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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2017
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0950382X_v104_n4_p608_Dieterle http://hdl.handle.net/20.500.12110/paper_0950382X_v104_n4_p608_Dieterle |
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paper:paper_0950382X_v104_n4_p608_Dieterle2023-06-08T15:54:24Z Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages Piuri, Mariana 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 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 Fil:Piuri, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2017 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0950382X_v104_n4_p608_Dieterle http://hdl.handle.net/20.500.12110/paper_0950382X_v104_n4_p608_Dieterle |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Piuri, Mariana Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages |
| topic_facet |
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 |
| description |
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 |
| author |
Piuri, Mariana |
| author_facet |
Piuri, Mariana |
| author_sort |
Piuri, Mariana |
| title |
Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages |
| title_short |
Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages |
| title_full |
Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages |
| title_fullStr |
Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages |
| title_full_unstemmed |
Evolved distal tail carbohydrate binding modules of Lactobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages |
| title_sort |
evolved distal tail carbohydrate binding modules of lactobacillus phage j-1: a novel type of anti-receptor widespread among lactic acid bacteria phages |
| publishDate |
2017 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0950382X_v104_n4_p608_Dieterle http://hdl.handle.net/20.500.12110/paper_0950382X_v104_n4_p608_Dieterle |
| work_keys_str_mv |
AT piurimariana evolveddistaltailcarbohydratebindingmodulesoflactobacillusphagej1anoveltypeofantireceptorwidespreadamonglacticacidbacteriaphages |
| _version_ |
1768544234539843584 |