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1 Department of Medicine, School of Medicine,
2 Department of Epidemiology, School of Public Health, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7030
and3 Department of Microbiology, Parasitology and Pathology, College of Veterinary Medicine, North Carolina State University, Raleigh, North Carolina 27606, U.S.A.
Antisera to a peptide representing the extreme carboxy terminus of the hepatitis delta virus antigen (HDAg) open reading frame (residues 197 to 211) recognized only the large (p27
) and not the small (p24
) form of HDAg in immunoblots of infected liver extracts, thereby providing direct proof that p27
and p24
differ in their carboxyl-terminal sequence and that p27
results from mutation within the stop codon terminating translation of p24
. Reactions with other peptide antisera demonstrated that multiple smaller virus-specified proteins were carboxy-terminally truncated forms of HDAg, and immunoprecipitation studies suggested that different forms of HDAg were present as heterologous complexes within the liver extract.
Received 15 July 1991;
accepted 17 September 1991.
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