Open reading frame III of borna disease virus encodes a nonglycosylated matrix protein.

Abstract:

: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.

journal_name

J Virol

journal_title

Journal of virology

authors

Kraus I,Eickmann M,Kiermayer S,Scheffczik H,Fluess M,Richt JA,Garten W

doi

10.1128/JVI.75.24.12098-12104.2001

subject

Has Abstract

pub_date

2001-12-01 00:00:00

pages

12098-104

issue

24

eissn

0022-538X

issn

1098-5514

journal_volume

75

pub_type

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