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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Zhou, S. Standring, D. N. |
| Description | Author Affiliation: Zhou S ( Hormone Research Institute, University of California, San Francisco 94143-0534.); |
| Abstract | Our studies on the assembly of hepatitis B virus capsids or core particles in Xenopus oocytes have demonstrated that unassembled p21.5 core proteins ('free p21.5') provide a pool of low-molecular-mass precursors for core-particle assembly. Here we have characterized this material. Free p21.5 sedimented through gradients of 3-25% sucrose (wt/vol) as a single protein species of approximately 40 kDa, corresponding to a p21.5 dimer. On nonreducing SDS/polyacrylamide gels, free p21.5 migrated as disulfide-linked p21.5 dimeric species of 35 and 37 kDa. Truncated core proteins lacking most or all of the 36-amino acid protamine region at the p21.5 carboxyl terminus were also found to behave as disulfide-linked dimers with appropriately reduced molecular masses. Our experiments failed to reveal monomeric core proteins or stable intermediates between dimers and capsids along the assembly pathway. We conclude that hepatitis B virus core particles are most likely assembled by aggregating 90 (or possibly 180) disulfide-linked p21.5 dimers. We discuss similarities between the assembly of hepatitis B virus capsids and simple T = 3 plant virus and bacteriophage structures. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 21 |
| Volume Number | 89 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1992-12-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Capsid Biosynthesis Hepatitis B Virus Metabolism Protein Precursors Viral Core Proteins Animals Isolation & Purification Centrifugation, Density Gradient Cysteine Electrophoresis, Polyacrylamide Gel Macromolecular Substances Molecular Weight Oocytes Plasmids RNA, Messenger Recombinant Proteins Sulfur Radioisotopes Xenopus Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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