TY - JOUR
T1 - Amino-terminal precursor sequence modulates canine distemper virus fusion protein function
AU - Von Messling, Veronika
AU - Cattaneo, Roberto
PY - 2002
Y1 - 2002
N2 - The fusion (F) proteins of most paramyxoviruses are classical type I glycoproteins with a short hydrophobic leader sequence closely following the translation initiation codon. The predicted reading frame of the canine distemper virus (CDV) F protein is more complex, with a short hydrophobic sequence beginning 115 codons downstream of the first AUG. To verify if the sequence between the first AUG and the hydrophobic region is translated, we produced a specific antiserum that indeed detected a short-lived F protein precursor that we named PreF0. A peptide resulting from PreF0 cleavage was identified and named Pre, and its half-life was measured to be about 30 min. PreF0 cleavage was completed before proteolytic activation of F0 into its F1 and F2 subunits by furin. To test the hypothesis that the Pre peptide may influence protein activity, we compared the function of F proteins synthesized with that peptide to that of F proteins synthesized with a shorter amino-terminal signal sequence. F proteins synthesized with the Pre peptide were more stable and less active. Thus, the Pre peptide modulates the function of the CDV F protein. Interestingly, a distinct two-hit activation process has been recently described for human respiratory syncytial virus, another paramyxovirus.
AB - The fusion (F) proteins of most paramyxoviruses are classical type I glycoproteins with a short hydrophobic leader sequence closely following the translation initiation codon. The predicted reading frame of the canine distemper virus (CDV) F protein is more complex, with a short hydrophobic sequence beginning 115 codons downstream of the first AUG. To verify if the sequence between the first AUG and the hydrophobic region is translated, we produced a specific antiserum that indeed detected a short-lived F protein precursor that we named PreF0. A peptide resulting from PreF0 cleavage was identified and named Pre, and its half-life was measured to be about 30 min. PreF0 cleavage was completed before proteolytic activation of F0 into its F1 and F2 subunits by furin. To test the hypothesis that the Pre peptide may influence protein activity, we compared the function of F proteins synthesized with that peptide to that of F proteins synthesized with a shorter amino-terminal signal sequence. F proteins synthesized with the Pre peptide were more stable and less active. Thus, the Pre peptide modulates the function of the CDV F protein. Interestingly, a distinct two-hit activation process has been recently described for human respiratory syncytial virus, another paramyxovirus.
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U2 - 10.1128/JVI.76.9.4172-4180.2002
DO - 10.1128/JVI.76.9.4172-4180.2002
M3 - Article
C2 - 11932382
AN - SCOPUS:0036227311
SN - 0022-538X
VL - 76
SP - 4172
EP - 4180
JO - Journal of virology
JF - Journal of virology
IS - 9
ER -