6r3b Citations

Structural transitions during the scaffolding-driven assembly of a viral capsid.

OpenAccess logo Nat Commun 10 4840 (2019)
Related entries: 6r3a, 6rtl

Cited: 13 times
EuropePMC logo PMID: 31649265

Abstract

Assembly of tailed bacteriophages and herpesviruses starts with formation of procapsids (virion precursors without DNA). Scaffolding proteins (SP) drive assembly by chaperoning the major capsid protein (MCP) to build an icosahedral lattice. Here we report near-atomic resolution cryo-EM structures of the bacteriophage SPP1 procapsid, the intermediate expanded procapsid with partially released SPs, and the mature capsid with DNA. In the intermediate state, SPs are bound only to MCP pentons and to adjacent subunits from hexons. SP departure results in the expanded state associated with unfolding of the MCP N-terminus and straightening of E-loops. The newly formed extensive inter-capsomere bonding appears to compensate for release of SPs that clasp MCP capsomeres together. Subsequent DNA packaging instigates bending of MCP A domain loops outwards, closing the hexons central opening and creating the capsid auxiliary protein binding interface. These findings provide a molecular basis for the sequential structural rearrangements during viral capsid maturation.

Reviews citing this publication (4)

  1. Cryo-electron microscopy for the study of virus assembly. Luque D, Castón JR. Nat Chem Biol 16 231-239 (2020)
  2. In Vitro Assembly of Virus-Like Particles and Their Applications. Le DT, Müller KM. Life (Basel) 11 334 (2021)
  3. Major tail proteins of bacteriophages of the order Caudovirales. Zinke M, Schröder GF, Lange A. J Biol Chem 298 101472 (2022)
  4. Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins. Dedeo CL, Teschke CM, Alexandrescu AT. Viruses 12 E1163 (2020)

Articles citing this publication (9)