ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structure of lactococcal phage p2 baseplate and its mechanism of activation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
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Who cites it
97 citing papers in PubMed.
- Cryo-EM structure of bacteriophage Nocturne116: insights into the architecture of c2-likeJournal of virology · 2026Article
- Conformational changes of the baseplate regulating tail contraction of Staphylococcus phage 812.The EMBO journal · 2026Article
- Dynamic adhesion device of phage OE33PA drives Gram-positive host recognition.bioRxiv : the preprint server for biology · 2026Article
- Structure of a Brochothrix thermosphacta bacteriophage reveals cell wall adsorption mechanism in Gram-positive infecting siphophages.Nature communications · 2026Article
- TheJournal of virology · 2025Article
- Structural determinants of SlpA-mediated phage recognition in Clostridioides difficile.PLoS pathogens · 2025Article
- Predicted Structures ofViruses · 2025Article
- Characterization of strictly lytic phages infectingMicrobiology spectrum · 2025Article
- Lactococcal phage-host profiling through binding studies between cell wall polysaccharide types andMicrobial genomics · 2025Article
- Isolation of phages infecting the zoonotic pathogenbioRxiv : the preprint server for biology · 2025Article
- Viral Genome Delivery Across Bacterial Cell Surfaces.Annual review of microbiology · 2024Review
- Structure and replication of Pseudomonas aeruginosa phage JBD30.The EMBO journal · 2024Article
- Deciphering the adsorption machinery of Deep-Blue and Vp4, two myophages targeting members of theJournal of virology · 2024Article
- NanoBERTa-ASP: predicting nanobody paratope based on a pretrained RoBERTa model.BMC bioinformatics · 2024Article
- Bacteriophage Receptor Recognition and Nucleic Acid Transfer.Sub-cellular biochemistry · 2024Review
- Partial Atomic Model of the Tailed Lactococcal Phage TP901-1 as Predicted by AlphaFold2: Revelations and Limitations.Viruses · 2023Article
- Structure of the siphophage neck-Tail complex suggests that conserved tail tip proteins facilitate receptor binding and tail assembly.PLoS biology · 2023Article
- Exploring Host-Binding Machineries of Mycobacteriophages with AlphaFold2.Journal of virology · 2023Article
- Structural basis of bacteriophage T5 infection trigger andScience advances · 2023Article
- Phage Adsorption to Gram-Positive Bacteria.Viruses · 2023Review
37 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors.
Funding
Abstract
Siphoviridae is the most abundant viral family on earth which infects bacteria as well as archaea. All known siphophages infecting gram+ Lactococcus lactis possess a baseplate at the tip of their tail involved in host recognition and attachment. Here, we report analysis of the p2 phage baseplate structure by X-ray crystallography and electron microscopy and propose a mechanism for the baseplate activation during attachment to the host cell. This approximately 1 MDa, Escherichia coli-expressed baseplate is composed of three protein species, including six trimers of the receptor-binding protein (RBP). RBPs host-recognition domains point upwards, towards the capsid, in agreement with the electron-microscopy map of the free virion. In the presence of Ca(2+), a cation mandatory for infection, the RBPs rotated 200 degrees downwards, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA passage. These conformational changes reveal a novel siphophage activation and host-recognition mechanism leading ultimately to DNA ejection.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.