ArticlePLoS biology2023
Structure of the siphophage neck-Tail complex suggests that conserved tail tip proteins facilitate receptor binding and tail assembly.
Article in PLoS biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 39 citations in OpenAlex.
- The Lord of the Rings: Cysteine bonds crosslink the tail of siphovirus.Protein science : a publication of the Protein Society · 2026Article
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- F-Type Pyocin Versus Phage λ Tail: Conserved Hub, Divergent Fibers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Extensive library ofMicrobiology spectrum · 2026Article
- Intact architectures of myophage phi92 in extended and contracted states.PLoS pathogens · 2026Article
- Isolation and characterization of Avs-1, a bacteriophage effective against the aquaculture pathogenApplied and environmental microbiology · 2026Article
- Isolation and characterisation of a novel Stenotrophomonas maltophilia phage vB_SmaS_BCU-1 with evaluation of mammalian cell safety.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Article
- Extensive screening of ten bacteriophage cocktails revealed an optimal combination with potent therapeutic activity against Acinetobacter baumannii.Scientific reports · 2026Article
- Genome characterization and receptor-binding protein identification of Klebsiella phage vB_VIPKPNMC05, a member of a novel viral family Pituviridae.Archives of virology · 2026Article
- In situ structures of the portal-neck-tail complex of bacteriophage T4 inform a viral genome positioning mechanism.Nature communications · 2026Article
- Cryo-EM structures of bacteriophage T4 portal-neck assembly intermediates reveal a viral genome retention mechanism.Nature communications · 2026Article
- A dramatic protein fold switch powers a bactericidal nanomachine.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
- Article
- Structure of defense against restriction proteins DarA and Hdf in phage P1 reveals a new molecular mechanism during phage assembly, infection and DNA ejection.PLoS pathogens · 2026Article
- Review
- Structural basis of bacteriophage Ur-lambda infection initiation.Science advances · 2025Article
- Novel and recurrent mutations in exon 8 of natural killer group 2D (NKG2D) gene among chronic myeloid leukemia patients and their potential role in pathogenesis.Molecular biology reports · 2025Article
- Predicted Structures ofViruses · 2025Article
- Characterization of strictly lytic phages infectingMicrobiology spectrum · 2025Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Siphophages have a long, flexible, and noncontractile tail that connects to the capsid through a neck. The phage tail is essential for host cell recognition and virus-host cell interactions; moreover, it serves as a channel for genome delivery during infection. However, the in situ high-resolution structure of the neck-tail complex of siphophages remains unknown. Here, we present the structure of the siphophage lambda "wild type," the most widely used, laboratory-adapted fiberless mutant. The neck-tail complex comprises a channel formed by stacked 12-fold and hexameric rings and a 3-fold symmetrical tip. The interactions among DNA and a total of 246 tail protein molecules forming the tail and neck have been characterized. Structural comparisons of the tail tips, the most diversified region across the lambda and other long-tailed phages or tail-like machines, suggest that their tail tip contains conserved domains, which facilitate tail assembly, receptor binding, cell adsorption, and DNA retaining/releasing. These domains are distributed in different tail tip proteins in different phages or tail-like machines. The side tail fibers are not required for the phage particle to orient itself vertically to the surface of the host cell during attachment.
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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.