Mutational analysis of the proteolytic cleavage site of glycoprotein B (gB) of Marek's disease virus.

Abstract

The Marek's disease virus (MDV) glycoprotein B (gB) precursor, gp100, is proteolytically cleaved into two disulfide-linked subunits, gp60 and gp49. In the gB homologs of most other herpesviruses, a tetrapeptide, Arg-Xaa-Arg-Arg, is immediately upstream from the predicted cleavage site. We have investigated the specificity of the proteolytic cleavage in gp100 by introducing mutations within its predicted cleavage site (Arg-Leu-Arg-Arg) and expressed these mutants in recombinant fowlpox virus (FPV). The results show that all three Arg residues at the predicted cleavage site play an important role in the specific proteolytic cleavage of gp100. Furthermore, we demonstrated that the cleavage of gp100 is not necessary for transport of gB to the cell surface.

• Authors: S Yoshida, L F Lee, N Yanagida, K Nazerian
• Journal: Gene (Gene) Vol. 150 Issue 2 Pg. 303-6 (Dec 15 1994) ISSN: 0378-1119 [Print] Netherlands
• PMID: 7821796 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antigens, Viral
• DNA Primers
• Protein Precursors
• Viral Envelope Proteins
• glycoprotein B, Marek's disease virus
• Methionine
• Endopeptidases

Topics

• Amino Acid Sequence
• Animals
• Antigens, Viral (biosynthesis)
• Base Sequence
• Cell Line
• Consensus Sequence
• DNA Mutational Analysis
• DNA Primers
• Endopeptidases (metabolism)
• Gene Expression
• Herpesvirus 2, Gallid (genetics, metabolism)
• Kinetics
• Methionine (metabolism)
• Molecular Sequence Data
• Mutagenesis, Site-Directed
• Protein Precursors (metabolism)
• Protein Processing, Post-Translational
• Sequence Homology, Amino Acid
• Substrate Specificity
• Viral Envelope Proteins (biosynthesis)