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J Gen Virol 68 (1987), 2939-2944; DOI 10.1099/0022-1317-68-11-2939
© 1987 Society for General Microbiology

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Single Amino Acid Substitution of Sendai Virus at the Cleavage Site of the Fusion Protein Confers Trypsin Resistance

Masae Itoh, Hiroshi Shibuta1 and Morio Homma

Department of Microbiology, Kobe University School of Medicine, Kusunoki-cho, Chuo-ku, Kobe 650 Japan
and1 Department of Viral Infection, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan

Amino acid sequences of fusion (F) proteins of two trypsin-resistant mutants of Sendai virus, TR-2 and TR-5, were deduced from nucleotide analysis of cDNA encoding the F gene and were compared with that of the trypsin-sensitive wild-type Sendai virus. In both mutants, amino acid substitutions were found at residues 116 (Arg -> Ile), the cleavage site of the F protein, and 109 (Asn -> Asp). Two trypsinsensitive revertants, TSrev-52 and TSrev-58, derived from TR-5 were both activated by trypsin similarly to the wild-type virus and had a single amino acid reversion from Ile to Arg at residue 116, leaving Asp as before at residue 109. These results indicate that the trypsin sensitivity of Sendai virus can be changed by a single amino acid substitution at the cleavage site of the F protein and a mutation from Arg to Ile is responsible for the acquisition of resistance to trypsin.

Keywords: Sendai virus, trypsin resistant mutant, fusion protein

Received 25 March 1987; accepted 22 July 1987.


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M. Itoh, H. Hotta, and M. Homma
Increased Induction of Apoptosis by a Sendai Virus Mutant Is Associated with Attenuation of Mouse Pathogenicity
J. Virol., April 1, 1998; 72(4): 2927 - 2934.
[Abstract] [Full Text] [PDF]




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