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

    Ignatiou, I. and Brasilès, S. and El Sadek Fadel, M. and Bürger, J. and Mielke, T. and Topf, Maya and Tavares, P. and Orlova, Elena (2019) Structural transitions during the scaffolding-driven assembly of a viral capsid. Nature Communications 10 , p. 4840. ISSN 2041-1723.

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    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 cryo-EM near-atomic 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, creating the capsid auxiliary protein binding interface. These findings uncover a molecular basis for the sequential structural rearrangements during viral capsid maturation. Athanasios , Sandrine , Mehdi , Jörg , Thorsten , Maya , Paulo , Elena V.


    Item Type: Article
    Keyword(s) / Subject(s): viral capsid maturation, intermediate states, tailed phage-herpesvirus lineage, scaffolding protein, cryo electron microscopy, single particle analysis
    School: School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 19 Nov 2019 15:06
    Last Modified: 14 Jun 2021 01:49


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