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Journal of Virology, December 2001, p. 12098-12104, Vol. 75, No. 24
Institut für Virologie,
Philipps-Universität Marburg, D-35037
Marburg,1 and Institut für
Virologie, Justus-Liebig-Universität Giessen, D-35392
Giessen,2 Germany
Received 20 July 2001/Accepted 24 September 2001
The 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 Mononegavirales order.
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.24.12098-12104.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Open Reading Frame III of Borna Disease Virus
Encodes a Nonglycosylated Matrix Protein
and
*
Corresponding author. Mailing address: Institut
für Virologie, Robert-Koch-Str. 17, D-35037 Marburg, Germany.
Phone: (49) 6421-28-65145. Fax: (49) 6421-28-68962. E-mail:
garten{at}mailer.unimarburg.de.
Present address: National Animal Disease Center, Ames, IA 50010.
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