Requirement of Heat Shock Protein 90 for Human Hepatitis B Virus Reverse Transcriptase Function

• DOI: 10.1128/jvi.78.23.13122-13131.2004
• Publication Date: 2004-11-12T20:29:30Z
• Authors: Jianming Hu; Dafna Flores; David Toft; Xingtai Wang; David Nguyen
• Keywords: Chaperone (clinical)

The initiation of reverse transcription and nucleocapsid assembly in hepatitis B virus (HBV) depends on the specific recognition an RNA signal (the packaging signal, epsilon) pregenomic (pgRNA) by viral transcriptase (RT). RT-epsilon interaction duck (DHBV) was recently shown to require molecular chaperone complex, heat shock protein 90 (Hsp90). However, requirement for human HBV has remained unknown due inability obtain a purified RT active epsilon binding. We now report that Hsp90 is also required interaction. Inhibition led diminished pgRNA into nucleocapsids cells, which Furthermore, using truncated proteins from bacteria five factors, we have developed vitro binding assay. Our results demonstrate Hsp90, dynamic process dependent ATP hydrolysis, facilitated HBV, as DHBV. Specific sequences both amino-terminal terminal carboxy-terminal domain. Only cognate epsilon, but not DHBV could bind proteins. internal bulge, apical loop, establishment defined reconstitution system paved way future biochemical structural studies elucidate mechanisms activation.