An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes

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 a...

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Autores principales: Murase, Y., Konnai, S., Yamada, S., Githaka, Naftaly W., Isezaki, M., Ito, T., Takano, A., Ando, S., Kawabata, H., Murata, S., Ohashi, K.
Formato: Journal Article
Lenguaje:Inglés
Publicado: Elsevier 2015
Materias:
Acceso en línea:https://hdl.handle.net/10568/80666
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author Murase, Y.
Konnai, S.
Yamada, S.
Githaka, Naftaly W.
Isezaki, M.
Ito, T.
Takano, A.
Ando, S.
Kawabata, H.
Murata, S.
Ohashi, K.
author_browse Ando, S.
Githaka, Naftaly W.
Isezaki, M.
Ito, T.
Kawabata, H.
Konnai, S.
Murase, Y.
Murata, S.
Ohashi, K.
Takano, A.
Yamada, S.
author_facet Murase, Y.
Konnai, S.
Yamada, S.
Githaka, Naftaly W.
Isezaki, M.
Ito, T.
Takano, A.
Ando, S.
Kawabata, H.
Murata, S.
Ohashi, K.
author_sort Murase, Y.
collection Repository of Agricultural Research Outputs (CGSpace)
description 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.
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spelling CGSpace806662023-12-08T19:36:04Z An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes Murase, Y. Konnai, S. Yamada, S. Githaka, Naftaly W. Isezaki, M. Ito, T. Takano, A. Ando, S. Kawabata, H. Murata, S. Ohashi, K. animal health cattle antibodies borrelia burgdorferi borreliosis immunity animal diseases 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. 2015-05 2017-04-05T10:33:14Z 2017-04-05T10:33:14Z Journal Article https://hdl.handle.net/10568/80666 en Limited Access Elsevier Murase, Y., Konnai, S., Yamada, S., Githaka, N., Isezaki, M., Ito, T., Takano, A., Ando, S., Kawabata, H., Murata, S. and Ohashi, K. 2015. An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes. Insect Biochemistry and Molecular Biology 60: 59–67.
spellingShingle animal health
cattle
antibodies
borrelia burgdorferi
borreliosis
immunity
animal diseases
Murase, Y.
Konnai, S.
Yamada, S.
Githaka, Naftaly W.
Isezaki, M.
Ito, T.
Takano, A.
Ando, S.
Kawabata, H.
Murata, S.
Ohashi, K.
An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes
title An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes
title_full An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes
title_fullStr An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes
title_full_unstemmed An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes
title_short An investigation of binding ability of Ixodes persulcatus Schulze Salp15 with Lyme disease spirochetes
title_sort investigation of binding ability of ixodes persulcatus schulze salp15 with lyme disease spirochetes
topic animal health
cattle
antibodies
borrelia burgdorferi
borreliosis
immunity
animal diseases
url https://hdl.handle.net/10568/80666
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