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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Simon, Claudia Herbst, Sabine Glaeser, Robert M. Klose, Thomas Lilie, Hauke Sinz, Andrea Stubbs, Milton T. Han, Bong Gyoon |
| Description | Author Affiliation: Simon C ( From the Institute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes Strasse 03, 06120 Halle, Germany.) |
| Abstract | VP1 is the major coat protein of murine polyomavirus and forms virus-like particles (VLPs) in vitro. VLPs consist of 72 pentameric VP1 subunits held together by a terminal clamp structure that is further stabilized by disulfide bonds and chelation of calcium ions. Yeast-derived VLPs (yVLPs) assemble intracellularly in vivo during recombinant protein production. These in vivo assembled yVLPs differ in several properties from VLPs assembled in vitro from bacterially produced pentamers. We found several intermolecular disulfide linkages in yVLPs involving 5 of the 6 cysteines of VP1 (Cys(115)-Cys(20), Cys(12)-Cys(20), Cys(16)-Cys(16), Cys(12)/ Cys(16)-Cys(115), and Cys(274)-Cys(274)), indicating a highly coordinated disulfide network within the in vivo assembled particles involving the N-terminal region of VP1. Cryoelectron microscopy revealed structured termini not resolved in the published crystal structure of the bacterially expressed VLP that appear to clamp the pentameric subunits together. These structural features are probably the reason for the observed higher stability of in vivo assembled yVLPs compared with in vitro assembled bacterially expressed VLPs as monitored by increased thermal stability, higher resistance to trypsin cleavage, and a higher activation enthalpy of the disassembly reaction. This high stability is decreased following disassembly of yVLPs and subsequent in vitro reassembly, suggesting a role for cellular components in optimal assembly. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 15 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-04-11 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Capsid Proteins Chemistry Disulfides Polyomavirus Amino Acid Sequence Capsid Cross-Linking Reagents Cryoelectron Microscopy Cysteine Hot Temperature Kinetics Kluyveromyces Metabolism Molecular Sequence Data Peptides Ultrastructure Protein Conformation Protein Structure, Tertiary Recombinant Proteins Ribonuclease, Pancreatic Trypsin Ultracentrifugation Virion Virus Assembly Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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