ArticleMolecular microbiology2010
Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 31 citations in OpenAlex.
- Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.Journal of virology · 2026Review
- Phi29 assembly intermediates reveal how scaffold interactions with capsid protein drive capsid construction and maturation.Science advances · 2025Article
- A Hydrophobic Network: Intersubunit and Intercapsomer Interactions Stabilizing the Bacteriophage P22 Capsid.Journal of virology · 2019Article
- The amazing HK97 fold: versatile results of modest differences.Current opinion in virology · 2019Review
- The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.eLife · 2019Article
- Protein cage assembly across multiple length scales.Chemical Society reviews · 2018Review
- Coat Protein Mutations That Alter the Flux of Morphogenetic Intermediates through the ϕX174 Early Assembly Pathway.Journal of virology · 2017Article
- A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly.Science advances · 2017Article
- Acquiring Structural Information on Virus Particles with Charge Detection Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly.Journal of virology · 2015Article
- Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.Virology · 2015Review
- Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling.Structure (London, England : 1993) · 2014Article
- Highly specific salt bridges govern bacteriophage P22 icosahedral capsid assembly: identification of the site in coat protein responsible for interaction with scaffolding protein.Journal of virology · 2014Article
- Architecture of a dsDNA viral capsid in complex with its maturation protease.Structure (London, England : 1993) · 2014Article
- An intramolecular chaperone inserted in bacteriophage P22 coat protein mediates its chaperonin-independent folding.The Journal of biological chemistry · 2013Article
- Three-dimensional structure of victorivirus HvV190S suggests coat proteins in most totiviruses share a conserved core.PLoS pathogens · 2013Article
- Effects of an early conformational switch defect during ϕX174 morphogenesis are belatedly manifested late in the assembly pathway.Journal of virology · 2013Article
- Conformational switch-defective X174 internal scaffolding proteins kinetically trap assembly intermediates before procapsid formation.Journal of virology · 2012Article
- Stepwise molecular display utilizing icosahedral and helical complexes of phage coat and decoration proteins in the development of robust nanoscale display vehicles.Biomaterials · 2012Article
- The energetic contributions of scaffolding and coat proteins to the assembly of bacteriophage procapsids.Virology · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
We have investigated determinants of polyhead formation in bacteriophage P22 in order to understand the molecular mechanism by which coat protein assembly goes astray. Polyhead assembly is caused by amino acid substitutions in coat protein at position 170, which is located in the β-hinge. In vivo scaffolding protein does not correct polyhead assembly by F170A or F170K coat proteins, but does for F170L. All F170 variants bind scaffolding protein more weakly than wild-type as observed by affinity chromatography with scaffolding protein-agarose and scaffolding protein shell re-entry experiments. Electron cryo-microscopy and three-dimensional image reconstructions of F170A and F170K empty procapsid shells showed that there is a decreased flexibility of the coat subunits relative to wild-type. This was confirmed by limited proteolysis and protein sequencing, which showed increased protection of the A-domain. Our data support the conclusion that the decrease in flexibility of the A-domain leads to crowding of the subunits at the centre of the pentons, thereby favouring the hexon configuration during assembly. Thus, correct coat protein interactions with scaffolding protein and maintenance of sufficient coat protein flexibility are crucial for proper P22 assembly. The coat protein β-hinge region is the major determinant for both features.
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