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Journal of General Virology header logo Journal of General Virology

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 No Access

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.

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Keyword(s): fusion protein , Sendai virus and trypsin-resistant mutant
© Society for General Microbiology 1988
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1988-11-01
2025-12-14

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/content/journal/jgv/10.1099/0022-1317-69-11-2907
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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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