Pneumopathogenicity in mice of a Sendai virus mutant, TSrev-58, is accompanied by in vitro activation with trypsin.
The pneumopathogenicity of a trypsin-sensitive revertant of Sendai virus, TSrev-58, which was derived from a trypsin-resistant mutant, TR-5, was examined in mice. In comparison with TR-5, the revertant had a single amino acid substitution at residue 116 (Ile----Arg) on F protein, which was the cleavage site, and had the same trypsin sensitivity as the wild-type virus. However, TSrev-58 still had a single amino acid difference from the wild-type virus at residue 109 (Asn----Asp) (M. Itoh, H. Shibuta, and M. Homma, J. Gen. Virol. 68:2939-2943, 1987). Nevertheless, the present study revealed that TSrev-58 had the same pneumopathogenicity in mice as the wild-type virus. This result indicates that the activating protease of Sendai virus present in the lungs of mice is quite similar to trypsin and also that the in vitro trypsin sensitivity of Sendai virus can be a good marker of pneumopathogenicity in mice.
Mochizuki
Y
Y
Department of Microbiology, Kobe University School of Medicine, Japan.
Tashiro
M
M
Homma
M
M
D000595:Amino Acid Sequence; D000818:Animals; D008171:Lung Diseases / Q000382:microbiology* / Q000473:pathology; D051379:Mice; D010222:Parainfluenza Virus 1, Human / Q000235:genetics / Q000472:pathogenicity*; D014357:Trypsin / Q000378:metabolism; D014760:Viral Fusion Proteins / Q000502:physiology*; D014779:Virus Replication
D014760:Viral Fusion Proteins; D014357:Trypsin