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

I Kraus1, M Eickmann, S Kiermayer

  • 1Institut für Virologie, Philipps-Universität Marburg, D-35037 Marburg, Germany.

Journal of Virology
|November 17, 2001
PubMed

Insights

Borna disease virus (BDV) p16 protein is not N-glycosylated and is not an integral membrane protein. Instead, it functions as a nonglycosylated matrix protein on the inner viral membrane surface.

Area of Science:

  • Virology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Borna disease virus (BDV) open reading frame III encodes a 16 kDa protein (p16/BDV-M).
  • Previous studies suggested p16 is N-glycosylated (gp18), despite lacking consensus glycosylation sites.

Purpose of the Study:

  • To investigate the glycosylation status of BDV p16.
  • To determine the membrane topology of BDV p16.

Main Methods:

  • Analysis of p16 processing using N- and C-terminal specific antisera.
  • Testing for N-glycosylation using endoglycosidases and lectin binding.
  • Site-directed mutagenesis to introduce N-glycosylation sites.
  • Density gradient flotation experiments to assess membrane association.

Main Results:

  • No evidence of N- or C-terminal peptide cleavage during p16 maturation.
  • No detectable deglycosylation or lectin binding, indicating lack of N-glycosylation.
  • Introduced N-glycosylation sites did not result in carbohydrate attachment.
  • p16 dissociated from membranes, indicating it is not an integral membrane protein.

Conclusions:

  • BDV p16 is a nonglycosylated matrix protein.
  • p16 associates with the inner surface of the viral membrane.
  • Findings align with matrix protein characteristics in other Mononegavirales.

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