ArticleNature communications2019
Structural transitions during the scaffolding-driven assembly of a viral capsid.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Small viruses reveal bidirectional evolution between HK97-fold viruses and encapsulins via procapsids.Nature communications · 2026Article
- Subcellular reorganization upon phage infection reveals stepwise assembly of viral particles from membrane-associated precursors.Nature communications · 2026Article
- Elucidating double stranded DNA viral scaffolding protein structures through advances in cryogenic electron microscopy data processing.Current opinion in structural biology · 2025Review
- Structure of the scaffolding protein and portal within the bacteriophage P22 procapsid provides insights into the self-assembly process.PLoS biology · 2025Article
- Phi29 assembly intermediates reveal how scaffold interactions with capsid protein drive capsid construction and maturation.Science advances · 2025Article
- Characterization of the novel cross-genus phage vB_SmaS_QH3 and evaluation of its antibacterial efficacy againstFrontiers in microbiology · 2025Article
- Capsid structure of bacteriophage ΦKZ provides insights into assembly and stabilization of jumbo phages.Nature communications · 2024Article
- Partial Atomic Model of the Tailed Lactococcal Phage TP901-1 as Predicted by AlphaFold2: Revelations and Limitations.Viruses · 2023Article
- A symmetry mismatch unraveled: How phage HK97 scaffold flexibly accommodates a 12-fold pore at a 5-fold viral capsid vertex.Science advances · 2023Article
- Assembly and Capsid Expansion Mechanism of Bacteriophage P22 Revealed by High-Resolution Cryo-EM Structures.Viruses · 2023Article
- Structures of a large prolate virus capsid in unexpanded and expanded states generate insights into the icosahedral virus assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cryo-EM Structure of a Kinetically Trapped Dodecameric Portal Protein from the Pseudomonas-phage PaP3.Journal of molecular biology · 2022Article
- Capsid Structure ofJournal of virology · 2021Article
- High Resolution Structure of the Mature Capsid ofInternational journal of molecular sciences · 2021Article
- Temporal compartmentalization of viral infection in bacterial cells.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- In Vitro Assembly of Virus-Like Particles and Their Applications.Life (Basel, Switzerland) · 2021Review
- Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins.Viruses · 2020Review
- The Mottled Capsid of theViruses · 2020Article
- Cryo-electron microscopy for the study of virus assembly.Nature chemical biology · 2020Review
Corrections and comments
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Authors and funding
8 authors.
Funding
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.
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