Choi, KJ Lim, CW Yoon, MY Ahn, BY Yu, YG 2024-01-21T06:41:29Z 2024-01-21T06:41:29Z 2021-09-05 2004-07-02 0006-291X https://pubs.kist.re.kr/handle/201004/137420 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 +/- 0.4 muM 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. (C) 2004 Elsevier Inc. All rights reserved. English ACADEMIC PRESS INC ELSEVIER SCIENCE PRE-S DOMAIN TRANSMEMBRANE TOPOLOGY PARTICLES ANTIGEN INFECTION PEPTIDES SEQUENCE GP41 Quantitative analysis of the interaction between the envelope protein domains and the core protein of human hepatitis B virus Article 10.1016/j.bbrc.2004.05.083 1 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.319, no.3, pp.959 - 966 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 319 3 959 966 scie scopus 000222195400036 2-s2.0-2942620427 Biochemistry & Molecular Biology Biophysics Biochemistry & Molecular Biology Biophysics Article PRE-S DOMAIN TRANSMEMBRANE TOPOLOGY PARTICLES ANTIGEN INFECTION PEPTIDES SEQUENCE GP41 hepatitis B virus surface protein pre-S domains core protein interaction