1887

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Volume 69, Issue 11

Single Amino Acid Change at the Cleavage Site of the Fusion Protein Is Responsible for Both Enhanced Chymotrypsin Sensitivity and Trypsin Resistance of a Sendai Virus Mutant, TR-5 Free

Abstract

Summary

A trypsin-resistant mutant of Sendai virus, TR-5, which was obtained by passaging the wild-type (wt) virus in the presence of chymotrypsin followed by plaque purification, also had an enhanced susceptibility to activation by chymotrypsin. A trypsin-sensitive revertant, TSrev-58, derived from TR-5 had a decreased susceptibility to chymotrypsin and was susceptible to trypsin to the same degree as the wt virus. Based on the facts that TR-5 had an amino acid change (Arg→Ile) at residue 116 of the fusion (F) protein, which is the cleavage site for trypsin in the wt virus F protein, and that this change had reverted in TSrev-58, it was concluded that the above amino acid change was responsible for both the enhanced chymotrypsin sensitivity and the trypsin resistance of TR-5. In this paper, the cleavage site of the F protein of TR-5 by chymotrypsin was determined in comparison with those of the wt virus and TSrev-58. The cleavage sites were not different among these viruses, being located between residues 114 (Gln) and 115 (Ser), the two residues at the N-terminal side of the trypsin cleavage site. A possible reason for the increased susceptibility of TR-5 to chymotrypsin is discussed.

  • Received:
  • Accepted:
  • Published Online:
Keyword(s): fusion protein , Sendai virus and trypsin-resistant mutant
© Society for General Microbiology 1988
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1988-11-01
2024-04-30
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Single Amino Acid Change at the Cleavage Site of the Fusion Protein Is Responsible for Both Enhanced Chymotrypsin Sensitivity and Trypsin Resistance of a Sendai Virus Mutant, TR-5
J. Gen. Virol. 69, 2907 (1988); https://doi.org/10.1099/0022-1317-69-11-2907
/content/journal/jgv/10.1099/0022-1317-69-11-2907
/content/journal/jgv/10.1099/0022-1317-69-11-2907
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