up" and "down" RBD conformations at a distinct, non-overlapping site outside of the TMPRSS2 binding motif, distinguishing itself from H501-022 and H501-008, which bind exclusively to the "up" RBD conformation. These mAbs represent the first type-specific HCoV-HKU1 mAbs isolated from a convalescent donor. Our findings provide molecular insight into HCoV-HKU1 antibody recognition and neutralization mechanisms, importantly highlighting antigenic differences comparing HCoVs and pandemic CoVs - a critical step towards advancing universal CoV vaccine design.
External linksBiorxiv / PubMed:41279056 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.6 - 3.8 Å
Structure data

PDB-9ygn:
HuCoV-HKU1 C S 2P in complex with H501-018 Fab (State 1, global cryoEM)
Method: ELECTRON MICROSCOPY / Resolution: 3.4 Å

PDB-9ygo:
HuCoV-HKU1 C S 2P in complex with H501-018 Fab (State 2, global cryoEM)
Method: ELECTRON MICROSCOPY / Resolution: 3.4 Å

PDB-9ygp:
HCoV-HKU1 C S 2P in complex with H501-018 Fab (local cryoEM)
Method: ELECTRON MICROSCOPY / Resolution: 3.2 Å

PDB-9ygq:
HCoV-HKU1 C S 2P in complex with H501-022 Fab (global cryoEM)
Method: ELECTRON MICROSCOPY / Resolution: 3.6 Å

PDB-9ygr:
HCoV-HKU1 C S 2P in complex with H501-022 Fab (local cryoEM)
Method: ELECTRON MICROSCOPY / Resolution: 3.8 Å

PDB-9yxw:
Crystal structure of HCoV-HKU1 RBD bound by H501-008 Fab
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

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

ChemComp-HOH:
WATER

Source
  • human coronavirus hku1
  • homo sapiens (human)
  • human coronavirus hku1 (isolate n5)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / coronavirus / HKU1 / mAb / cryoEM / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex / Spike / HCoV-HKU1 / antibody / Fab

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