Identification of the amino terminal subunit of the glycoprotein of Borna disease virus |
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Authors: | Kiermayer Simone Kraus Ina Richt Jürgen A Garten Wolfgang Eickmann Markus |
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Institution: | Institut für Virologie der Philipps-Universit?t Marburg, Marburg, Germany. |
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Abstract: | The only surface membrane glycoprotein of Borna disease virus (BDV) is synthesized as a polypeptide with a molecular mass of 57 kDa and N-glycosylated to a precursor glycoprotein (GP) of about 94 kDa. It is processed by the cellular protease furin into the C-terminal membrane-anchored subunit GP-C, also known as gp43, and a presumptive N-terminal subunit GP-N, that is highly glycosylated and has a molecular mass of about 51 kDa. However, up to now the latter remained undetected in BDV-infected material. We describe a novel approach to identify glycan masked linear antigenic epitopes. In the present study, GP-N was identified in BDV-infected cells by a combination of lectin precipitation, enzymatic deglycosylation on blot and immunochemistry using an N-terminal specific antiserum. The GP-N has an apparent molecular mass of 45-50 kDa in its glycosylated form and 27 kDa in its deglycosylated form. N-glycan analysis revealed that the precursor GP contains only mannose-rich N-glycans, whereas GP-N and GP-C contain mannose-rich and complex-type N-glycans. |
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Keywords: | Borna disease virus Glycoprotein Amino terminal subunit Carbohydrate masking Blot deglycosylation |
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