| Autor: |
Kraus, Ina, Eickmann, Markus, Kiermayer, Simone, Scheffczik, Hanno, Fluess, Manuela, Richt, Ju¨rgen A., Garten, Wolfgang |
| Zdroj: |
The Journal of Virology; December 2001, Vol. 75 Issue: 24 p12098-12104, 7p |
| Abstrakt: |
ABSTRACTThe open reading frame III of Borna disease virus (BDV) codes for a protein with a mass of 16 kDa, named p16 or BDV-M. p16 was described as an N-glycosylated protein in several previous publications and therefore was termed gp18, although the amino acid sequence of p16 does not contain any regular consensus sequence for N glycosylation. We examined glycosylation of p16 and studied its membrane topology using antisera raised against peptides, which comprise the N and the C termini. Neither an N- nor a C-terminal peptide is cleaved from p16 during maturation. Neither deglycosylation of p16 by endoglycosidases nor binding of lectin to p16 was detectable. Introduction of typical N-glycosylation sites at the proposed sites of p16 failed in carbohydrate attachment. Flotation experiments with membranes of BDV-infected cells on density gradients revealed that p16 is not an integral membrane protein, since it can be dissociated from membranes. Our experimental data strongly suggest that p16 is a typical nonglycosylated matrix protein associated at the inner surface of the viral membrane, as is true for homologous proteins of other members of the Mononegaviralesorder. |
| Databáze: |
Supplemental Index |
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