Single amino acid substitution of Sendai virus at the cleavage site of the fusion protein confers trypsin resistance.
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 trypsin-sensitive 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.
Itoh
M
M
Department of Microbiology, Kobe University School of Medicine, Japan.
Shibuta
H
H
Homma
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D004252:DNA Mutational Analysis; D005814:Genes, Viral; D008969:Molecular Sequence Data; D010222:Parainfluenza Virus 1, Human / Q000502:physiology*; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000378:metabolism; D014760:Viral Fusion Proteins / Q000235:genetics / Q000502:physiology*
D014760:Viral Fusion Proteins; D014357:Trypsin