Cryo-EM structures of an Acinetobacter baumannii podovirus reveal a canonical capsid maturation
Phages that hunting multidrug resistant bacteria represent a promising approach in precision medicine nowadays, including these infecting Acinetobacter baumannii. To data, a large number of A. baumannii phages has been isolated, however, complete structural information remains not adequately released. Previously, we reported a podovirus, AbP20, that infects A. baumannii with potent efficacy in…
Cryo-electron microscopy structures of the Acinetobacter baumannii podovirus AbP20 have unveiled a canonical capsid maturation mechanism. AbP20, which effectively infects the multidrug-resistant bacterium A. baumannii, was previously reported to possess five distinct structural subunits: capsid, portal, nozzle, fiber, and adaptor.
The near-atomic resolution structures of AbP20 and its procapsid revealed a double-layered, concentric spherical architecture with a nearly 1:1 ratio of the scaffold and capsid proteins. The study also found that co-expressing the scaffold and capsid proteins of AbP20 led to the self-assembly of a DNA-free procapsid. Comparing the mature and apo-forms of the capsid unveiled a canonical model of conformational switch from procapsid to capsid.
This research provides the first whole-atom structure of a podovirus infecting A. baumannii, offering a valuable reference for structure-based phage engineering and editing in precision medicine.
Written by urgent.news from bioRxiv's reporting — not their text. Machine-written — may contain errors; check the original before relying on it.
