Biologically active peptides of the vesicular stomatitis virus glycoprotein.
A peptide corresponding to the amino-terminal 25 amino acids of the mature vesicular stomatitis virus glycoprotein has recently been shown to be a pH-dependent hemolysin. In the present study, we analyzed smaller constituent peptides and found that the hemolytic domain resides within the six amino-terminal amino acids. Synthesis of variant peptides indicates that the amino-terminal lysine can be replaced by another positively charged amino acid (arginine) but that substitution with glutamic acid results in the total loss of the hemolytic function. Peptide-induced hemolysis was dependent upon buffer conditions and was inhibited when isotonicity was maintained with mannitol, sucrose, or raffinose. In sucrose, all hemolytic peptides were also observed to mediate hemagglutination. The large 25-amino acid peptide is also a pH-dependent cytotoxin for mammalian cells and appears to effect gross changes in cell permeability. Conservation of the amino terminus of vesicular stomatitis virus and rabies virus suggests that the membrane-destabilizing properties of this domain may be important for glycoprotein function.
Schlegel
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Wade
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D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002470:Cell Survival / Q000187:drug effects; D002522:Chlorocebus aethiops; D006384:Hemagglutination; D006460:Hemolysin Proteins / Q000633:toxicity; D006461:Hemolysis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007668:Kidney; D007700:Kinetics; D008562:Membrane Glycoproteins; D010446:Peptide Fragments / Q000032:analysis; D012756:Sheep; D014721:Vesicular stomatitis Indiana virus / Q000502:physiology*; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000302:isolation & purification*
C028391:G protein, vesicular stomatitis virus; D006460:Hemolysin Proteins; D008562:Membrane Glycoproteins; D010446:Peptide Fragments; D014759:Viral Envelope Proteins; D014764:Viral Proteins