Analysis of the virion of Aleutian disease virus of mink

The ADV-G virion was analyzed with monoclonal antibodies and polyclonal antiserum. There was homology between the two major structural proteins, p66.5 and p82, as others have previously reported. Trypsin treatment of the virion with subsequent immunoblotting revealed that the 66.5K peptide represents the main peptide on the exterior of virion, and that p82 is probably embedded within the capsid. Additional analyses of the trypsin-treated virions showed that p66.5 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.; The higher molecular weight peptides (104-126K) probably represent products of denaturation of the virions, while the 58.6K and 51.6K peptides may be breakdown products from the 66.5K polypeptide or alternatively products of multiply spliced transcripts. If the 82K and 66.5K peptides are breakdown products instead of the main viral polypeptides, then p86 and p73.4 might represent the true viral polypeptides from which the 82K and 66.5K peptides are derived.