ArticleMolecular & cellular proteomics : MCP2010
Critical salt bridges guide capsid assembly, stability, and maturation behavior in bacteriophage HK97.
Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Fluorescence, Circular Dichroism and Mass Spectrometry as Tools to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.Structure (London, England : 1993) · 2023Article
- Article
- A Hydrophobic Network: Intersubunit and Intercapsomer Interactions Stabilizing the Bacteriophage P22 Capsid.Journal of virology · 2019Article
- A 3.0-Angstrom Resolution Cryo-Electron Microscopy Structure and Antigenic Sites of Coxsackievirus A6-Like Particles.Journal of virology · 2018Article
- Cryo-EM structure of the bacteriophage T4 isometric head at 3.3-Å resolution and its relevance to the assembly of icosahedral viruses.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Flexible Connectors between Capsomer Subunits that Regulate Capsid Assembly.Journal of molecular biology · 2017Article
- Isotope Labeling of Biomolecules: Structural Analysis of Viruses by HDX-MS.Methods in enzymology · 2016Article
- Raman spectroscopic signatures of echovirus 1 uncoating.Journal of virology · 2014Article
- Article
- Transient contacts on the exterior of the HK97 procapsid that are essential for capsid assembly.Journal of molecular biology · 2014Article
- pH-induced stability switching of the bacteriophage HK97 maturation pathway.Journal of the American Chemical Society · 2014Article
- Architecture of a dsDNA viral capsid in complex with its maturation protease.Structure (London, England : 1993) · 2014Article
- A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 A resolution.eLife · 2013Article
- Confessions of an icosahedral virus crystallographer.Microscopy (Oxford, England) · 2013Review
- Maturation in action: CryoEM study of a viral capsid caught during expansion.Structure (London, England : 1993) · 2012Article
- Structural evolution of the P22-like phages: comparison of Sf6 and P22 procapsid and virion architectures.Virology · 2012Article
- The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm.The EMBO journal · 2012Article
- Exploring the symmetry and mechanism of virus capsid maturation via an ensemble of pathways.Biophysical journal · 2012Article
- Virus maturation.Annual review of biophysics · 2012Review
Corrections and comments
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5 authors.
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Abstract
HK97 is a double-stranded DNA bacteriophage that undergoes dramatic conformational changes during viral capsid maturation and for which x-ray structures, at near atomic resolution, of multiple intermediate and mature capsid states are available. Both amide H/(2)H exchange and crystallographic comparisons between the pre-expanded Prohead II particles and the expanded Head II of bacteriophage HK97 revealed quaternary interactions that remain fixed throughout maturation and appear to maintain intercapsomer integrity at all quasi- and icosahedral 3-fold axes. These 3-fold staples are formed from Arg and Glu residues and a metal binding site. Mutations of either Arg-347 or Arg-194 or a double mutation of E344Q and E363A resulted in purification of the phage in capsomer form (hexamers and pentamers). Mutants that did assemble had both decreased thermal stability and decreased in vitro expansion rates. Amide H/(2)H exchange mass spectrometry showed that in the wild type capsid some subunits had a bent "spine" helix (highly exchanging), whereas others were straight (less exchanging). Similar analysis of the never assembled mutant capsomers showed uniform amide exchange in all of these that was higher than that of the straight spine helices (characterized in more mature intermediates), suggesting that the spine helix is somewhat bent prior to capsid assembly. The result further supports a previously proposed mechanism for capsid expansion in which the delta domains of each subunit induce a high energy intermediate conformation, which now appears to include a bent helix during capsomer assembly.
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