The targeted recognition of <scp><i>L</i></scp><i>actococcus lactis</i> phages to their polysaccharide receptors

McCabe, Orla; Spinelli, S.; Farenc, Carine; Labbé, Myriam; Tremblay, Denise M.; Blangy, Stéphanie; Oscarson, Stefan; Moineau, Sylvain; Cambillau, Christian

doi:10.1111/mmi.12978

Cited by 40 publications

(33 citation statements)

References 40 publications

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“… Comparison of the four RBPs from lactococcal phages of known structure. (A to D) RBPs of phages 1358 ( 40 , 77 ) (A), p2 ( 53 ) (B), TP901-1 ( 25 , 42 ) (C), and Tuc2009 (D). The RBP trimers are rainbow colored.…”

Section: Discussionmentioning

confidence: 99%

The Atomic Structure of the Phage Tuc2009 Baseplate Tripod Suggests that Host Recognition Involves Two Different Carbohydrate Binding Modules

Legrand

Collins

Blangy

et al. 2016

mBio

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The Gram-positive bacterium Lactococcus lactis, used for the production of cheeses and other fermented dairy products, falls victim frequently to fortuitous infection by tailed phages. The accompanying risk of dairy fermentation failures in industrial facilities has prompted in-depth investigations of these phages. Lactococcal phage Tuc2009 possesses extensive genomic homology to phage TP901-1. However, striking differences in the baseplate-encoding genes stimulated our interest in solving the structure of this host’s adhesion device. We report here the X-ray structures of phage Tuc2009 receptor binding protein (RBP) and of a “tripod” assembly of three baseplate components, BppU, BppA, and BppL (the RBP). These structures made it possible to generate a realistic atomic model of the complete Tuc2009 baseplate that consists of an 84-protein complex: 18 BppU, 12 BppA, and 54 BppL proteins. The RBP head domain possesses a different fold than those of phages p2, TP901-1, and 1358, while the so-called “stem” and “neck” domains share structural features with their equivalents in phage TP901-1. The BppA module interacts strongly with the BppU N-terminal domain. Unlike other characterized lactococcal phages, Tuc2009 baseplate harbors two different carbohydrate recognition sites: one in the bona fide RBP head domain and the other in BppA. These findings represent a major step forward in deciphering the molecular mechanism by which Tuc2009 recognizes its saccharidic receptor(s) on its host.

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Section: Discussionmentioning

confidence: 99%

The Atomic Structure of the Phage Tuc2009 Baseplate Tripod Suggests that Host Recognition Involves Two Different Carbohydrate Binding Modules

Legrand

Collins

Blangy

et al. 2016

mBio

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“…In contrast, ϕ11 Gp45, the RBP, does not exhibit analogy with other phage RBPs, in particular with those from lactococcal phages that also bind to saccharidic receptors. Lactococcal phages p2 52, TP901-1 53, Tuc2009 19, bIL170 54 and 1358 4 all possess a trimeric receptor recognition head sharing a bona fide or a modified jelly-roll motif. The rest of their RBPs share common motifs in the neck or in the N-terminal domain (or stem).…”

Section: Discussionmentioning

confidence: 99%

Structure of the host-recognition device of Staphylococcus aureus phage ϕ11

Koç

Xia

Kühner

et al. 2016

Sci Rep

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Phages play key roles in the pathogenicity and adaptation of the human pathogen Staphylococcus aureus. However, little is known about the molecular recognition events that mediate phage adsorption to the surface of S. aureus. The lysogenic siphophage ϕ11 infects S. aureus SA113. It was shown previously that ϕ11 requires α- or β-N-acetylglucosamine (GlcNAc) moieties on cell wall teichoic acid (WTA) for adsorption. Gp45 was identified as the receptor binding protein (RBP) involved in this process and GlcNAc residues on WTA were found to be the key component of the ϕ11 receptor. Here we report the crystal structure of the RBP of ϕ11, which assembles into a large, multidomain homotrimer. Each monomer contains a five-bladed propeller domain with a cavity that could accommodate a GlcNAc moiety. An electron microscopy reconstruction of the ϕ11 host adhesion component, the baseplate, reveals that six RBP trimers are assembled around the baseplate core. The Gp45 and baseplate structures provide insights into the overall organization and molecular recognition process of the phage ϕ11 tail. This assembly is conserved among most glycan-recognizing Siphoviridae, and the RBP orientation would allow host adhesion and infection without an activation step.

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“…Other studies failed to reveal a significant phage resistant phenotype in EPS and CPS producer strains ( Deveau et al, 2002 ; Rodriguez et al, 2008 ); in contrast, McCabe et al (2015) recently reported on the targeted recognition of Lactococcus lactis phages to their polysaccharide receptors.…”

Section: Role Of Eps-producing Lab and Their Polymersmentioning

confidence: 98%

Biopolymers from lactic acid bacteria. Novel applications in foods and beverages

2015

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Lactic acid bacteria (LAB) are microorganisms widely used in the fermented food industry worldwide. Certain LAB are able to produce exopolysaccharides (EPS) either attached to the cell wall (capsular EPS) or released to the extracellular environment (EPS). According to their composition, LAB may synthesize heteropolysaccharides or homopolysaccharides. A wide diversity of EPS are produced by LAB concerning their monomer composition, molecular mass, and structure. Although EPS-producing LAB strains have been traditionally applied in the manufacture of dairy products such as fermented milks and yogurts, their use in the elaboration of low-fat cheeses, diverse type of sourdough breads, and certain beverages are some of the novel applications of these polymers. This work aims to collect the most relevant issues of the former reviews concerning the monomer composition, structure, and yields and biosynthetic enzymes of EPS from LAB; to describe the recently characterized EPS and to present the application of both EPS-producing strains and their polymers in the fermented (specifically beverages and cereal-based) food industry.

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The targeted recognition of Lactococcus lactis phages to their polysaccharide receptors

Cited by 40 publications

References 40 publications

The Atomic Structure of the Phage Tuc2009 Baseplate Tripod Suggests that Host Recognition Involves Two Different Carbohydrate Binding Modules

The Atomic Structure of the Phage Tuc2009 Baseplate Tripod Suggests that Host Recognition Involves Two Different Carbohydrate Binding Modules

Structure of the host-recognition device of Staphylococcus aureus phage ϕ11

Biopolymers from lactic acid bacteria. Novel applications in foods and beverages

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