RT Journal Article
T1 Interaction of preS domains of Hepatitis B Virus with phospholipid vesicles
A1 Núñez, Elena
A1 Yélamos, Belén
A1 Delgado, Carmen
A1 Gómez-Gutiérrez, Julián
A1 Peterson, Darrell L.
A1 Gavilanes, Francisco
AB The role of preS domains of the hepatitis B virus (HBV) envelope proteins in the first steps of viral infection has been restricted to their implication in virus attachment to a putative hepatocyte receptor. In order to explore a fusion activity in these regions, we used recombinant preS domains to characterize their interaction with liposomes. Binding experiments carried out with NBD-labeled proteins indicated that preS were able to interact in a monomeric way with acidic phospholipid vesicles, being the partition coefficient similar to that described for peptides which can insert deeply into bilayers. Fluorescence depolarization of DPH-labeled vesicles confirmed the specificity for negative charged phospholipids. Upon interaction the proteins induced aggregation, lipid mixing and release of internal contents of acidic vesicles at both acid and neutral pH in a concentration-dependent manner. Taken together, all these data indicate that preS domains are able to insert into the hydrophobic core of the bilayer. Moreover, the insertion resulted in a protein conformational change which increased the helical content. Therefore all these results suggest that, besides their participation in the recognition of a cellular receptor, the preS domains could be involved in the fusion mechanism of HBV with the plasma membrane of target cells.
PB Elsevier Science BV
SN 0005-2736
YR 2009
FD 2009-02
LK https://hdl.handle.net/20.500.14352/44767
UL https://hdl.handle.net/20.500.14352/44767
LA eng
NO Dirección General de Investigación of the Ministerio de Educación y Ciencia (Spain)
DS Docta Complutense
RD 1 may 2024