Retrovirus capsid protein assembly arrangements
| Autor: | Douglas L. Huseby, Jason E. McDermott, Brian Arvidson, Keith Mayo, Eric Barklis, Liam Finlay |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular viruses Dimer Protein subunit Molecular Sequence Data Static Electricity Crystallography X-Ray chemistry.chemical_compound Retrovirus Imaging Three-Dimensional Structural Biology Murine leukemia virus Amino Acid Sequence Protein Structure Quaternary Molecular Biology biology Virus Assembly Group-specific antigen biology.organism_classification Molecular biology In vitro Cell biology Microscopy Electron Protein Subunits Retroviridae chemistry Capsid HIV-1 Capsid Proteins Moloney murine leukemia virus Linker Dimerization Protein Binding |
| Zdroj: | Journal of molecular biology. 325(1) |
| ISSN: | 0022-2836 |
| Popis: | During retrovirus particle assembly and morphogenesis, the retrovirus structural (Gag) proteins organize into two different arrangements: an immature form assembled by precursor Gag (PrGag) proteins; and a mature form, composed of proteins processed from PrGag. Central to both Gag protein arrangements is the capsid (CA) protein, a domain of PrGag, which is cleaved from the precursor to yield a mature Gag protein composed of an N-terminal domain (NTD), a flexible linker region, and a C-terminal domain (CTD). Because Gag interactions have proven difficult to examine in virions, a number of investigations have focused on the analysis of structures assembled in vitro. We have used electron microscope (EM) image reconstruction techniques to examine assembly products formed by two different CA variants of both human immunodeficiency virus type 1 (HIV-1) and the Moloney murine leukemia virus (M-MuLV). Interestingly, two types of hexameric protein arrangements were observed for each virus type. One organizational scheme featured hexamers composed of putative NTD dimer subunits, with sharing of subunits between neighbor hexamers. The second arrangement used apparent NTD monomers to coordinate hexamers, involved no subunit sharing, and employed putative CTD interactions to connect hexamers. Conversion between the two assembly forms may be achieved by making or breaking the proposed symmetric NTD dimer contacts in a process that appears to mimic viral morphogenesis. |
| Databáze: | OpenAIRE |
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