Quantitative analysis of the interaction between the envelope protein domains and the core protein of human hepatitis B virus.

Autor: Choi KJ; Life Sciences Division, Korea Institute of Science and Technology, Hawolgok-dong, Seongbuk-gu, Seoul 136-791, Republic of Korea., Lim CW, Yoon MY, Ahn BY, Yu YG
Jazyk: angličtina
Zdroj: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2004 Jul 02; Vol. 319 (3), pp. 959-66.
DOI: 10.1016/j.bbrc.2004.05.083
Abstrakt: Interaction between preformed nucleocapsids and viral envelope proteins is critical for the assembly of virus particles in infected cells. The pre-S1 and pre-S2 and cytosolic regions of the human hepatitis B virus envelope protein had been implicated in the interaction with the core protein of nucleocapsids. The binding affinities of specific subdomains of the envelope protein to the core protein were quantitatively measured by both ELISA and BIAcore assay. While a marginal binding was detected with the pre-S1 or pre-S2, the core protein showed high affinities to pre-S with apparent dissociation constants (K(D)(app)) of 7.3+/-0.9 and 8.2+/-0.4microM by ELISA and BIAcore assay, respectively. The circular dichroism analysis suggested that conformational change occurs in pre-S through interaction with core protein. These results substantiate the importance of specific envelope domains in virion assembly, and demonstrate that the interaction between viral proteins can be quantitatively measured in vitro.
Databáze: MEDLINE
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