2017/08/10 by Lye Siang Lee, Nicholas E. Brunk, Daniel G. Haywood +7 · 3 citations
Environmental Science · Medicine · Biochemistry, Genetics and Molecular Biology · Chemistry · #Bacteriophages and microbial interactions #Hepatitis B Virus Studies #RNA and protein synthesis mechanisms #Capsid #Protein subunit #Chemistry #Hepatitis B virus #Biophysics #Virology #Virus #Biology #Biochemistry #Gene
paper · doi:10.1002/pro.3265
openalex publication_date 2017/08/10 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
Hepatitis B virus (HBV) core protein is a model system for studying assembly and disassembly of icosahedral structures. Controlling disassembly will allow re-engineering the 120 subunit HBV capsid, making it a molecular breadboard. We examined removal of subunits from partially crosslinked capsids to form stable incomplete particles. To characterize incomplete capsids, we used two single molecule techniques, resistive-pulse sensing and charge detection mass spectrometry. We expected to find a binomial distribution of capsid fragments. Instead, we found a preponderance of 3 MDa complexes (90 subunits) and no fragments smaller than 3 MDa. We also found 90-mers in the disassembly of uncrosslinked HBV capsids. 90-mers seem to be a common pause point in disassembly reactions. Partly explaining this result, graph theory simulations have showed a threshold for capsid stability between 80 and 90 subunits. To test a molecular breadboard concept, we showed that missing subunits could be refilled resulting in chimeric, 120 subunit particles. This result may be a means of assembling unique capsids with functional decorations.