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Deciphering bacteriophage T5 host recognition mechanism and infection trigger
Open accessPreprint — published as 10.1128/jvi.01584-22 · Paper page
Abstract
Bacteriophages, viruses infecting bacteria, recognise their host with high specificity, either binding to saccharide motifs or proteins of the cell wall of their host. In the majority of bacteriophages, this host recognition is performed by Receptor Binding Proteins (RBPs) located at the extremity of a tail. Interaction between the RBPs and the host is the trigger for bacteriophage infection, but the molecular details of the mechanisms are unknown for the majority of bacteriophages. Here, we present the electron cryo-microscopy structure of bacteriophage T5 RBP pb5 in complex with its E. coli receptor, the iron ferrichrome transporter FhuA. Monomeric RBP pb5 is located at the extremity of T5 long flexible tail, and its irreversible binding to FhuA commits T5 to infection. Analysis of RBP pb5 structure within the complex, comparison with its AlphaFold2 predicted structure, and its fit into a previously determined map of T5 tail tip in complex with FhuA allow us to propose a mechanism of transmission of RBP pb5 receptor binding to the straight fibre, initiating the cascade of events that commits T5 to DNA ejection.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Degroux, S., Effantin, G., Linares, R., Schoehn, G., & Breyton, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Breyton, Cécile
- Venue
- Journal of Virology
- Publisher
- openRxiv
- Published
- 2022-09-23
- Volume
- 97
- Issue
- 3
- Pages
- e0158422-e0158422
- ISSN
- 0022-538X (ISSN-L)
- PMC
- PMC10062170
- OpenAlex
- W4320485520
- Cited by
- 49
- References
- 1
- Citations by year
- 2026: 9 · 2025: 18 · 2024: 14 · 2023: 7 · 2022: 1
- FWCI
- 7.76
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by
- Locations
- Journal of Virology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by)
- HAL (submittedVersion, other-oa)
- Funders
- Infrastructures en Biologie Santé et Agronomie (ANR-17-EURE-0003, ANR-10-INBS-05-02)
- Agence Nationale de la Recherche (UAR 3518 CNRS-CEA-UGA-EMBL, ANR-21-CE11-0023, ANR-17-EURE-0003, ANR-10-INBS-05-02, ANR-10- INBS-05, ANR-17-EURE-, ANR-16-CE11-002, ANR-20-CE11-0023, ANR-16-CE11-0027, ANR-17, ANR-10, ANR-10-INBS-0005)
- European Synchrotron Radiation Facility
- Fondation pour la Recherche Médicale (ANR-17-EURE-0003, ANR-10-INBS-05-02)
- Centre National de la Recherche Scientifique (UAR 3518 CNRS-CEA-UGA-EMBL)
- Région Auvergne-Rhône-Alpes (ANR-17-EURE-0003, ANR-10-INBS-05-02)
- French Infrastructure for Integrated Structural Biology (ANR-17-EURE-0003, ANR-10-INBS-05–02, ANR-10-INBS-0.5)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- bacteriophage T5, host recognition, receptor binding protein, FhuA, DNA injection, phage-host interactions, cryo-EM structure
- MeSH terms
- Bacterial Outer Membrane Proteins, Bacteriophages, Escherichia coli, Protein Binding, Viral Proteins, Cryoelectron Microscopy, Escherichia coli Proteins
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