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TitleA broadly reactive ultralong bovine antibody that can determine the integrity of foot-and-mouth disease virus capsids.
Journal, issue, pagesJ Gen Virol, Vol. 105, Issue 10, Year 2024
Publish dateOct 18, 2024
AuthorsJohn D Clarke / Helen M E Duyvesteyn / Eva Perez-Martin / Undīne Latišenko / Claudine Porta / Kathleen V Humphreys / Abigail L Hay / Jingshan Ren / Elizabeth E Fry / Erwin van den Born / Bryan Charleston / Marie Bonnet-Di Placido / Raymond J Owens / David I Stuart / John A Hammond /
PubMed AbstractFoot-and-mouth disease vaccination using inactivated virus is suboptimal, as the icosahedral viral capsids often disassemble into antigenically distinct pentameric units during long-term storage, or ...Foot-and-mouth disease vaccination using inactivated virus is suboptimal, as the icosahedral viral capsids often disassemble into antigenically distinct pentameric units during long-term storage, or exposure to elevated temperature or lowered pH, and thus raise a response that is no longer protective. Furthermore, as foot-and-mouth disease virus (FMDV)'s seven serotypes are antigenically diverse, cross-protection from a single serotype vaccine is limited, and most existing mouse and bovine antibodies and camelid single-domain heavy chain-only antibodies are serotype-specific. For quality control purposes, there is a real need for pan-serotype antibodies that clearly distinguish between pentamer (12S) and protective intact FMDV capsid. To date, few cross-serotype bovine-derived antibodies have been reported in the literature. We identify a bovine antibody with an ultralong CDR-H3, Ab117, whose structural analysis reveals that it binds to a deep, hydrophobic pocket on the interior surface of the capsid via the CDR-H3. Main-chain and hydrophobic interactions provide broad serotype specificity. ELISA analysis confirms that Ab117 is a novel pan-serotype and conformational epitope-specific 12S reagent, suitable for assessing capsid integrity.
External linksJ Gen Virol / PubMed:39422666 / PubMed Central
MethodsEM (single particle)
Resolution2.9 Å
Structure data

EMDB-51105, PDB-9g6v:
Dissociated FMDV SAT2 Pentamer in complex with ultralong Fab117
Method: EM (single particle) / Resolution: 2.9 Å

Source
  • bos taurus (domestic cattle)
  • foot-and-mouth disease virus sat 2
KeywordsVIRUS LIKE PARTICLE / disrupted / dissociated / VLP / internal epitope / pan-specific / ultralong

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