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10.1292/jvms.71.243 http://scihub22266oqcxt.onion/10.1292/jvms.71.243 19262042!ä!19262042 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Vet+Med+Sci 2009 ; 71 (2): 243-6 Nephropedia Template TP {{tp|p=19262042|t=2009. Binding properties of GP1 protein of Borna disease virus |pdf=|usr=}}{{19262042}} gab.com Text Binding properties of GP1 protein of Borna disease virus JO: J Vet Med Sci http://www.kidney.de/pget.php?&tw=1&pmid=19262042 #FOAvip The surface glycoprotein (G) of Borna disease virus (BDV) plays central roles in the process of viral entry. BDV G is cleaved by cellular furin-like proteases into two components, GP1 and GP2. Although GP1 is involved in the virus entry into cells, the binding activity of GP1 to cells is unknown. Therefore, we expressed the wild-type GP1 and a variety of GP1 deletion mutants that were FLAG-tagged at the C-terminus in human embryonic kidney 293T cells. These proteins were then purified using an anti-FLAG antibody and evaluated for their ability to bind to cell lines. GP1 bound to BDV-permissive cells but not to non-permissive cells. GP1 also inhibited BDV infection via its binding to cells. This binding assay should prove useful to map the receptor-binding domain of BDV. Twit Text FOAVip Binding properties of GP1 protein of Borna disease virus ????J Vet Med Sci http://www.kidney.de/pget.php?&tw=1&pmid=19262042 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19262042 #FOAvip English Wikipedia <ref>{{Cite pmid|19262042}}</ref> Binding properties of GP1 protein of Borna disease virus #MMPMID19262042 Makino A; Horimoto T; Kawaoka Y J Vet Med Sci 2009[Feb]; 71 (2): 243-6 PMID19262042show ga The surface glycoprotein (G) of Borna disease virus (BDV) plays central roles in the process of viral entry. BDV G is cleaved by cellular furin-like proteases into two components, GP1 and GP2. Although GP1 is involved in the virus entry into cells, the binding activity of GP1 to cells is unknown. Therefore, we expressed the wild-type GP1 and a variety of GP1 deletion mutants that were FLAG-tagged at the C-terminus in human embryonic kidney 293T cells. These proteins were then purified using an anti-FLAG antibody and evaluated for their ability to bind to cell lines. GP1 bound to BDV-permissive cells but not to non-permissive cells. GP1 also inhibited BDV infection via its binding to cells. This binding assay should prove useful to map the receptor-binding domain of BDV. |*Protein Processing, Post-Translational[MESH] |Animals[MESH] |Antibodies, Anti-Idiotypic/genetics/metabolism[MESH] |Biological Assay[MESH] |Borna disease virus/*genetics/metabolism/pathogenicity[MESH] |Cell Line/*metabolism[MESH] |Humans[MESH] |Kidney/cytology[MESH] |Membrane Glycoproteins/genetics/*metabolism[MESH] |Protein Binding[MESH] |Sequence Deletion[MESH]Binding properties of GP1 protein of Borna disease virus (epmc).pdf DeepDyve Pubget Overpricing