Open Reading Frame III of Borna Disease Virus Encodes a Nonglycosylated Matrix Protein

AUTOR(ES)

Kraus, Ina

FONTE

American Society for Microbiology

RESUMO

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.

Documentos Relacionados

• Norwalk Virus Open Reading Frame 3 Encodes a Minor Structural Protein
• Open reading frame vpr of simian immunodeficiency virus encodes a virion-associated protein.
• Modulation of Borna Disease Virus Phosphoprotein Nuclear Localization by the Viral Protein X Encoded in the Overlapping Open Reading Frame
• Sequence variability of Borna disease virus open reading frame II found in human peripheral blood mononuclear cells.
• The herpes simplex virus Us11 open reading frame encodes a sequence-specific RNA-binding protein.