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A broadly reactive ultralong bovine antibody that can determine the integrity of foot-and-mouth disease virus capsids. | LitMetric

AI Article Synopsis

  • - Foot-and-mouth disease (FMD) vaccines using inactivated virus are not very effective because the viral capsids can break apart over time or under certain conditions, resulting in a less protective immune response.
  • - The FMD virus has seven different serotypes, and most antibodies generated from existing vaccines are specific to just one type, limiting cross-protection.
  • - A novel bovine antibody (Ab117) has been identified, which can bind to a crucial area of the FMD capsid and demonstrate broad serotype coverage, making it useful for ensuring vaccine quality by assessing capsid integrity.

Article Abstract

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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11488517PMC
http://dx.doi.org/10.1099/jgv.0.002032DOI Listing

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