ArticleJournal of virology2013
Structure, adsorption to host, and infection mechanism of virulent lactococcal phage p2.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 107 citations in OpenAlex.
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- Functional Evaluation of a Conserved HNH Endonuclease Gene in Lactococcal Skunavirus Genomes.Microbial biotechnology · 2026Article
- Bacterial defense mechanisms against bacteriophages: an evolutionary arms race.Archives of microbiology · 2026Review
- Structure of a Brochothrix thermosphacta bacteriophage reveals cell wall adsorption mechanism in Gram-positive infecting siphophages.Nature communications · 2026Article
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- Proteomic Analysis of Marine Bacteriophages: Structural Conservation, Post-Translational Modifications, and Phage-Host Interactions.Environmental microbiology · 2025Article
- Functional and practical insights into three lactococcal antiphage systems.Applied and environmental microbiology · 2024Article
- Isolation and characterization of lytic bacteriophages from various sources in Addis Ababa against antimicrobial-resistant diarrheagenic Escherichia coli strains and evaluation of their therapeutic potential.BMC infectious diseases · 2024Article
- Bacteriophage Receptor Recognition and Nucleic Acid Transfer.Sub-cellular biochemistry · 2024Review
- Molecular mechanisms underlying the structural diversity of rhamnose-rich cell wall polysaccharides in lactococci.The Journal of biological chemistry · 2024Article
- Partial Atomic Model of the Tailed Lactococcal Phage TP901-1 as Predicted by AlphaFold2: Revelations and Limitations.Viruses · 2023Article
- PBP2b Mutations Improve the Growth of Phage-ResistantApplied and environmental microbiology · 2023Article
- Bacteriophages in Infectious Diseases and Beyond-A Narrative Review.Antibiotics (Basel, Switzerland) · 2023Review
- Rheinheimera faecalis sp. nov., isolated from Ceratotherium simum feces.Archives of microbiology · 2023Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 3 countries.
Funding
Abstract
Lactococcal siphophages from the 936 and P335 groups infect the Gram-positive bacterium Lactococcus lactis using receptor binding proteins (RBPs) attached to their baseplate, a large multiprotein complex at the distal part of the tail. We have previously reported the crystal and electron microscopy (EM) structures of the baseplates of phages p2 (936 group) and TP901-1 (P335 group) as well as the full EM structure of the TP901-1 virion. Here, we report the complete EM structure of siphophage p2, including its capsid, connector complex, tail, and baseplate. Furthermore, we show that the p2 tail is characterized by the presence of protruding decorations, which are related to adhesins and are likely contributed by the major tail protein C-terminal domains. This feature is reminiscent of the tail of Escherichia coli phage λ and Bacillus subtilis phage SPP1 and might point to a common mechanism for establishing initial interactions with their bacterial hosts. Comparative analyses showed that the architecture of the phage p2 baseplate differs largely from that of lactococcal phage TP901-1. We quantified the interaction of its RBP with the saccharidic receptor and determined that specificity is due to lower k(off) values of the RBP/saccharidic dissociation. Taken together, these results suggest that the infection of L. lactis strains by phage p2 is a multistep process that involves reversible attachment, followed by baseplate activation, specific attachment of the RBPs to the saccharidic receptor, and DNA ejection.
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Registered trials
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.