Journal of General Virology, Vol 79, 1115-1119, Copyright © 1998 by Society for General Microbiology

ARTICLES

Interaction between hepatitis delta virus-encoded proteins and hepatitis B virus envelope protein domains

C Hourioux, C Sureau, F Poisson, D Brand, A Goudeau and P Roingeard
Laboratoire de Virologie EP CNRS 117, Faculte de Medecine, Tours, France.

Hepatitis delta virus (HDV) packaging requires prenylation of the HDV large protein (p27), as well as a direct protein-protein interaction between HDV proteins and hepatitis B virus (HBV) envelope protein domains. To investigate this interaction, we have analysed the binding capacity of baculovirus-expressed delta p24 and p27 proteins to synthetic peptides specific for the HBV envelope. Although a higher degree of binding was observed with p27, both p24 and p27 could bind HBV envelope peptides. One such peptide corresponded to residues 56-80 located in the cytosolic loop of the small HBV envelope protein, and another corresponded to 23 carboxy-terminal residues of the pre-S1 specific to the large HBV envelope protein. This indicates that in addition to p27, p24 may contribute to packaging of HDV through a protein-protein interaction with HBV envelope domains, and that an interaction between the pre-S1 polypeptide and delta proteins may play a role in infectivity.

This article has been cited by other articles:

				B. B. Bordier, P. L. Marion, K. Ohashi, M. A. Kay, H. B. Greenberg, J. L. Casey, and J. S. Glenn A Prenylation Inhibitor Prevents Production of Infectious Hepatitis Delta Virus Particles J. Virol., September 11, 2002; 76(20): 10465 - 10472. [Abstract] [Full Text] [PDF]

				C. Hourioux, A. Touzé, P. Coursaget, and P. Roingeard DNA-containing and empty hepatitis B virus core particles bind similarly to envelope protein domains J. Gen. Virol., April 1, 2000; 81(4): 1099 - 1101. [Abstract] [Full Text]