title: Topographical analysis of the G virion of Aleutian mink disease parvovirus with monoclonal antibodies.
abstract: The topography of the Aleutian mink disease parvovirus (ADV) G virion was analyzed with monoclonal antibodies and polyclonal antiserum. There was homology between the two major structural proteins as others have previously reported. Trypsin treatment of the virion with subsequent immunoblotting revealed that VP2 represents the main peptide on the exterior of virion and that VP1 is probably embedded within the capsid. Additional analyses of the trypsin-treated virions showed that VP2 is responsible for binding complement and that it also represents the structural part of the virion that binds to cellular receptors. A third protein, p34, was detected that might represent a third structural polypeptide because of its many unique epitopes relative to the other peptides detected.
mesh_terms: D000454:Aleutian Mink Disease Virus / Q000276:immunology* / Q000648:ultrastructure; D000911:Antibodies, Monoclonal / Q000276:immunology; D000914:Antibodies, Viral / Q000276:immunology; D000918:Antibody Specificity; D015153:Blotting, Western; D002213:Capsid / Q000276:immunology; D002500:Centrifugation, Isopycnic; D003168:Complement Fixation Tests; D000939:Epitopes; D008970:Molecular Weight; D010446:Peptide Fragments / Q000276:immunology; D014357:Trypsin; D014764:Viral Proteins / Q000737:chemistry / Q000276:immunology*; D014771:Virion / Q000648:ultrastructure*
chemical_list: D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D000939:Epitopes; D010446:Peptide Fragments; D014764:Viral Proteins; D014357:Trypsin