Binding of viral glycoprotein with trypsin and its relation to virulency. I. Initial step of binding.
The interaction between surface proteins of some enveloped viruses and trypsin was studied by computer analysis. Prior to the cleavage of the viral protein by trypsin, hydrophobic interaction between them at the vicinity of their active sites may occur. An exposed hydrophobic portion was found there which theoretically could stimulate the interaction. This interaction would be rather non-specific: according to the analysis, trypsin could bind equally well with weakly virulent virus and virulent viruses. Following this interaction, a specific reaction between their active sites would occur. The specificity was found to be related to the virulency of the virus.
Shimamoto
T
T
Institute for Molecular and Cellular Biology, Osaka University, Japan.
Shimamoto
T
T
Okada
Y
Y
Yamada
N
N
Miyata
K
K
Kiho
Y
Y
D000595:Amino Acid Sequence; D001665:Binding Sites; D046911:Macromolecular Substances; D008432:Mathematical Computing; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012984:Software; D014357:Trypsin / Q000737:chemistry / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000378:metabolism*; D014760:Viral Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D014774:Virulence; D014780:Viruses / Q000378:metabolism* / Q000472:pathogenicity
D046911:Macromolecular Substances; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins; D014357:Trypsin