ArticlePhysical biology2010
Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins.
Article in Physical biology, 2010. 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, 31 citations in OpenAlex.
- Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.Journal of virology · 2026Review
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- An intron endonuclease facilitates interference competition between coinfecting viruses.Science (New York, N.Y.) · 2024Article
- The amazing HK97 fold: versatile results of modest differences.Current opinion in virology · 2019Review
- Protein cage assembly across multiple length scales.Chemical Society reviews · 2018Review
- Article
- Acquiring Structural Information on Virus Particles with Charge Detection Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain.The Journal of biological chemistry · 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
- 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
- Location of the bacteriophage P22 coat protein C-terminus provides opportunities for the design of capsid-based materials.Biomacromolecules · 2013Article
- Organization of the influenza virus replication machinery.Science (New York, N.Y.) · 2012Article
- 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
- Structural evolution of the P22-like phages: comparison of Sf6 and P22 procapsid and virion architectures.Virology · 2012Article
- Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays.Nature chemistry · 2012Article
- Principles of virus structural organization.Advances in experimental medicine and biology · 2012Review
- Bacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus.Virology · 2011Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Bacteriophage P22 forms an isometric capsid during normal assembly, yet when the coat protein (CP) is altered at a single site, helical structures (polyheads) also form. The structures of three distinct polyheads obtained from F170L and F170A variants were determined by cryo-reconstruction methods. An understanding of the structures of aberrant assemblies such as polyheads helps to explain how amino acid substitutions affect the CP, and these results can now be put into the context of CP pseudo-atomic models. F170L CP forms two types of polyhead and each has the CP organized as hexons (oligomers of six CPs). These hexons have a skewed structure similar to that in procapsids (precursor capsids formed prior to dsDNA packaging), yet their organization differs completely in polyheads and procapsids. F170A CP forms only one type of polyhead, and though this has hexons organized similarly to hexons in F170L polyheads, the hexons are isometric structures like those found in mature virions. The hexon organization in all three polyheads suggests that nucleation of procapsid assembly occurs via a trimer of CP monomers, and this drives formation of a T = 7, isometric particle. These variants also form procapsids, but they mature quite differently: F170A expands spontaneously at room temperature, whereas F170L requires more energy. The P22 CP structure along with scaffolding protein interactions appear to dictate curvature and geometry in assembled structures and residue 170 significantly influences both assembly and maturation.
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