Comparative analysis of antibody responses to outer surface protein (Osp)A and OspC in dogs vaccinated with Lyme disease vaccines

Abstract

Lyme disease (LD), the most common tick-borne disease of canines and humans in N. America, is caused by the spirochete Borreliella burgdorferi . Subunit and bacterin vaccines are available for the prevention of LD in dogs. LD bacterin vaccines, which are comprised of cell lysates of two strains of B. burgdorferi , contain over 1000 different proteins and cellular constituents. In contrast, subunit vaccines are defined in composition and consist of either outer surface protein (Osp)A or OspA and an OspC chimeritope. In this study, we comparatively assessed antibody responses to OspA and OspC induced by vaccination with all canine bacterin and subunit LD vaccines that are commercially available in North America. Dogs were administered a two-dose series of the vaccine to which they were assigned (3 weeks apart): Subunit-AC, Subunit-A, Bacterin-1, and Bacterin-2. Antibody titers to OspA and OspC were determined by ELISA and the ability of each vaccine to elicit antibodies that recognize diverse OspC proteins (referred to as OspC types) assessed by immunoblot. While all of the vaccines elicited similar OspA antibody responses, only Subunit-AC triggered a robust and broadly cross-reactive antibody response to divergent OspC proteins. The data presented within provide new information regarding vaccination-induced antibody responses to key tick and mammalian phase antigens by both subunit and bacterin LD canine vaccine formulations.

FtlA and FtlB Are Candidates for Inclusion in a Next-Generation Multiantigen Subunit Vaccine for Lyme Disease

“…The B. burgdorferi strain B31 ftlA (encoding the protein with accession number WP_106017559.1 ), ftlB ( WP_010890300.1 ), ftlC ( WP_012672184.1 ), and ftlD ( WP_146124603.1 ) gene sequences were codon optimized for expression in Escherichia coli , synthesized (minus the leader sequence), and inserted into pET45b(+) at its BamHI and EagI restriction sites (GenScript). Overlapping ftlA gene fragments corresponding to amino acids 19 to 143 (F1), 109 to 233 (F2), and 171 to 297 (F3) were PCR amplified from B. burgdorferi B31 DNA using Phusion polymerase, standard amplification conditions, and primers that harbor BamHI (forward primer) and EagI (reverse primer) restriction sites ( 40 ). The amplicons were cut with BamHI and EagI, purified, and ligated into pET45b(+) (Novagen), and the plasmids propagated in E. coli NovaBlue cells.…”

“…The amplicons were cut with BamHI and EagI, purified, and ligated into pET45b(+) (Novagen), and the plasmids propagated in E. coli NovaBlue cells. The plasmids were purified and transformed into E. coli BL21(DE3) cells, protein expression was induced with IPTG (isopropyl-β- d -thiogalactopyranoside; 1 mM), and the His-tagged proteins were purified using nickel affinity chromatography on an ÄKTA fast protein liquid chromatography (FPLC) platform (Cytiva) ( 40 ). Some proteins were subjected to a second round of FPLC purification using a cobalt column on the ÄKTA platform.…”

A Review on Bacterial Infectious Diseases of Dogs

“…Several commercial vaccines are available worldwide for the prevention of disease in dogs [32]. These vaccines include killed whole borreliae bacteria or specific recombinant or chimeric outer surface proteins (OspA and/or OspC), with or without adjuvant [33]. Lyme's vaccine has been generally recommended in endemic areas.…”

Borrelia Lyme Group

“…This increment of temperature seems to be responsible that most Lyme Group Borreliae stop expressing OspA and OspB on the surface and express OspC, which is activated during the first day of the blood meal and peaks 48 hours after the Ixodes spp. tick bite [51].…”