Dynamic adhesion device of phage OE33PA drives Gram-positive host recognition
- 1CNRS
Abstract
Bacteriophages (phages) infecting Gram-positive bacteria must bind to host receptors across thick cell walls to initiate infection, yet the underlying structural mechanisms remain unclear. Here, we report cryo-electron microscopy structures of the Oenococcus oeni siphophage OE33PA, providing the first high-resolution view of a phage infecting this wine-industry bacterium. While the overall virion architecture is conserved, the adhesion device displays distinctive features. Its receptor-binding proteins adopt multiple orientations, revealing an intrinsically dynamic assembly. In situ cryo-electron tomography captures distinct conformations upon host attachment, providing rare structural insight into interactions with Gram-positive hosts. Functional assays further show that a mobile carbohydrate-binding module in the distal tail protein mediates host cell binding. Additionnally, the tape measure protein adopts a hexameric organization, updating the prevailing trimeric model in siphophages. Together, these findings reveal a dynamic adhesion device in a phage infecting Gram-positive bacteria and highlight the structural and functional diversity of phages.
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BibTeX
@misc{schmitt2026dynamic,
title = {{Dynamic adhesion device of phage OE33PA drives Gram-positive host recognition}},
author = {L. Schmitt and A. Chaib and D. Ptchelkine and E. Kandiah and C. Le Marrec and C. Cambillau and A. Goulet},
howpublished = {bioRxiv},
year = {2026},
month = may,
doi = {10.64898/2026.05.20.726473},
url = {https://www.biorxiv.org/content/10.64898/2026.05.20.726473v3},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Dynamic adhesion device of phage OE33PA drives Gram-positive host recognition
AU - L. Schmitt
AU - A. Chaib
AU - D. Ptchelkine
AU - E. Kandiah
AU - C. Le Marrec
AU - C. Cambillau
AU - A. Goulet
PY - 2026
DA - 2026/05/20
PB - bioRxiv
DO - 10.64898/2026.05.20.726473
UR - https://www.biorxiv.org/content/10.64898/2026.05.20.726473v3
AB - Bacteriophages (phages) infecting Gram-positive bacteria must bind to host receptors across thick cell walls to initiate infection, yet the underlying structural mechanisms remain unclear. Here, we report cryo-electron microscopy structures of the Oenococcus oeni siphophage OE33PA, providing the first high-resolution view of a phage infecting this wine-industry bacterium. While the overall virion architecture is conserved, the adhesion device displays distinctive features. Its receptor-binding proteins adopt multiple orientations, revealing an intrinsically dynamic assembly. In situ cryo-electron tomography captures distinct conformations upon host attachment, providing rare structural insight into interactions with Gram-positive hosts. Functional assays further show that a mobile carbohydrate-binding module in the distal tail protein mediates host cell binding. Additionnally, the tape measure protein adopts a hexameric organization, updating the prevailing trimeric model in siphophages. Together, these findings reveal a dynamic adhesion device in a phage infecting Gram-positive bacteria and highlight the structural and functional diversity of phages.
ER -