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Identification of the amino terminal subunit of the glycoprotein of Borna disease virus
Author(s) -
Kiermayer Simone,
Kraus Ina,
Richt Jürgen A,
Garten Wolfgang,
Eickmann Markus
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03513-5
Subject(s) - glycoprotein , epitope , glycan , protein subunit , biochemistry , molecular mass , protease , microbiology and biotechnology , mannose , lectin , biology , glycosylation , chemistry , antigen , enzyme , gene , immunology
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.