Characterization of prophages containing "evolved" Dit/Tal modules in the genome of Lactobacillus casei BL23.
Identifieur interne : 000073 ( Main/Merge ); précédent : 000072; suivant : 000074Characterization of prophages containing "evolved" Dit/Tal modules in the genome of Lactobacillus casei BL23.
Auteurs : María Eugenia Dieterle [Argentine] ; Joaquina Fina Martin [Argentine] ; Rosario Durán [Uruguay] ; Sergio I. Nemirovsky [Argentine] ; Carmen Sanchez Rivas [Argentine] ; Charles Bowman [États-Unis] ; Daniel Russell [États-Unis] ; Graham F. Hatfull [États-Unis] ; Christian Cambillau [France] ; Mariana Piuri [Argentine]Source :
- Applied Microbiology and Biotechnology [ 0175-7598 ] ; 2016-07-23.
English descriptors
Abstract
Lactic acid bacteria (LAB) have many applications in food and industrial fermentations. Prophage induction and generation of new virulent phages is a risk for the dairy industry. We identified three complete prophages (PLE1, PLE2, and PLE3) in the genome of the well-studied probiotic strain Lactobacillus casei BL23. All of them have mosaic architectures with homologous sequences to Streptococcus, Lactococcus, Lactobacillus, and Listeria phages or strains. Using a combination of quantitative real-time PCR, genomics, and proteomics, we showed that PLE2 and PLE3 can be induced-but with different kinetics-in the presence of mitomycin C, although PLE1 remains as a prophage. A structural analysis of the distal tail (Dit) and tail associated lysin (Tal) baseplate proteins of these prophages and other L. casei/paracasei phages and prophages provides evidence that carbohydrate-binding modules (CBM) located within these "evolved" proteins may replace receptor binding proteins (RBPs) present in other well-studied LAB phages. The detailed study of prophage induction in this prototype strain in combination with characterization of the proteins involved in host recognition will facilitate the design of new strategies for avoiding phage propagation in the dairy industry.
Url:
DOI: 10.1007/s00253-016-7727-x
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Hal:pasteur-01498340Le document en format XML
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<country>États-Unis</country>
<placeName><settlement type="city">Pittsburgh</settlement>
<region type="state">Pennsylvanie</region>
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<orgName type="university">Université de Pittsburgh</orgName>
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<author><name sortKey="Russell, Daniel" sort="Russell, Daniel" uniqKey="Russell D" first="Daniel" last="Russell">Daniel Russell</name>
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<desc><address><addrLine>Department of Biological Sciences,Pittsburgh, PA 15260</addrLine>
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<country>États-Unis</country>
<placeName><settlement type="city">Pittsburgh</settlement>
<region type="state">Pennsylvanie</region>
</placeName>
<orgName type="university">Université de Pittsburgh</orgName>
</affiliation>
</author>
<author><name sortKey="Hatfull, Graham F" sort="Hatfull, Graham F" uniqKey="Hatfull G" first="Graham F" last="Hatfull">Graham F. Hatfull</name>
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<desc><address><addrLine>Department of Biological Sciences,Pittsburgh, PA 15260</addrLine>
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<country>États-Unis</country>
<placeName><settlement type="city">Pittsburgh</settlement>
<region type="state">Pennsylvanie</region>
</placeName>
<orgName type="university">Université de Pittsburgh</orgName>
</affiliation>
</author>
<author><name sortKey="Cambillau, Christian" sort="Cambillau, Christian" uniqKey="Cambillau C" first="Christian" last="Cambillau">Christian Cambillau</name>
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<orgName>Architecture et fonction des macromolécules biologiques</orgName>
<orgName type="acronym">AFMB</orgName>
<date type="start">2012</date>
<desc><address><addrLine>Faculté des Sciences de Luminy - Case 932 163, Avenue de Luminy13288 Marseille Cedex 09</addrLine>
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</address>
<ref type="url">http://www.afmb.univ-mrs.fr/</ref>
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<country>France</country>
<placeName><settlement type="city">Marseille</settlement>
<region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region>
</placeName>
<orgName type="university">Université d'Aix-Marseille</orgName>
</affiliation>
</author>
<author><name sortKey="Piuri, Mariana" sort="Piuri, Mariana" uniqKey="Piuri M" first="Mariana" last="Piuri">Mariana Piuri</name>
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<orgName type="acronym">IQUIBICEN-CONICE</orgName>
<desc><address><addrLine>Facultad de Ciencias Exactas y Naturales - Intendente Guiraldes 2160, C1428EGA Buenos Aire</addrLine>
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</address>
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<desc><address><addrLine>Viamonte 430/44 C1053ABJ, Ciudad de Buenos Aires</addrLine>
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<ref type="url">http://www.uba.ar/</ref>
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<country>Argentine</country>
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<idno type="DOI">10.1007/s00253-016-7727-x</idno>
<series><title level="j">Applied Microbiology and Biotechnology</title>
<idno type="ISSN">0175-7598</idno>
<imprint><date type="datePub">2016-07-23</date>
</imprint>
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<profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term>Bacteriophage</term>
<term>Baseplate</term>
<term>Lactobacillus casei</term>
<term>Prophage</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Lactic acid bacteria (LAB) have many applications in food and industrial fermentations. Prophage induction and generation of new virulent phages is a risk for the dairy industry. We identified three complete prophages (PLE1, PLE2, and PLE3) in the genome of the well-studied probiotic strain Lactobacillus casei BL23. All of them have mosaic architectures with homologous sequences to Streptococcus, Lactococcus, Lactobacillus, and Listeria phages or strains. Using a combination of quantitative real-time PCR, genomics, and proteomics, we showed that PLE2 and PLE3 can be induced-but with different kinetics-in the presence of mitomycin C, although PLE1 remains as a prophage. A structural analysis of the distal tail (Dit) and tail associated lysin (Tal) baseplate proteins of these prophages and other L. casei/paracasei phages and prophages provides evidence that carbohydrate-binding modules (CBM) located within these "evolved" proteins may replace receptor binding proteins (RBPs) present in other well-studied LAB phages. The detailed study of prophage induction in this prototype strain in combination with characterization of the proteins involved in host recognition will facilitate the design of new strategies for avoiding phage propagation in the dairy industry.</div>
</front>
</TEI>
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