Conformational changes of the baseplate regulating tail contraction of Staphylococcus phage 812
4 affiliations
- 1Central European Institute of Technology, Brno, Czech Republic
- 2National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Brno, Czech Republic
- 3Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, Czech Republic
- 4Central European Institute of Technology, Brno, Czech Republic. [email protected]
Abstract
Phages with contractile tails employ elaborate mechanisms to penetrate bacterial cell walls and deliver their genomes into the host cytoplasm. Here, we used cryo-EM to show that the baseplate of phage 812, a member of the Kayvirus genus, which infects Gram-positive Staphylococcus strains, is formed of a core, wedge modules, and baseplate arms carrying receptor-binding proteins 1 and 2 and tripod complexes. Upon binding to a host cell, the receptor-binding proteins of phage 812 baseplate reorient and undergo conformational changes. The changes to the tripod complexes trigger the release of the central spike and weld proteins, which expose peptidoglycan-degrading domains of the hub proteins. Changes in the positions of baseplate arms are transmitted through wedge modules to tail sheath initiator proteins. The ring of the tail sheath initiator proteins expands and triggers the contraction of the tail sheath, which shortens to 50% and pushes the tail tube 10-30 nm into the bacterial cytoplasm. Homologous molecular mechanisms are probably shared by phages of the Herelleviridae family with contractile tails to infect Gram-positive bacteria.
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BibTeX
@article{binovsky2026conformational,
title = {{Conformational changes of the baseplate regulating tail contraction of Staphylococcus phage 812}},
author = {Ján Bíňovský and Marta Šiborová and Maryna Zlatohurska and Jiří Nováček and Pavol Bárdy and Roman Baška and Karel Škubník and Tibor Botka and Martin Benešík and Roman Pantůček and Konstantinos Tripsianes and Pavel Plevka},
journal = {The EMBO Journal},
year = {2026},
month = jun,
doi = {10.1038/s44318-026-00834-9},
url = {https://doi.org/10.1038/s44318-026-00834-9},
note = {CC BY},
}
RIS
TY - JOUR
TI - Conformational changes of the baseplate regulating tail contraction of Staphylococcus phage 812
AU - Ján Bíňovský
AU - Marta Šiborová
AU - Maryna Zlatohurska
AU - Jiří Nováček
AU - Pavol Bárdy
AU - Roman Baška
AU - Karel Škubník
AU - Tibor Botka
AU - Martin Benešík
AU - Roman Pantůček
AU - Konstantinos Tripsianes
AU - Pavel Plevka
PY - 2026
DA - 2026/06/26
JO - The EMBO Journal
DO - 10.1038/s44318-026-00834-9
UR - https://doi.org/10.1038/s44318-026-00834-9
AB - Phages with contractile tails employ elaborate mechanisms to penetrate bacterial cell walls and deliver their genomes into the host cytoplasm. Here, we used cryo-EM to show that the baseplate of phage 812, a member of the Kayvirus genus, which infects Gram-positive Staphylococcus strains, is formed of a core, wedge modules, and baseplate arms carrying receptor-binding proteins 1 and 2 and tripod complexes. Upon binding to a host cell, the receptor-binding proteins of phage 812 baseplate reorient and undergo conformational changes. The changes to the tripod complexes trigger the release of the central spike and weld proteins, which expose peptidoglycan-degrading domains of the hub proteins. Changes in the positions of baseplate arms are transmitted through wedge modules to tail sheath initiator proteins. The ring of the tail sheath initiator proteins expands and triggers the contraction of the tail sheath, which shortens to 50% and pushes the tail tube 10-30 nm into the bacterial cytoplasm. Homologous molecular mechanisms are probably shared by phages of the Herelleviridae family with contractile tails to infect Gram-positive bacteria.
SN - 0261-4189
SN - 1460-2075
ER -