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| Title | Capsid structure of phage SPO1 reveals novel minor capsid proteins and insights into capsid stabilization. |
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| Journal, issue, pages | Structure, Vol. 33, Issue 11, Page 1844-11855.e2, Year 2025 |
| Publish date | Nov 6, 2025 |
Authors | Xinyue Zhao / Aohan Wang / Yueting Wang / Yue Kang / Qianqian Shao / Lin Li / Yaqi Zheng / Hongli Hu / Xiangyun Li / Hongling Fan / Can Cai / Bing Liu / Qianglin Fang / ![]() |
| PubMed Abstract | SPO1-related bacteriophages are promising candidates for phage therapy. We present the 3.0 Å cryo-electron microscopy (cryo-EM) structure of the SPO1 capsid with a triangulation number T = 16, ...SPO1-related bacteriophages are promising candidates for phage therapy. We present the 3.0 Å cryo-electron microscopy (cryo-EM) structure of the SPO1 capsid with a triangulation number T = 16, enabling the construction of an atomic model comprising the major capsid protein and three types of minor capsid proteins: gp29.2, gp2.7, and gp36.3. These minor capsid proteins adopt novel folds. They might stabilize the capsid and determine its curvature. Gp29.2 monomers contain a three-blade propeller fold and are located at the 3-fold and quasi-three-fold axes. Gp2.7 forms pentamers atop pentameric capsomers, while gp36.3 binds to the capsid's inner surface, forming star-shaped structures increasing connections between pentameric and hexameric capsomers. The surface exposed regions of gp29.2 and gp2.7 make SPO1 of interest as a nanocage for phage display. Our findings advance the understanding of capsid architecture, stabilization, and local curvature determination for SPO1-related bacteriophages. |
External links | Structure / PubMed:40885197 |
| Methods | EM (single particle) |
| Resolution | 3.0 - 5.5 Å |
| Structure data | EMDB-65011, PDB-9vel: ![]() EMDB-65012: A block of bacteriophage SPO1 capsid ![]() EMDB-65738: The consensus cryo-EM structure of bacteriophage SPO1 capsid |
| Source |
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Keywords | VIRUS / SPO1 / Phage / Capsid |
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bacillus phage spo1 (virus)
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