Salp15, a 15-kDa tick
salivary gland protein, has several suppressive modes of activity against host immunity and plays a critical role in the transmission of
Lyme disease spirochetes in Ixodes scapularis and Ixodes ricinus, major vectors of
Lyme disease in North America and Western Europe. Salp15 adheres to Borrelia burgdorferi and specifically interacts with its
outer surface protein C (
OspC), protecting the spirochete from antibody-mediated cytotoxicity and facilitating
infection in the mice. Recently, we identified two Salp15 homologues, IperSalp15-1 and IperSalp15-2, in Ixodes persulcatus, a vector for
Lyme disease in Japan. Here we describe the function of IperSalp15 in the transmission of
Lyme borreliosis. To investigate the function of IperSalp15, recombinant IperSalp15-1 and IperSalp15-2 were prepared in bacterial and insect cells. Both were identified in the sera of tick-immunized hamsters, indicating that these are secretory
proteins in exposed host animals. Solid-phase overlay and indirect fluorescence assays showed that IperSalp15 binds to
OspC from B. burgdorferi, Borrelia garinii, and Borrelia afzelii. Importantly, this binding likely protected the spirochete from antibody-mediated cytotoxicity in vitro. In addition, IperSalp15 tended to facilitate
infection in mice. Thus, further characterization of tick molecules, including IperSalp15, could lead to the development of new strategies to prevent the transmission of
tick-borne diseases.