Molecular insights on the recognition of a Lactococcus lactis cell wall pellicle by the phage 1358 receptor binding protein

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DOIResolve DOI: http://doi.org/10.1128/JVI.00739-14
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TypeArticle
Journal titleJournal of Virology
ISSN1098-5514
Volume88
Issue12
Pages70057015; # of pages: 11
Subjectbinding protein; glucose 1 phosphate; monomer; monosaccharide; phage 1358 receptor binding protein; unclassified drug; article; bacterial cell wall; bacterial cell wall pellicle; bacteriophage; binding site; cell surface; controlled study; crystal structure; Lactococcus lactis; nonhuman; phage 1358; phage TP091 1; priority journal; protein carbohydrate interaction; protein domain; protein motif; protein structure
AbstractThe Gram-positive bacterium Lactococcus lactis is used for the production of cheeses and other fermented dairy products. Accidental infection of L. lactis cells by virulent lactococcal tailed phages is one of the major risks of fermentation failures in industrial dairy factories. Lactococcal phage 1358 possesses a host range limited to a few L. lactis strains and strong genomic similarities to Listeria phages. We report here the X-ray structures of phage 1358 receptor binding protein (RBP) in complex with monosaccharides. Each monomer of its trimeric RBP is formed of two domains: a "shoulder" domain linking the RBP to the rest of the phage and a jelly roll fold "head/host recognition" domain. This domain harbors a saccharide binding crevice located in the middle of a monomer. Crystal structures identified two sites at the RBP surface,̃8 Å from each other, one accommodating a GlcNAc monosaccharide and the other accommodating a GlcNAc or a glucose 1-phosphate (Glc1P) monosaccharide. GlcNAc and GlcNAc1P are components of the polysaccharide pellicle that we identified at the cell surface of L. lactis SMQ-388, the host of phage 1358. We therefore modeled a galactofuranose (Galf) sugar bridging the two GlcNAc saccharides, suggesting that the trisaccharidic motif GlcNAc-Galf-GlcNAc (or Glc1P) might be common to receptors of genetically distinct lactococcal phages p2, TP091-1, and 1358. Strain specificity might therefore be elicited by steric clashes induced by the remaining components of the pellicle hexasaccharide. Taken together, these results provide a first insight into the molecular mechanism of host receptor recognition by lactococcal phages. © 2014, American Society for Microbiology.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences (IBS-ISB)
Peer reviewedYes
NPARC number21272263
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Record identifierfcf3eeaa-bf53-49d3-95d9-91ecedb26857
Record created2014-07-23
Record modified2016-05-09
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