ArticleJournal of bacteriology2006
Receptor-binding protein of Lactococcus lactis phages: identification and characterization of the saccharide receptor-binding site.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 114 citations in OpenAlex.
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- Characterization and genome analysis of a novel phage BP15 infecting Vibrio parahaemolyticus.Scientific reports · 2025Article
- Viral Genome Delivery Across Bacterial Cell Surfaces.Annual review of microbiology · 2024Review
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- Characterization of the Attachment of Three New Coliphages onto the Ferrichrome Transporter FhuA.Journal of virology · 2023Article
- Phage Adsorption to Gram-Positive Bacteria.Viruses · 2023Review
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- Intestinal virome and therapeutic potential of bacteriophages in liver disease.Journal of hepatology · 2021Review
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- Lysogenization of a Lactococcal Host with Three Distinct Temperate Phages Provides Homologous and Heterologous Phage Resistance.Microorganisms · 2020Article
- Glycotyping and Specific Separation of Listeria monocytogenes with a Novel Bacteriophage Protein Tool Kit.Applied and environmental microbiology · 2020Article
- Three distinct glycosylation pathways are involved in the decoration ofThe Journal of biological chemistry · 2020Article
- Phage diversity, genomics and phylogeny.Nature reviews. Microbiology · 2020Review
- Structure and genome ejection mechanism ofScience advances · 2019Article
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- A comparative genomics approach for identifying host-range determinants in Streptococcus thermophilus bacteriophages.Scientific reports · 2019Article
- Identification of Dual Receptor Binding Protein Systems in Lactococcal 936 Group Phages.Viruses · 2018Article
7 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phage p2, a member of the lactococcal 936 phage species, infects Lactococcus lactis strains by binding initially to specific carbohydrate receptors using its receptor-binding protein (RBP). The structures of p2 RBP, a homotrimeric protein composed of three domains, and of its complex with a neutralizing llama VH domain (VHH5) have been determined (S. Spinelli, A. Desmyter, C. T. Verrips, H. J. de Haard, S. Moineau, and C. Cambillau, Nat. Struct. Mol. Biol. 13:85-89, 2006). Here, we show that VHH5 was able to neutralize 12 of 50 lactococcal phages belonging to the 936 species. Moreover, escape phage mutants no longer neutralized by VHH5 were isolated from 11 of these phages. All of the mutations (but one) cluster in the RBP/VHH5 interaction surface that delineates the receptor-binding area. A glycerol molecule, observed in the 1.7-A resolution structure of RBP, was found to bind tightly (Kd= 0.26 microM) in a crevice located in this area. Other saccharides bind RBP with comparable high affinity. These data prove the saccharidic nature of the bacterial receptor recognized by phage p2 and identify the position of its binding site in the RBP head domain.
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