Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface.
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.
partment of Virology, Research Institute for Microbial Diseases (BIKEN), Osaka University, Suita, Osaka 565-0871, Japan.
Tomoyuki
T
Honda
Masayuki
M
Horie
Takuji
T
Daito
Kazuyoshi
K
Ikuta
Keizo
K
Tomonaga
D001891:Borna disease virus / Q000502:physiology*; D002460:Cell Line; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D009836:Oligodendroglia / Q000821:virology; D011485:Protein Binding; D025941:Protein Interaction Mapping; D015678:Viral Structural Proteins / Q000378:metabolism*; D053586:Virus Internalization
D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D015678:Viral Structural Proteins