Single-domain antibodies reveal unique borrelicidal epitopes on the Lyme disease vaccine antigen, outer surface protein A (OspA).

ABSTRACT: Camelid-derived, single-domain antibodies (V_HHs) have proven to be extremely powerful tools in defining the antigenic landscape of immunologically heterogeneous surface proteins. In this report, we generated a phage-displayed V_HH library directed against the candidate Lyme disease vaccine antigen, outer surface protein A (OspA). Two alpacas were immunized with recombinant OspA serotype 1 from Borrelia burgdorferi sensu stricto strain B31, in combination with the canine vaccine RECOMBITEK Lyme containing lipidated OspA. The phage library was subjected to two rounds of affinity enrichment ("panning") against recombinant OspA, yielding 21 unique V_HHs within two epitope bins, as determined through competition enzyme linked immunosorbent assays (ELISAs) w

SUBMITTER: Vance DJ 

PROVIDER: S-EPMC11003225 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature