Joshua B. Maurer
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Joshua B. Maurer has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- James F. Conway
Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA
2 shared publications - Robert L. Duda
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States
2 shared publications - Alexis G. E. Huet
Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, USA
1 shared publication - Alexis Huet
Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA
1 shared publication Anna K. Belford
Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, USA
1 shared publication- Anna K. Belford
Laboratory of Cellular Oncology, National Cancer Institute, 37 Convent Dr., Bethesda, MD 20894, USA
1 shared publication
Latest Publications
- Open Access
- 23 November 2025
- Published by Springer Nature in Nature Communications
- Vol. 16 (1)
Structural insights into scaffold-guided assembly of the Pseudomonas phage D3 capsid
Tailed bacteriophages comprise the largest structural family of viruses with close relatives in archaea and the eukaryotic herpesviruses. The common assembly pathway produces an icosahedrally symmetric protein shell, called capsid, into which the double-stranded DNA genome is packaged. While capsid sizes and amino acid sequences vary considerably, the major capsid protein (MCP) folds are remarkably similar throughout the family. To investigate the mechanisms governing capsid size, we characterize the procapsid and mature capsid of phage D3, which expresses an icosahedral lattice with Triangulation number T = 9. We find that the MCP scaffold domain binds to the interior capsid surface, acting as a clamp to constrain subunit interactions. Following scaffold digestion, the MCP capsid domains form strong interactions that maintain capsid structure throughout maturation. The scaffold constraints appear critical for capsid size determination and provide important understanding of the factors governing capsid assembly in general and expands our understanding of these ecologically and biomedically important viruses.
- 23 November 2025
- Published by Springer Nature in Nature Communications
- Vol. 16 (1)
Open AccessStructural insights into scaffold-guided assembly of the Pseudomonas phage D3 capsid
Tailed bacteriophages comprise the largest structural family of viruses with close relatives in archaea and the eukaryotic herpesviruses. The common assembly pathway produces an icosahedrally symmetric protein shell, called capsid, into which the double-stranded DNA genome is packaged. While capsid sizes and amino acid sequences vary considerably, the major capsid protein (MCP) folds are remarkably similar throughout the family. To investigate the mechanisms governing capsid size, we characterize the procapsid and mature capsid of phage D3, which expresses an icosahedral lattice with Triangulation number T = 9. We find that the MCP scaffold domain binds to the interior capsid surface, acting as a clamp to constrain subunit interactions. Following scaffold digestion, the MCP capsid domains form strong interactions that maintain capsid structure throughout maturation. The scaffold constraints appear critical for capsid size determination and provide important understanding of the factors governing capsid assembly in general and expands our understanding of these ecologically and biomedically important viruses.
- Open Access
Structural insights into scaffold-guided assembly of the Pseudomonas phage D3 capsid
Tailed bacteriophages comprise the largest structural family of viruses with close relatives in archaea and the eukaryotic herpesviruses. The common assembly pathway produces an icosahedrally symmetric protein shell, called capsid, into which the double-stranded DNA genome is packaged. While capsid sizes and amino acid sequences vary considerably, the major capsid protein (MCP) folds are remarkably similar throughout the family. To investigate the mechanisms governing capsid size, we characterized the procapsid and mature capsid of phage D3, which expresses an icosahedral lattice with Triangulation number T=9. We found that the MCP scaffold domain binds to the interior capsid surface, acting as a clamp to constrain subunit interactions. Following scaffold digestion, the MCP capsid domains form strong interactions that maintain capsid structure throughout maturation. The scaffold constraints appear critical for capsid size determination and provide important understanding of the factors governing capsid assembly in general and expands our understanding of these ecologically and biomedically important viruses.
Open AccessStructural insights into scaffold-guided assembly of the Pseudomonas phage D3 capsid
Tailed bacteriophages comprise the largest structural family of viruses with close relatives in archaea and the eukaryotic herpesviruses. The common assembly pathway produces an icosahedrally symmetric protein shell, called capsid, into which the double-stranded DNA genome is packaged. While capsid sizes and amino acid sequences vary considerably, the major capsid protein (MCP) folds are remarkably similar throughout the family. To investigate the mechanisms governing capsid size, we characterized the procapsid and mature capsid of phage D3, which expresses an icosahedral lattice with Triangulation number T=9. We found that the MCP scaffold domain binds to the interior capsid surface, acting as a clamp to constrain subunit interactions. Following scaffold digestion, the MCP capsid domains form strong interactions that maintain capsid structure throughout maturation. The scaffold constraints appear critical for capsid size determination and provide important understanding of the factors governing capsid assembly in general and expands our understanding of these ecologically and biomedically important viruses.