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Journal of Virology, December 2009, p. 12622-12625, Vol. 83, No. 23
0022-538X/09/$08.00+0     doi:10.1128/JVI.01201-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Molecular Chaperone BiP Interacts with Borna Disease Virus Glycoprotein at the Cell Surface{triangledown} ,{dagger}

Tomoyuki Honda,1,2* Masayuki Horie,1 Takuji Daito,1 Kazuyoshi Ikuta,1 and Keizo Tomonaga1,3*

Department of Virology, Research Institute for Microbial Diseases (BIKEN), Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan,1 Japan Society for the Promotion of Science (JSPS), Chiyoda-ku, Tokyo 102-8472, Japan,2 PRESTO, Japan Science and Technology Agency (JST), Chiyoda-ku, Tokyo 102-0075, Japan3

Received 11 June 2009/ Accepted 15 September 2009

Borna disease virus (BDV) is characterized by highly neurotropic infection. BDV enters its target cells using virus surface glycoprotein (G), but the cellular molecules mediating this process remain to be elucidated. We demonstrate here that the N-terminal product of G, GP1, interacts with the 78-kDa chaperone protein BiP. BiP was found at the surface of BDV-permissive cells, and anti-BiP antibody reduced BDV infection as well as GP1 binding to the cell surface. We also reveal that BiP localizes at the synapse of neurons. These results indicate that BiP may participate in the cell surface association of BDV.

* Corresponding author. Mailing address: Department of Virology, Research Institute for Microbial Diseases (BIKEN), Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan. Phone: 81-6-6879-8308. Fax: 81-6-6879-8310. E-mail for K. Tomonaga: tomonaga{at}biken.osaka-u.ac.jp. E-mail for T. Honda: tomohond{at}biken.osaka-u.ac.jp

{triangledown} Published ahead of print on 23 September 2009.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.

Journal of Virology, December 2009, p. 12622-12625, Vol. 83, No. 23
0022-538X/09/$08.00+0     doi:10.1128/JVI.01201-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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