title: Purification and location of the major glycoprotein of vaccinia virus.
abstract: A glycoprotein component of vaccinia virus was extracted with a non-ionic detergent NP-40 (Nonidet P-40) and purified by gel chromatography. The single antigen extracted by the detergent had a molecular weight estimated between 100,000 and 200,000 daltons. This glycoprotein was found to contain less than 1% hexosamine which would correspond to 5--10 sugar residues per molecule. Antibodies produced against this glycoprotein were able to neutralize vaccinia virus. Using immunoelectron microscopy, this molecule was found to be located in the outer layer of the virion. These results further suggest that this protein called complex E (for external) is a surface component of vaccinia virus.
mesh_terms: D000937:Antigen-Antibody Reactions; D006023:Glycoproteins / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D006595:Hexosamines / Q000032:analysis; D008854:Microscopy, Electron; D008970:Molecular Weight; D014616:Vaccinia virus / Q000032:analysis* / Q000276:immunology / Q000648:ultrastructure; D014764:Viral Proteins / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*
chemical_list: D006023:Glycoproteins; D006595:Hexosamines; D014764:Viral Proteins