ArticleApplied and environmental microbiology2004
Identification of Lactococcus lactis genes required for bacteriophage adsorption.
Article in Applied and environmental microbiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Members of theMicrobial genomics · 2026Article
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- The cell surface-associated rhamnose-glucose polysaccharide represents the receptor ofApplied and environmental microbiology · 2025Article
- Dual Nature of Bacteriophages: Friends or Foes in Minimally Processed Food Products-A Comprehensive Review.Viruses · 2025Review
- Lactococcal phage-host profiling through binding studies between cell wall polysaccharide types andMicrobial genomics · 2025Article
- Article
- PBP2b Mutations Improve the Growth of Phage-ResistantApplied and environmental microbiology · 2023Article
- Host genetic requirements for DNA release of lactococcal phage TP901-1.Microbial biotechnology · 2022Article
- Brussowvirus SW13 Requires a Cell Surface-Associated Polysaccharide To Recognize Its Streptococcus thermophilus Host.Applied and environmental microbiology · 2022Article
- Bacteriophage-host interactions as a platform to establish the role of phages in modulating the microbial composition of fermented foods.Microbiome research reports · 2022Review
- Cell wall polysaccharides of Gram positive ovococcoid bacteria and their role as bacteriophage receptors.Computational and structural biotechnology journal · 2021Review
- Three distinct glycosylation pathways are involved in the decoration ofThe Journal of biological chemistry · 2020Article
- Article
- A Specific Sugar Moiety in the Lactococcus lactis Cell Wall Pellicle Is Required for Infection by CHPC971, a Member of the Rare 1706 Phage Species.Applied and environmental microbiology · 2019Article
- Comparative Genome Analysis ofFrontiers in microbiology · 2019Article
- Review
- Generation of Bacteriophage-Insensitive Mutants of Streptococcus thermophilus via an Antisense RNA CRISPR-Cas Silencing Approach.Applied and environmental microbiology · 2018Article
- Genetic and functional characterisation of the lactococcal P335 phage-host interactions.BMC genomics · 2017Article
- The Baseplate of Lactobacillus delbrueckii Bacteriophage Ld17 Harbors a Glycerophosphodiesterase.The Journal of biological chemistry · 2016Article
- Bacterial glycobiology: rhamnose-containing cell wall polysaccharides in Gram-positive bacteria.FEMS microbiology reviews · 2016Review
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The aim of this work was to identify genes in Lactococcus lactis subsp. lactis IL1403 and Lactococcus lactis subsp. cremoris Wg2 important for adsorption of the 936-species phages bIL170 and phi 645, respectively. Random insertional mutagenesis of the two L. lactis strains was carried out with the vector pGh9:ISS1, and integrants that were resistant to phage infection and showed reduced phage adsorption were selected. In L. lactis IL1403 integration was obtained in the ycaG and rgpE genes, whereas in L. lactis Wg2 integration was obtained in two genes homologous to ycbC and ycbB of L. lactis IL1403. rgpE and ycbB encode putative glycosyltransferases, whereas ycaG and ycbC encode putative membrane-spanning proteins with unknown functions. Interestingly, ycaG, rgpE, ycbC, and ycbB are all part of the same operon in L. lactis IL1403. This operon is probably involved in biosynthesis and transport of cell wall polysaccharides (WPS). Binding and infection studies showed that phi645 binds to and infects L. lactis Wg2, L. lactis IL1403, and L. lactis IL1403 strains with pGh9:ISS1 integration in ycaG and rgpE, whereas bIL170 binds to and infects only L. lactis IL1403 and cannot infect Wg2. These results indicate that phi 645 binds to a WPS structure present in both L. lactis IL1403 and L. lactis Wg2, whereas bIL170 binds to another WPS structure not present in L. lactis Wg2. Binding of bIL170 and phi 645 to different WPS structures was supported by alignment of the receptor-binding proteins of bIL170 and phi 645 that showed no homology in the C-terminal part.
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