Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	DEV phage exploits the essential LptD outer membrane protein as receptor for adsorption.
Journal, issue, pages	mBio, Vol. 17, Issue 2, Page e0356125, Year 2026
Publish date	Feb 11, 2026
Authors	Jimena Nieto Noblecia / Nathan F Bellis / Cristian A Antichi / Shirin Aminian / Francesca Forti / Federica A Falchi / Davide Sposato / Francesco Imperi / Gino Cingolani / Federica Briani /
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 ... 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. IMPORTANCE: phage DEV uses the O-antigen of lipopolysaccharide as its primary receptor. In this study, we found that LptD, an essential and highly conserved outer membrane protein, serves as the secondary receptor for DEV. This interaction is mediated by a specialized receptor-binding fiber composed of the DEV proteins , , and . We posit that the genes form a functional module, possibly disseminated via horizontal gene transfer among distantly related phages, involved in tail sealing and the regulated unplugging of the tail upon interaction with the bacterial receptor. Given the high conservation of receptor-binding proteins among phages in the DEV genus, we anticipate that other members of this genus may also use LptD as their receptor. Since are actively explored for phage therapy, insights into the interaction between DEV and its receptors could help develop more effective and targeted phage-based treatments.
External links	mBio / PubMed:41568963 / PubMed Central
Methods	EM (single particle)
Resolution	3.6 - 8.5 Å
Structure data	74075 9zdw EMDB-74075, PDB-9zdw: Pseudomonas phage DEV delta-gp53 mutant neck and tail (portal, head-to-tail and tail tube proteins) Method: EM (single particle) / Resolution: 3.6 Å 74091 9ze4 EMDB-74091, PDB-9ze4: Asymmetric Tail Gating Complex of Pseudomonas Phage DEV Method: EM (single particle) / Resolution: 8.5 Å
Source	pseudomonas phage vb_paep_dev (virus)
Keywords	VIRAL PROTEIN / bacteriophage / virus / receptor-binding protein