Cryo-EM structures of an Acinetobacter baumannii podovirus reveal a canonical capsid maturation

Near-atomic cryo-EM structures of the Acinetobacter baumannii podovirus AbP20 reveal a canonical procapsid-to-capsid conformational switch and a five-part capsid architecture.

• Why it matters: Structural information for A. baumannii phages is still incomplete, limiting structure-based design despite AbP20’s potent efficacy in a mouse infection model.
• What they did: The authors solved high-resolution cryo-EM structures of AbP20 and its procapsid, co-expressing scaffold and capsid proteins to build a DNA-free self-assembled procapsid.
• The result: The procapsid reconstruction shows a double-layered concentric spherical architecture with an approximately 1:1 ratio of the two proteins, enabling a reference model for structure-based phage engineering.

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