Rice dwarf virus (RDV) is a double-shelled icosahedral virus.Using electron cryomicroscopy and computer reconstruction techniques, we have determined a 3.3 nm resolution three-dimensional (3D) structure of the inner s...Rice dwarf virus (RDV) is a double-shelled icosahedral virus.Using electron cryomicroscopy and computer reconstruction techniques, we have determined a 3.3 nm resolution three-dimensional (3D) structure of the inner shell capsid without the outer shell and viral RNA. The results show that the inner shell is a thin, densely packed, smooth structure, which provides a scaffold for the full virus. A total of 120 copies of the major inner shell capsid protein P3 forms 60 dimers arranged in a T=1 icosahedral lattice. A close examination on the subunit packing of the T=1 inner core P3 with that of the T=13l outer shell P8 indicated that P8 trimers connect with P3 through completely non-equivalent, yet highly specific, intermolecular interactions.展开更多
The three-dimensional(3D)structure of intact rice dwarf virus(RDV)has been deter-mined to 2.6 nm resolution by 400kV electron cryomicroscopy and computer reconstructiontechniques.The intact virion of 69.8 nm in diamet...The three-dimensional(3D)structure of intact rice dwarf virus(RDV)has been deter-mined to 2.6 nm resolution by 400kV electron cryomicroscopy and computer reconstructiontechniques.The intact virion of 69.8 nm in diameter was seen to be made up of an outer shellof 6.9 nm in thickness and an inner shell of 2.5 nm in thickness at a diameter of 54 nm.Theouter shell surface forms a T=13 icosahedral lattice with holes at 5-and 6-coordinated posi-tions.The 780 capsomeres at local 3-fold positions appear trimeric.The interface betweenthese two shells could be clearly delineated and the interaction was maintained by a cylindri-cal density whose upper domain connects subunits of the trimeric capsomeres by an interlock-ing mechanism.The 3D structure of inner shell was also reconstructed to 3.3 nm from100kV images of purified inner shell particles,confirming our interpretation of the multilayerstructure of intact RDV.展开更多
基金theNational Natural Science Foundation of China (Grant No. 39870181), NIH (USA, AI 46420 to ZHZ) and the Welch Foundation (AU-1492 to ZHZ).
文摘Rice dwarf virus (RDV) is a double-shelled icosahedral virus.Using electron cryomicroscopy and computer reconstruction techniques, we have determined a 3.3 nm resolution three-dimensional (3D) structure of the inner shell capsid without the outer shell and viral RNA. The results show that the inner shell is a thin, densely packed, smooth structure, which provides a scaffold for the full virus. A total of 120 copies of the major inner shell capsid protein P3 forms 60 dimers arranged in a T=1 icosahedral lattice. A close examination on the subunit packing of the T=1 inner core P3 with that of the T=13l outer shell P8 indicated that P8 trimers connect with P3 through completely non-equivalent, yet highly specific, intermolecular interactions.
文摘The three-dimensional(3D)structure of intact rice dwarf virus(RDV)has been deter-mined to 2.6 nm resolution by 400kV electron cryomicroscopy and computer reconstructiontechniques.The intact virion of 69.8 nm in diameter was seen to be made up of an outer shellof 6.9 nm in thickness and an inner shell of 2.5 nm in thickness at a diameter of 54 nm.Theouter shell surface forms a T=13 icosahedral lattice with holes at 5-and 6-coordinated posi-tions.The 780 capsomeres at local 3-fold positions appear trimeric.The interface betweenthese two shells could be clearly delineated and the interaction was maintained by a cylindri-cal density whose upper domain connects subunits of the trimeric capsomeres by an interlock-ing mechanism.The 3D structure of inner shell was also reconstructed to 3.3 nm from100kV images of purified inner shell particles,confirming our interpretation of the multilayerstructure of intact RDV.
