9ZDW

Pseudomonas phage DEV delta-gp53 mutant neck and tail (portal, head-to-tail and tail tube proteins)

This is a non-PDB format compatible entry.

Summary for 9ZDW

• Entry DOI: 10.2210/pdb9zdw/pdb
• EMDB information: 74075
• Descriptor: gp80 portal protein, gp75 tail tube, gp83 head-to-tail (3 entities in total)
• Functional Keywords: bacteriophage, virus, viral protein
• Biological source: Pseudomonas phage vB_PaeP_DEV; More
• Total number of polymer chains: 36
• Total formula weight: 1738507.22

Authors

Bellis, N.F.,Cingolani, G. (deposition date: 2025-11-26, release date: 2026-01-21, Last modification date: 2026-02-25)

Primary citation

Nieto Noblecia, J.,Bellis, N.F.,Antichi, C.A.,Aminian, S.,Forti, F.,Falchi, F.A.,Sposato, D.,Imperi, F.,Cingolani, G.,Briani, F.
Pseudomonas aeruginosa DEV phage exploits the essential LptD outer membrane protein as receptor for adsorption.
Mbio, 17:e0356125-e0356125, 2026

PubMed Abstract: bacteriophage (phage) DEV is a podovirus of the family, related to the prototypical phage N4. N4 uses the novel glycan receptor (NGR) surface glycan, presumably bound by the gp66 appendages, and the NGR transporter NfrA, recognized by the phage gp65 tail sheath, as receptors for adsorption. In contrast, DEV relies on the O-antigen moiety of lipopolysaccharide (LPS) as the primary receptor recognized by the gp53 long tail fibers. However, DEV can infect deep-rough strains that lack the O-antigen moiety by using another, still unknown receptor. Here, we provide evidence that the essential LPS transporter LptD serves as the DEV secondary receptor and that DEV gp54 is its cognate receptor-binding protein. gp54 is encoded within the essential operon, which also includes , the short tail fiber gene. Using cryogenic electron microscopy, AlphaFold modeling, and genetic analysis, we show that DEV gp56, gp55, and gp54 assemble into a receptor-binding fiber (RBF) positioned laterally to a previously uncharacterized tail plug protein, gp74. The DEV RBF is functionally equivalent to the N4 sheath protein gp65, which associates with the tail plug gp53. Thus, DEV and N4 both use a glycan and its surface-exposing transporter as receptors for adsorption. To our knowledge, this is the first example of a phage using an essential outer membrane protein as a receptor, with implications for phage therapy.

PubMed: 41568963
DOI: 10.1128/mbio.03561-25

Experimental method

ELECTRON MICROSCOPY (3.6 Å)