Exposing the secrets of two well-known Lactobacillus casei phages, J-1 and PL-1, by genomic and structural analysis
Bacteriophage J-1 was isolated in 1965 from an abnormal fermentation of Yakult using Lactobacillus casei strain Shirota, and a related phage, PL-1, was subsequently recovered from a strain resistant to J-1. Complete genome sequencing shows that J-1 and PL-1 are almost identical, but PL-1 has a delet...
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paper:paper_00992240_v80_n22_p7107_Dieterle2023-06-08T15:10:08Z Exposing the secrets of two well-known Lactobacillus casei phages, J-1 and PL-1, by genomic and structural analysis Turjanski, Adrián Gustavo Piuri, Mariana Bacteriophages Bins Genes Mass spectrometry Proteins Carbohydrate-binding modules Differential adsorption Lactobacillus casei Mass spectrometry analysis Proteolytic processing Sequence similarity Structural proteins Translational frameshift Crystal structure bacteriophage bacterium chemical binding fermentation genomics immunity inhibition mass spectrometry protein Lactobacillus casei Rhodococcus rhodochrous virus protein amino acid sequence bacteriophage chemistry comparative study genetics genomics Lactobacillus casei metabolism molecular genetics nucleotide sequence physiology sequence alignment Siphoviridae virology virus genome Amino Acid Sequence Bacteriophages Base Sequence Genome, Viral Genomics Lactobacillus casei Molecular Sequence Data Sequence Alignment Siphoviridae Viral Proteins Bacteriophage J-1 was isolated in 1965 from an abnormal fermentation of Yakult using Lactobacillus casei strain Shirota, and a related phage, PL-1, was subsequently recovered from a strain resistant to J-1. Complete genome sequencing shows that J-1 and PL-1 are almost identical, but PL-1 has a deletion of 1.9 kbp relative to J-1, resulting in the loss of four predicted gene products involved in immunity regulation. The structural proteins were identified by mass spectrometry analysis. Similarly to phage A2, two capsid proteins are generated by a translational frameshift and undergo proteolytic processing. The structure of gene product 16 (gp16), a putative tail protein, was modeled based on the crystal structure of baseplate distal tail proteins (Dit) that form the baseplate hub in other Siphoviridae. However, two regions of the C terminus of gp16 could not be modeled using this template. The first region accounts for the differences between J-1 and PL-1 gp16 and showed sequence similarity to carbohydratebinding modules (CBMs). J-1 and PL-1 GFP-gp16 fusions bind specifically to Lactobacillus casei/paracasei cells, and the addition of L-rhamnose inhibits binding. J-1 gp16 exhibited a higher affinity than PL-1 gp16 for cell walls of L. casei ATCC 27139 in phage adsorption inhibition assays, in agreement with differential adsorption kinetics observed for both phages in this strain. The data presented here provide insights into how Lactobacillus phages interact with their hosts at the first steps of infection. © 2014, American Society for Microbiology. Fil:Turjanski, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Piuri, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00992240_v80_n22_p7107_Dieterle http://hdl.handle.net/20.500.12110/paper_00992240_v80_n22_p7107_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 |
Bacteriophages Bins Genes Mass spectrometry Proteins Carbohydrate-binding modules Differential adsorption Lactobacillus casei Mass spectrometry analysis Proteolytic processing Sequence similarity Structural proteins Translational frameshift Crystal structure bacteriophage bacterium chemical binding fermentation genomics immunity inhibition mass spectrometry protein Lactobacillus casei Rhodococcus rhodochrous virus protein amino acid sequence bacteriophage chemistry comparative study genetics genomics Lactobacillus casei metabolism molecular genetics nucleotide sequence physiology sequence alignment Siphoviridae virology virus genome Amino Acid Sequence Bacteriophages Base Sequence Genome, Viral Genomics Lactobacillus casei Molecular Sequence Data Sequence Alignment Siphoviridae Viral Proteins |
| spellingShingle |
