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TitleCattle antibodies identify a cross-serotype broadly neutralising foot-and-mouth disease virus epitope.
Journal, issue, pagesNPJ Vaccines, Vol. 11, Issue 1, Year 2026
Publish dateApr 2, 2026
AuthorsMarie Bonnet-Di Placido / Helen M E Duyvesteyn / Angela W Steyn / Abigail L Hay / Claudine Porta / Kristel Ramirez Valdez / Elena Lokhman / Sylvia Crossley / Kevan Hanson / William N Mwangi / Danish Munir / Eva Perez-Martin / Nick J Knowles / Alison Burman / Abdelaziz A Yassin / Amin Asfor / Cristina Faralla / Katherine J Lam / Róisín McComb / Carina Leifeld / Kimberly Pietersz / Donald P King / Erwin van den Born / Sherie K Duncan / Bryan Charleston / Elizabeth E Fry / Jingshan Ren / David I Stuart / John A Hammond /
PubMed AbstractFoot-and-mouth disease virus (FMDV) causes a devastating disease that threatens global food security. Vaccination is hindered by antigenic diversity across serotypes. To identify cross-serotype ...Foot-and-mouth disease virus (FMDV) causes a devastating disease that threatens global food security. Vaccination is hindered by antigenic diversity across serotypes. To identify cross-serotype neutralising epitopes, we isolated 24 FMDV-specific antibodies from cattle sequentially vaccinated with antigens from four serotypes, of which three neutralised three vaccine strains. These three antibodies neutralised 21 and bound 59 additional topotypes across O, A, Asia 1, and C serotypes. Cryo-EM complexes of Fabs with FMD virus-like particles indicated all three recognise a common flexible epitope at the VP1 C-terminus, confirmed by binding competition. Crystallography and structural modelling revealed that a normally inaccessible surface of the hydrophobic VP1 C-terminal peptides inserts into a similar groove in all three antibodies. Comparison of neutralisation activity and integrin receptor blocking by whole antibodies, F(ab')s, and Fabs suggests neutralisation is mediated by Fc steric hindrance of receptor binding. This cryptic, linear, and cross-serotype neutralising epitope may inform improved FMD vaccines.
External linksNPJ Vaccines / PubMed:41927576 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.72 - 3.89 Å
Structure data

EMDB-54248: Trispecific fab 17 with O1M 93C virus like particle
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-54261: Trispecific fab 34 with O1M 93C virus like particle
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-54263: Trispecific fab 49 with O1M 93C virus like particle
Method: EM (single particle) / Resolution: 3.4 Å

PDB-9hv1:
Crystal structure of tri-specific FMDV mAb-17 Fab
Method: X-RAY DIFFRACTION / Resolution: 1.96 Å

PDB-9hv2:
Crystal structure of tri-specific FMDV mAb-34 Fab
Method: X-RAY DIFFRACTION / Resolution: 1.77 Å

PDB-9hv8:
Crystal structure of tri-specific FMDV mAb-49 Fab
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

PDB-9hv9:
Crystal structure of Fab34 complexed with a 7-mer peptide of FMDV VP1
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-9hva:
Crystal structure of Fab34 complexed with a 18-mer peptide of FMDV VP1
Method: X-RAY DIFFRACTION / Resolution: 3.89 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-MG:
Unknown entry

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

Source
  • bos taurus (domestic cattle)
  • foot-and-mouth disease virus
KeywordsIMMUNE SYSTEM / foot-and-mouth disease virus / cattle antibody / cross-reactive / linear epitope / antibody structure

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