Structural organisation of the head-to-tail interface of a bacterial virus
Identifieur interne : 003510 ( Main/Exploration ); précédent : 003509; suivant : 003511Structural organisation of the head-to-tail interface of a bacterial virus
Auteurs : Rudi Lurz [Allemagne] ; Elena V. Orlova [Allemagne] ; Dirk Günther [Allemagne] ; Prakash Dube [Royaume-Uni] ; Anja Dröge [Allemagne] ; Frank Weise [Allemagne] ; Marin Van Heel [Royaume-Uni] ; Paulo Tavares [France, Allemagne]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 2001.
English descriptors
- KwdEn :
- Teeft :
- Bacillus subtilis bacteriophage spp1, Bacteriophage, Bacteriophage lambda, Bacteriophage spp1, Bacteriophage spp1 connector, Bacteriophage spp1 connector figure, Bacteriophage spp1 portal protein, Biol, Capsid, Carrascosa, Characteristic views, Class averages, Connector, Connector particles, Connector preparation, Connector proteins, Connector region, Connector structure, Cyclical, Dube, Edta, Eigenimage number, Electron microscope, Electron microscopy, Head completion proteins, Helical, Helical tail, Icosahedral capsid, Image processing, Individual particles, Interface, Lurz, Lysis buffer, Mature virions, Morphogenesis, Organisation, Packaging machinery, Phage, Phage particle, Portal, Portal protein, Portal vertex, Procapsid, Procapsid assembly, Protein, Spp1, Spp1 connector, Spp1 interface, Spp1 particles, Spp1 portal protein, Spp1 virions, Structural organisation, Subunit, Tail structures, Tavares, Unpublished results, Viral, Viral capsid, Virion, Western blot.
Abstract
Abstract: In tailed icosahedral bacteriophages the connection between the 5-fold symmetric environment of the portal vertex in the capsid and the 6-fold symmetric phage tail is formed by a complex interface structure. The current study provides the detailed analysis of the assembly and structural organisation of such an interface within a phage having a long tail. The region of the interface assembled as part of the viral capsid (connector) was purified from DNA-filled capsids of the Bacillus subtilis bacteriophage SPP1. It is composed of oligomers of gp6, the SPP1 portal protein, of gp15, and of gp16. The SPP1 connector structure is formed by a mushroom-like portal protein whose cap faces the interior of the viral capsid in intact virions, an annular structure below the stem of the mushroom, and a second narrower annulus that is in direct contact with the helical tail extremity. The layered arrangement correlates to the stacking of gp6, gp15, and gp16 on top of the tail. The gp16 ring is exposed to the virion outside. During SPP1 morphogenesis, gp6 participates in the procapsid assembly reaction, an early step in the assembly pathway, while gp15 and gp16 bind to the capsid portal vertex after viral chromosome encapsidation. gp16 is processed during or after tail attachment to the connector region. The portal protein gp6 has 12-fold cyclical symmetry in the connector structure, whereas assembly-naı̈ve gp6 exhibits 13-fold symmetry. We propose that it is the interaction of gp6 with other viral morphogenetic proteins that drives its assembly into the 12-mer state.
Url:
DOI: 10.1006/jmbi.2001.4800
Affiliations:
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<front><div type="abstract" xml:lang="en">Abstract: In tailed icosahedral bacteriophages the connection between the 5-fold symmetric environment of the portal vertex in the capsid and the 6-fold symmetric phage tail is formed by a complex interface structure. The current study provides the detailed analysis of the assembly and structural organisation of such an interface within a phage having a long tail. The region of the interface assembled as part of the viral capsid (connector) was purified from DNA-filled capsids of the Bacillus subtilis bacteriophage SPP1. It is composed of oligomers of gp6, the SPP1 portal protein, of gp15, and of gp16. The SPP1 connector structure is formed by a mushroom-like portal protein whose cap faces the interior of the viral capsid in intact virions, an annular structure below the stem of the mushroom, and a second narrower annulus that is in direct contact with the helical tail extremity. The layered arrangement correlates to the stacking of gp6, gp15, and gp16 on top of the tail. The gp16 ring is exposed to the virion outside. During SPP1 morphogenesis, gp6 participates in the procapsid assembly reaction, an early step in the assembly pathway, while gp15 and gp16 bind to the capsid portal vertex after viral chromosome encapsidation. gp16 is processed during or after tail attachment to the connector region. The portal protein gp6 has 12-fold cyclical symmetry in the connector structure, whereas assembly-naı̈ve gp6 exhibits 13-fold symmetry. We propose that it is the interaction of gp6 with other viral morphogenetic proteins that drives its assembly into the 12-mer state.</div>
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