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Borrelia burgdorferi  synthesizes an HtrA protease (BbHtrA) which is a surface-exposed, conserved protein within Lyme disease spirochetes with activity toward CheX and BmpD of  Borrelia  spp, as well as aggrecan, fibronectin and proteoglycans found in skin, joints and neural tissues of vertebrates. An antibody response against BbHtrA is observed in Lyme disease patients and in experimentally infected laboratory mice and rabbits. Given the surface location of BbHtrA on  B .  burgdorferi  and its ability to elicit an antibody response in infected hosts, we explored recombinant BbHtrA as a potential vaccine candidate in a mouse model of tick-transmitted Lyme disease. We immunized mice with two forms of BbHtrA: the proteolytically active native form and BbHtrA ablated of activity by a serine to alanine mutation at amino acid 226 (BbHtrA S226A ). Although inoculation with either BbHtrA or BbHtrA S226A  produced high-titer antibody responses in C3H/HeJ mice, neither antigen was successful in protecting mice from  B .  burgdorferi  challenge. These results indicate that the search for novel vaccine candidates against Lyme borreliosis remains a challenge.

Evaluation of Borrelia burgdorferi BbHtrA Protease as a Vaccine Candidate for Lyme Borreliosis in Mice