Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages
Bacteriophage replication requires specific host-recognition. Some siphophages harbour a large complex, the baseplate, at the tip of their non-contractile tail. This baseplate holds receptor binding proteins (RBPs) that can recognize the host cell-wall polysaccharide (CWPS) and specifically attach t...
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| Otros Autores: | , , , |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
Blackwell Publishing Ltd
2017
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 14975caa a22014657a 4500 | ||
|---|---|---|---|
| 001 | PAPER-15032 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518204539.0 | ||
| 008 | 190410s2017 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-85014635701 | |
| 024 | 7 | |2 cas |a lactic acid, 113-21-3, 50-21-5; Carbohydrates; Lactic Acid; Viral Tail Proteins | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a MOMIE | ||
| 100 | 1 | |a Dieterle, M.-E. | |
| 245 | 1 | 0 | |a Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages |
| 260 | |b Blackwell Publishing Ltd |c 2017 | ||
| 270 | 1 | 0 | |m Piuri, M.; Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, IQUIBICEN-CONICETArgentina; email: marianapiuri@gmail.com |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a Bacteriophage replication requires specific host-recognition. Some siphophages harbour a large complex, the baseplate, at the tip of their non-contractile tail. This baseplate holds receptor binding proteins (RBPs) that can recognize the host cell-wall polysaccharide (CWPS) and specifically attach the phage to its host. While most phages possess a dedicated RBP, the phage J-1 that infects Lactobacillus casei seemed to lack one. It has been shown that the phage J-1 distal tail protein (Dit) plays a role in host recognition and that its sequence comprises two inserted modules compared with ‘classical’ Dits. The first insertion is similar to carbohydrate-binding modules (CBMs), whereas the second insertion remains undocumented. Here, we determined the structure of the second insertion and found it also similar to several CBMs. Expressed insertion CBM2, but not CBM1, binds to L. casei cells and neutralize phage attachment to the bacterial cell wall and the isolated and purified CWPS of L. casei BL23 prevents CBM2 attachment to the host. Electron microscopy single particle reconstruction of the J-1 virion baseplate revealed that CBM2 is projected at the periphery of Dit to optimally bind the CWPS receptor. Taken together, these results identify J-1 evolved Dit as the phage RBP. © 2017 John Wiley & Sons Ltd |l eng | |
| 593 | |a Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, IQUIBICEN-CONICET, Buenos Aires, Argentina | ||
| 593 | |a Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique (CNRS), Campus de Luminy, Case 932, Marseille Cedex 09, 13288, France | ||
| 593 | |a Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université (AMU), Campus de Luminy, Case 932, Marseille Cedex 09, 13288, France | ||
| 593 | |a Université Lille Nord de France, Lille, F-59000, France | ||
| 593 | |a Université du Littoral-Côte d'Opale, LR2B/UMT 08, Bassin Napoléon, BP 120, Boulogne-sur-Mer Cedex, F-62327, France | ||
| 690 | 1 | 0 | |a CARBOHYDRATE BINDING PROTEIN |
| 690 | 1 | 0 | |a CARBOHYDRATE |
| 690 | 1 | 0 | |a LACTIC ACID |
| 690 | 1 | 0 | |a PROTEIN BINDING |
| 690 | 1 | 0 | |a VIRAL PROTEIN |
| 690 | 1 | 0 | |a AMINO TERMINAL SEQUENCE |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a BACTERIAL CELL WALL |
| 690 | 1 | 0 | |a BACTERIAL STRAIN |
| 690 | 1 | 0 | |a BACTERIOPHAGE |
| 690 | 1 | 0 | |a BACTERIUM ISOLATE |
| 690 | 1 | 0 | |a CONTROLLED STUDY |
| 690 | 1 | 0 | |a ELECTRON MICROSCOPY |
| 690 | 1 | 0 | |a LACTIC ACID BACTERIUM |
| 690 | 1 | 0 | |a LACTOBACILLUS CASEI |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN BINDING |
| 690 | 1 | 0 | |a PROTEIN DOMAIN |
| 690 | 1 | 0 | |a PROTEIN EXPRESSION |
| 690 | 1 | 0 | |a PROTEIN FOLDING |
| 690 | 1 | 0 | |a VIRION |
| 690 | 1 | 0 | |a BACTERIOPHAGE |
| 690 | 1 | 0 | |a GENETICS |
| 690 | 1 | 0 | |a HOST RANGE |
| 690 | 1 | 0 | |a LACTOBACILLUS |
| 690 | 1 | 0 | |a LACTOBACILLUS CASEI |
| 690 | 1 | 0 | |a LACTOCOCCUS LACTIS |
| 690 | 1 | 0 | |a METABOLISM |
| 690 | 1 | 0 | |a PROTEIN CONFORMATION |
| 690 | 1 | 0 | |a STRUCTURE ACTIVITY RELATION |
| 690 | 1 | 0 | |a ULTRASTRUCTURE |
| 690 | 1 | 0 | |a BACTERIOPHAGES |
| 690 | 1 | 0 | |a CARBOHYDRATES |
| 690 | 1 | 0 | |a HOST SPECIFICITY |
| 690 | 1 | 0 | |a LACTIC ACID |
| 690 | 1 | 0 | |a LACTOBACILLUS |
| 690 | 1 | 0 | |a LACTOBACILLUS CASEI |
| 690 | 1 | 0 | |a LACTOCOCCUS LACTIS |
| 690 | 1 | 0 | |a MICROSCOPY, ELECTRON |
| 690 | 1 | 0 | |a PROTEIN BINDING |
| 690 | 1 | 0 | |a PROTEIN CONFORMATION |
| 690 | 1 | 0 | |a STRUCTURE-ACTIVITY RELATIONSHIP |
| 690 | 1 | 0 | |a VIRAL TAIL PROTEINS |
| 690 | 1 | 0 | |a VIRION |
| 700 | 1 | |a Spinelli, S. | |
| 700 | 1 | |a Sadovskaya, I. | |
| 700 | 1 | |a Piuri, M. | |
| 700 | 1 | |a Cambillau, C. | |
| 773 | 0 | |d Blackwell Publishing Ltd, 2017 |g v. 104 |h pp. 608-620 |k n. 4 |p Mol. Microbiol. |x 0950382X |w (AR-BaUEN)CENRE-6160 |t Molecular Microbiology | |
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