I. Rodriguez-crespo et al., Fusogenic activity of hepadnavirus peptides corresponding to sequences downstream of the putative cleavage site, VIROLOGY, 261(1), 1999, pp. 133-142
Sequence homology between the amino-terminal region of the S protein of hep
atitis B Virus (HBV) and known fusion peptides from retroviruses and paramy
xoviruses led us to propose that this region might be equally involved in t
he initial infective steps of hepadnaviruses. In fact, we showed that a syn
thetic peptide corresponding to the N-terminus region of the S protein of H
BV had membrane-interacting properties and was able to induce liposome fusi
on adopting an extended (beta-sheet) conformation (Rodiguez-Crespo et al.,
1996, 1995). We describe herein studies on the interaction of peptides deri
ved from the N-terminal region of the S protein of duck (DHBV: Met-Ser-Gly-
Thr-Phe-Gly-Gly-Ile-Leu-Ala-Gly-Leu-Ile-Gly-Leu-Leu) and woodchuck hepatiti
s B viruses (WHV: Met-Ser-Pro-Ser-Ser-Leu-Leu-Gly-Leu-Leu-Ala-Gly-Leu-Gln-V
al-Val) with liposomes. These peptides were able to induce to a different e
xtent aggregation, lipid mixing, and leakage of internal aqueous contents f
rom both neutral and negatively charged phospholipid vesicles in a concentr
ation-dependent and pH-independent manner. Fluorescence depolarization of 1
,6-diphenyl-1,3,5-hexatriene-labeled vesicles indicated that both peptides
become inserted into the hydrophobic core of the lipid bilayer. Circular di
chroism studies indicated that the DHBV peptide adopts an extended conforma
tion in the presence of lipids, whereas the WHV peptide displays a high con
tent of a-helical conformation. Therefore, these results extend our previou
s findings obtained for human hepatitis B virus to other members of the hep
adnavirus family and suggest that this region of the S protein is important
in the initial steps of the infective cycle. (C) 1999 Academic Press.