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lüll Cell entry of Borna disease virus follows a clathrin-mediated endocytosis pathway that requires Rab5 and microtubules Clemente R; de la Torre JCJ Virol 2009[Oct]; 83 (20): 10406-16Borna disease virus (BDV), the prototypic member of the Bornaviridae family within the order Mononegavirales, exhibits high neurotropism and provides an important and unique experimental model system for studying virus-cell interactions within the central nervous system. BDV surface glycoprotein (G) plays a critical role in virus cell entry via receptor-mediated endocytosis, and therefore, G is a critical determinant of virus tissue and cell tropism. However, the specific cell pathways involved in BDV cell entry have not been determined. Here, we provide evidence that BDV uses a clathrin-mediated, caveola-independent cell entry pathway. We also show that BDV G-mediated fusion takes place at an optimal pH of 6.0 to 6.2, corresponding to an early-endosome compartment. Consistent with this finding, BDV cell entry was Rab5 dependent but Rab7 independent and exhibited rapid fusion kinetics. Our results also uncovered a key role for microtubules in BDV cell entry, whereas the integrity and dynamics of actin cytoskeleton were not required for efficient cell entry of BDV.|*Endocytosis[MESH]|*Host-Pathogen Interactions[MESH]|Animals[MESH]|Borna Disease/virology[MESH]|Borna disease virus/genetics/metabolism/*pathogenicity[MESH]|Cell Line[MESH]|Chlorocebus aethiops[MESH]|Clathrin/metabolism/pharmacology[MESH]|Humans[MESH]|Microtubules/*metabolism[MESH]|Oligodendroglia/*virology[MESH]|Vero Cells[MESH]|Virus Internalization[MESH]|rab5 GTP-Binding Proteins/genetics/*metabolism[MESH] |