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J Gen Virol 73 (1992), 183-188; DOI 10.1099/0022-1317-73-1-183
© 1992 Society for General Microbiology

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Immunoblot analysis demonstrates that the large and small forms of hepatitis delta virus antigen have different C-terminal amino acid sequences

Jia-Gang Wang1,2, John Cullen3 and Stanley M. Lemon1

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{delta}) and not the small (p24{delta}) form of HDAg in immunoblots of infected liver extracts, thereby providing direct proof that p27{delta} and p24{delta} differ in their carboxyl-terminal sequence and that p27{delta} results from mutation within the stop codon terminating translation of p24{delta}. 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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