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Abstract:

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

Registro:

Documento: Artículo
Título:Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages
Autor:Dieterle, M.-E.; Spinelli, S.; Sadovskaya, I.; Piuri, M.; Cambillau, C.
Filiación:Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, IQUIBICEN-CONICET, Buenos Aires, Argentina
Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique (CNRS), Campus de Luminy, Case 932, Marseille Cedex 09, 13288, France
Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université (AMU), Campus de Luminy, Case 932, Marseille Cedex 09, 13288, France
Université Lille Nord de France, Lille, F-59000, France
Université du Littoral-Côte d'Opale, LR2B/UMT 08, Bassin Napoléon, BP 120, Boulogne-sur-Mer Cedex, F-62327, France
Palabras clave:carbohydrate binding protein; carbohydrate; lactic acid; protein binding; viral protein; amino terminal sequence; Article; bacterial cell wall; bacterial strain; bacteriophage; bacterium isolate; controlled study; electron microscopy; lactic acid bacterium; Lactobacillus casei; nonhuman; priority journal; protein binding; protein domain; protein expression; protein folding; virion; bacteriophage; genetics; host range; Lactobacillus; Lactobacillus casei; Lactococcus lactis; metabolism; protein conformation; structure activity relation; ultrastructure; Bacteriophages; Carbohydrates; Host Specificity; Lactic Acid; Lactobacillus; Lactobacillus casei; Lactococcus lactis; Microscopy, Electron; Protein Binding; Protein Conformation; Structure-Activity Relationship; Viral Tail Proteins; Virion
Año:2017
Volumen:104
Número:4
Página de inicio:608
Página de fin:620
DOI: http://dx.doi.org/10.1111/mmi.13649
Título revista:Molecular Microbiology
Título revista abreviado:Mol. Microbiol.
ISSN:0950382X
CODEN:MOMIE
CAS:lactic acid, 113-21-3, 50-21-5; Carbohydrates; Lactic Acid; Viral Tail Proteins
Registro:http://digital.bl.fcen.uba.ar/collection/paper/document/paper_0950382X_v104_n4_p608_Dieterle

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Citas:

---------- APA ----------
Dieterle, M.-E., Spinelli, S., Sadovskaya, I., Piuri, M. & Cambillau, C. (2017) . Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages. Molecular Microbiology, 104(4), 608-620.
http://dx.doi.org/10.1111/mmi.13649
---------- CHICAGO ----------
Dieterle, M.-E., Spinelli, S., Sadovskaya, I., Piuri, M., Cambillau, C. "Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages" . Molecular Microbiology 104, no. 4 (2017) : 608-620.
http://dx.doi.org/10.1111/mmi.13649
---------- MLA ----------
Dieterle, M.-E., Spinelli, S., Sadovskaya, I., Piuri, M., Cambillau, C. "Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages" . Molecular Microbiology, vol. 104, no. 4, 2017, pp. 608-620.
http://dx.doi.org/10.1111/mmi.13649
---------- VANCOUVER ----------
Dieterle, M.-E., Spinelli, S., Sadovskaya, I., Piuri, M., Cambillau, C. Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages. Mol. Microbiol. 2017;104(4):608-620.
http://dx.doi.org/10.1111/mmi.13649