Amy M. Prichard
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Amy M. Prichard has a total of 14 co-authors. Here are the top co-authors by number of shared publications:
- Amar Deep
Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, California, USA
1 shared publication - Christian Seitz
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, United States
1 shared publication - Elizabeth Villa
Department of Molecular Biology, University of California San Diego, La Jolla CA 92093
1 shared publication - Emily G. Armbruster
School of Biological Sciences, University of California San Diego
1 shared publication - Eray Enustun
School of Biological Sciences, University of California San Diego
1 shared publication - Erica A. Birkholz
Department of Molecular Biology, University of California, San Diego, La Jolla, CA
1 shared publication
Latest Publications
- Open Access
Architecture and self-assembly of the jumbo bacteriophage nuclear shell
Bacteria encode myriad defenses that target the genomes of infecting bacteriophage, including restriction-modification and CRISPR/Cas systems. In response, one family of large bacteriophage employs a nucleus-like compartment to protect their replicating genomes by excluding host defense factors. However, the principle composition and structure of this compartment remain unknown. Here, we find that the bacteriophage nuclear shell assembles primarily from one protein, termed chimallin. Combining cryo-electron tomography of nuclear shells in bacteriophage-infected cells and cryo-electron microscopy of a minimal chimallin compartment in vitro, we show that chimallin cooperatively self-assembles as a flexible sheet into closed micron-scale compartments. The architecture and assembly dynamics of the chimallin shell suggest mechanisms for its nucleation and growth, and its role as a scaffold for phage-encoded factors mediating macromolecular transport, cytoskeletal interactions, and viral maturation.
Open AccessArchitecture and self-assembly of the jumbo bacteriophage nuclear shell
Bacteria encode myriad defenses that target the genomes of infecting bacteriophage, including restriction-modification and CRISPR/Cas systems. In response, one family of large bacteriophage employs a nucleus-like compartment to protect their replicating genomes by excluding host defense factors. However, the principle composition and structure of this compartment remain unknown. Here, we find that the bacteriophage nuclear shell assembles primarily from one protein, termed chimallin. Combining cryo-electron tomography of nuclear shells in bacteriophage-infected cells and cryo-electron microscopy of a minimal chimallin compartment in vitro, we show that chimallin cooperatively self-assembles as a flexible sheet into closed micron-scale compartments. The architecture and assembly dynamics of the chimallin shell suggest mechanisms for its nucleation and growth, and its role as a scaffold for phage-encoded factors mediating macromolecular transport, cytoskeletal interactions, and viral maturation.