Nucleocapsid and glycoprotein organization in an enveloped virus
Article Abstract:
A 25 angstrom resolution cryo-electron microscopic and image reconstruction study of Ross River virus helps study the organization of alpha-viruses. Twelve pentamers and 30 hexamers constitute the monomeric subunits that form the nucleocapsid core. The inner nucleocapsid core and outer envelope glycoproteins flank the lipid bilayer membrane. The quasi-threefold axes carry 60 spikes, each of which is bound to three SiN capsid protein (SCP) subunits among the pentamers and hexamers while the spikes on isohedral threefold axes are linked to three SCP units on hexamers.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Assembly of a tailed bacterial virus and its genome release studied in three dimensions
Article Abstract:
A three-dimensional reconstruction of a prolate, tailed phage and its empty prohead precursor was described and examined using cryo-electron microscopy. The head-tail connector was visualized within a Bacillus subtilis dsDNA phage. The connector appeared to fit loosely into a pentameric vertex of the head that may be required to rotate the connector to package DNA. Reconstruction of an emptied phage particle showed that the connector and neck/tail assembly undergo conformational changes upon ejection of DNA.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host
Article Abstract:
Studies done on a 17-angstrom resolution, three-dimensional, cryoEM reconstruction of the contracted T4 tail are reported and the locations and shapes of its component proteins are identified and presented. A comparison with the metastable hexagonal baseplate of the mature virus indicates that the baseplate proteins move as rigid bodies relative to each other during the structural change.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
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