Bacteriophages Bins Genes Mass spectrometry Proteins Carbohydrate-binding modules Differential adsorption Lactobacillus casei Mass spectrometry analysis Proteolytic processing Sequence similarity Structural proteins Translational frameshift Crystal structure bacteriophage bacterium chemical binding fermentation genomics immunity inhibition mass spectrometry protein Lactobacillus casei Rhodococcus rhodochrous virus protein amino acid sequence bacteriophage chemistry comparative study genetics genomics Lactobacillus casei metabolism molecular genetics nucleotide sequence physiology sequence alignment Siphoviridae virology virus genome Amino Acid Sequence Bacteriophages Base Sequence Genome, Viral Genomics Lactobacillus casei Molecular Sequence Data Sequence Alignment Siphoviridae Viral Proteins Turjanski, Adrián Gustavo Piuri, Mariana Exposing the secrets of two well-known Lactobacillus casei phages, J-1 and PL-1, by genomic and structural analysis |
| topic_facet |
Bacteriophages Bins Genes Mass spectrometry Proteins Carbohydrate-binding modules Differential adsorption Lactobacillus casei Mass spectrometry analysis Proteolytic processing Sequence similarity Structural proteins Translational frameshift Crystal structure bacteriophage bacterium chemical binding fermentation genomics immunity inhibition mass spectrometry protein Lactobacillus casei Rhodococcus rhodochrous virus protein amino acid sequence bacteriophage chemistry comparative study genetics genomics Lactobacillus casei metabolism molecular genetics nucleotide sequence physiology sequence alignment Siphoviridae virology virus genome Amino Acid Sequence Bacteriophages Base Sequence Genome, Viral Genomics Lactobacillus casei Molecular Sequence Data Sequence Alignment Siphoviridae Viral Proteins |
| description |
Bacteriophage J-1 was isolated in 1965 from an abnormal fermentation of Yakult using Lactobacillus casei strain Shirota, and a related phage, PL-1, was subsequently recovered from a strain resistant to J-1. Complete genome sequencing shows that J-1 and PL-1 are almost identical, but PL-1 has a deletion of 1.9 kbp relative to J-1, resulting in the loss of four predicted gene products involved in immunity regulation. The structural proteins were identified by mass spectrometry analysis. Similarly to phage A2, two capsid proteins are generated by a translational frameshift and undergo proteolytic processing. The structure of gene product 16 (gp16), a putative tail protein, was modeled based on the crystal structure of baseplate distal tail proteins (Dit) that form the baseplate hub in other Siphoviridae. However, two regions of the C terminus of gp16 could not be modeled using this template. The first region accounts for the differences between J-1 and PL-1 gp16 and showed sequence similarity to carbohydratebinding modules (CBMs). J-1 and PL-1 GFP-gp16 fusions bind specifically to Lactobacillus casei/paracasei cells, and the addition of L-rhamnose inhibits binding. J-1 gp16 exhibited a higher affinity than PL-1 gp16 for cell walls of L. casei ATCC 27139 in phage adsorption inhibition assays, in agreement with differential adsorption kinetics observed for both phages in this strain. The data presented here provide insights into how Lactobacillus phages interact with their hosts at the first steps of infection. © 2014, American Society for Microbiology. |
| author |
Turjanski, Adrián Gustavo Piuri, Mariana |
| author_facet |
Turjanski, Adrián Gustavo Piuri, Mariana |
| author_sort |
Turjanski, Adrián Gustavo |
| title |
Exposing the secrets of two well-known Lactobacillus casei phages, J-1 and PL-1, by genomic and structural analysis |
| title_short |
Exposing the secrets of two well-known Lactobacillus casei phages, J-1 and PL-1, by genomic and structural analysis |
| title_full |
Exposing the secrets of two well-known Lactobacillus casei phages, J-1 and PL-1, by genomic and structural analysis |
| title_fullStr |
Exposing the secrets of two well-known Lactobacillus casei phages, J-1 and PL-1, by genomic and structural analysis |
| title_full_unstemmed |
Exposing the secrets of two well-known Lactobacillus casei phages, J-1 and PL-1, by genomic and structural analysis |
| title_sort |
exposing the secrets of two well-known lactobacillus casei phages, j-1 and pl-1, by genomic and structural analysis |
| publishDate |
2014 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00992240_v80_n22_p7107_Dieterle http://hdl.handle.net/20.500.12110/paper_00992240_v80_n22_p7107_Dieterle |
| work_keys_str_mv |
AT turjanskiadriangustavo exposingthesecretsoftwowellknownlactobacilluscaseiphagesj1andpl1bygenomicandstructuralanalysis AT piurimariana exposingthesecretsoftwowellknownlactobacilluscaseiphagesj1andpl1bygenomicandstructuralanalysis |
| _version_ |
1768545088808419328 |