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Updated: Jun 12, 2026

Phage Phenomics: Physiological Approaches to Characterize Novel Viral Proteins
Published on: June 11, 2015
Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus
Xiangan Liu1, Qinfen Zhang, Kazuyoshi Murata
1National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry & Molecular Biology, Baylor College of Medicine, Houston, Texas, USA.
Abstract:
Podovirus P-SSP7 infects Prochlorococcus marinus, the most abundant oceanic photosynthetic microorganism. Single-particle cryo-electron microscopy yields icosahedral and asymmetrical structures of infectious P-SSP7 with 4.6-A and 9-A resolution, respectively. The asymmetric reconstruction reveals how symmetry mismatches are accommodated among five of the gene products at the portal vertex. Reconstructions of infectious and empty particles show a conformational change of the 'valve' density in the nozzle, an orientation difference in the tail fibers, a disordering of the C terminus of the portal protein and the disappearance of the core proteins. In addition, cryo-electron tomography of P-SSP7 infecting Prochlorococcus showed the same tail-fiber conformation as that in empty particles. Our observations suggest a mechanism whereby, upon binding to the host cell, the tail fibers induce a cascade of structural alterations of the portal vertex complex that triggers DNA release.
Insights
Podovirus P-SSP7 infects abundant marine cyanobacteria. Cryo-EM reveals structural changes in the virus upon host cell binding, triggering DNA release and infection.
Area of Science:
- Microbiology
- Structural Biology
- Oceanography
Background:
- Prochlorococcus marinus is the most abundant photosynthetic microorganism in oceans.
- Podovirus P-SSP7 is a virus that infects Prochlorococcus marinus.
Purpose of the Study:
- To determine the structure of Podovirus P-SSP7 using cryo-electron microscopy.
- To elucidate the mechanism of P-SSP7 infection and DNA release in Prochlorococcus.
Main Methods:
- Single-particle cryo-electron microscopy (cryo-EM) was used to obtain high-resolution structures.
- Cryo-electron tomography (cryo-ET) was employed to study virus-host interactions.
Main Results:
- Icosahedral and asymmetrical structures of infectious P-SSP7 were resolved at 4.6-Å and 9-Å resolution.
- Structural changes were observed in infectious vs. empty particles, including alterations in the portal vertex, nozzle, tail fibers, and core proteins.
- Cryo-ET showed tail fiber conformation in infected cells matched empty particles, suggesting a role in triggering DNA release.
Conclusions:
- The study proposes a mechanism for P-SSP7 DNA release involving tail fiber-induced structural changes upon host cell binding.
- These alterations cascade through the portal vertex complex, leading to genome ejection.
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