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Amino-terminal precursor sequence modulates canine distemper virus fusion protein function
Veronika von Messling1, Roberto Cattaneo
1Molecular Medicine Program, Mayo Clinic, Rochester, Minnesota 55905, USA.
Journal of Virology
|April 5, 2002
Summary
Canine distemper virus (CDV) fusion (F) protein has a unique precursor, PreF(0), which is cleaved to release a peptide that modulates F protein activity, making it more stable but less active.
Area of Science:
- Virology
- Molecular Biology
- Protein Biochemistry
Background:
- Paramyxovirus fusion (F) proteins are typically type I glycoproteins with short hydrophobic leader sequences.
- Canine distemper virus (CDV) presents a complex F protein reading frame with a hydrophobic sequence downstream of the initial AUG.
Purpose of the Study:
- To investigate the translation and function of the CDV F protein, particularly the region preceding the hydrophobic sequence.
- To determine if a short-lived precursor protein, PreF(0), and its cleaved peptide, Pre, influence F protein activity.
Main Methods:
- Production of specific antiserum to detect the F protein precursor.
- Identification and half-life measurement of the Pre peptide.
- Comparison of F protein function with and without the Pre peptide.
Main Results:
- A short-lived F protein precursor, PreF(0), was detected, with its cleavage product, the Pre peptide, having a half-life of approximately 30 minutes.
- PreF(0) cleavage precedes the activation of F(0) into F(1) and F(2) subunits by furin.
- F proteins synthesized with the Pre peptide exhibited increased stability and reduced activity compared to those with a shorter signal sequence.
Conclusions:
- The Pre peptide plays a crucial role in modulating the function and stability of the CDV F protein.
- This finding highlights a unique regulatory mechanism for paramyxovirus fusion proteins, distinct from the classical model.