Literature DB >> 10814566

Phytoreovirus T = 1 core plays critical roles in organizing the outer capsid of T = 13 quasi-equivalence.

B Wu1, L Hammar, L Xing, S Markarian, J Yan, K Iwasaki, Y Fujiyoshi, T Omura, R H Cheng.   

Abstract

The structures of the double-shelled rice dwarf virus and of its single-shell core have been determined by cryoelectron microscopy and image reconstruction. The core carries a prominent density located at each of the icosahedral faces of its T = 1 lattice. These protrusions are formed by outer shell trimers, tightly inserted at the threefold positions of the core. Such configuration of the core may guide the assembly of the outer shell, aided by lateral interactions between its subunits, into a T = 13 lattice. The organization of the phytoreovirus capsid elucidates for the first time a general model for assembling two unique T numbers of quasi-equivalence. Copyright 2000 Academic Press.

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Year:  2000        PMID: 10814566     DOI: 10.1006/viro.2000.0300

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  3 in total

1.  Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion.

Authors:  M Mathieu; I Petitpas; J Navaza; J Lepault; E Kohli; P Pothier; B V Prasad; J Cohen; F A Rey
Journal:  EMBO J       Date:  2001-04-02       Impact factor: 11.598

2.  Assembly of double-shelled, virus-like particles in transgenic rice plants expressing two major structural proteins of rice dwarf virus.

Authors:  H Zheng; L Yu; C Wei; D Hu; Y Shen; Z Chen; Y Li
Journal:  J Virol       Date:  2000-10       Impact factor: 5.103

Review 3.  Hierarchical structure assembly model of rice dwarf virus particle formation.

Authors:  Atsushi Nakagawa; Naoyuki Miyazaki; Akifumi Higashiura
Journal:  Biophys Rev       Date:  2017-12-14
  3 in total

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