title: Shedding of vesicular stomatitis virus soluble glycoprotein by removal of carboxy-terminal peptide.
abstract: A comparison of partial NH2-terminal sequences of vesicular stomatitis viral glycoprotein G (molecular weight, 69,000) and the soluble extracellular glycoprotein antigen Gs (molecular weight, 57,000) shows that both of the sequences are identical. Tryptic fingerprint analyses show that Gs lacks the carboxy-terminal region containing the membrane-anchoring hydrophobic domain of G. These results suggest that Gs is formed by cleavage in the carboxy-terminal region of G.
mesh_terms: D000595:Amino Acid Sequence; D000956:Antigens, Viral / Q000378:metabolism*; D005110:Extracellular Space / Q000276:immunology; D008562:Membrane Glycoproteins; D010455:Peptides / Q000032:analysis; D014357:Trypsin; D014721:Vesicular stomatitis Indiana virus / Q000276:immunology*; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D000956:Antigens, Viral; C028391:G protein, vesicular stomatitis virus; D008562:Membrane Glycoproteins; D010455:Peptides; D014759:Viral Envelope Proteins; D014764:Viral Proteins; D014357:Trypsin