Deciphering Bacteriophage T5 Host Recognition Mechanism and Infection Trigger
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Abstract
Tailed bacteriophages specifically recognize their bacterial host by interaction of their receptor binding protein(s) (RBPs) with saccharides and/or proteins located at the surface of their prey. This crucial interaction commits the virus to infection, but the molecular details of this mechanism are unknown for the majority of bacteriophages.
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Cites
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 · see citing works
ColabFold - Making protein folding accessible to all
Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391 · see citing works
Protein complex prediction with AlphaFold-Multimer
Evans, R., O’Neill, M., Pritzel, A., Antropova, N., Senior, A., Green, T., Žídek, A., Bates, R., Blackwell, S., Yim, J., et al. (2021) · doi:10.1101/2021.10.04.463034 · Cited by 3,808 · see citing works
Highly accurate protein structure prediction for the human proteome
Tunyasuvunakool, K., Adler, J., Wu, Z., Green, T., Zielinski, M., Žídek, A., Bridgland, A., Cowie, A., Meyer, C., Laydon, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03828-1 · Cited by 3,025 · cited 2× · see citing works
“…from 7.6 to 18.2 Å over all 572 residues for the five AF-RBPpb5 models). pLDDT values below 50 are indicated to be strong predictors of disorder (Tunyasuvunakool et al, 2021), suggesting that the regions are unstructured in physiological conditions: they would only fold upon interaction with…”
BackgroundInfluentialKühlbrandt, W. (2014) · Science · doi:10.1126/science.1251652 · Cited by 1,325 · see citing works
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- 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
- American Society for Microbiology
- Published
- 2023-03-30
- Volume
- 97
- Issue
- 3
- Pages
- e0158422-e0158422
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC10062170
- OpenAlex
- W4320485520
- Cited by
- 49
- References
- 5
- Citations by year
- 2026: 9 · 2025: 18 · 2024: 14 · 2023: 7 · 2022: 1
- FWCI
- 7.75
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- 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
- Agence Nationale de la Recherche (ANR-16-CE11-002, ANR-21-CE11-0023, ANR-10-INBS-05-02, ANR-17-EURE-0003)
- Topics
- Physical Sciences › Environmental Science › Ecology › Bacteriophages and microbial interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Physical Sciences › Materials Science › Materials Chemistry › 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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