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dc.contributor.author
Palomino, Maria Mercedes  
dc.contributor.author
Allievi, Mariana Claudia  
dc.contributor.author
Gründling, Angelika  
dc.contributor.author
Sanchez, Carmen  
dc.contributor.author
Ruzal, Sandra Monica  
dc.date.available
2015-06-16T20:03:03Z  
dc.date.issued
2013-11  
dc.identifier.citation
Palomino, Maria Mercedes; Allievi, Mariana Claudia; Gründling, Angelika; Sanchez, Carmen; Ruzal, Sandra Monica; Lipoteichoic acid (LTA) modifications during osmotic stress adaptation in Lactobacillus casei BL23.; Maik Nauka/interperiodica/springer; Microbiology; 159; 11-2013; 2416-2426  
dc.identifier.issn
0026-2617  
dc.identifier.uri
http://hdl.handle.net/11336/769  
dc.description.abstract
The probiotic Gram-positive bacterium Lactobacillus casei BL23 is naturally confronted with salt- stress habitats. It has been previously reported that growth in high-salt medium, containing 0.8 M NaCl, leads to modifications in the cell envelope of this bacterium. In this study, we report that L. casei BL23 has an increased ability to form biofilms and to bind cations in high-salt conditions. This behaviour correlated with modifications of surface properties involving teichoic acids, which are important cell wall components. We also showed that, in these high-salt conditions, L. casei BL23 produces less of the cell wall polymer lipoteichoic acid (LTA), and that this anionic polymer has a shorter mean chain length and a lower level of D-alanyl-substitution. Analysis of the transcript levels of the dltABCD operon, encoding the enzymes required for the incorporation of D-alanine into anionic polymers, showed a 16-fold reduction in mRNA levels, which is consistent with a decrease in D-alanine substitutions on LTA. Furthermore, a 13-fold reduction in the transcript levels was observed for the gene LCABL_09330 coding for a putative LTA synthase. To provide further experimental evidence that LCABL_09330 is a true LTA synthase (LtaS) in L. casei BL23, the enzymic domain was cloned and expressed in E. coli. The purified protein was able to hydrolyse the membrane lipid phosphatidylglycerol as expected for an LTA synthase enzyme, and hence LCABL_09330 was renamed LtaS. The purified enzyme showed Mn2+-ion dependent activity, and its activity was modulated by differences in NaCl concentration. The decrease in both ltaS transcript levels and enzyme activity observed in high-salt conditions might influence the length of the LTA backbone chain. A putative function of the modified LTA structure is discussed that is compatible with the growth under salt-stress conditions and with the overall envelope modifications taking place during this stress condition.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Maik Nauka/interperiodica/springer  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Lactobacillus  
dc.subject
Lta  
dc.subject
Osmotic Stress  
dc.subject.classification
Ciencias Naturales y Exactas  
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Ciencias Biológicas  
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Biología Celular, Microbiología  
dc.title
Lipoteichoic acid (LTA) modifications during osmotic stress adaptation in Lactobacillus casei BL23.  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2016-03-30 10:35:44.97925-03  
dc.journal.volume
159  
dc.journal.pagination
2416-2426  
dc.journal.pais
Reino Unido  
dc.journal.ciudad
Kiev  
dc.description.fil
Fil: Palomino, Maria Mercedes. Consejo Nacional de Invest.cientif.y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Instituto de Quimica Biologica de la Facultad de Cs. Exactas y Naturales; Argentina;  
dc.description.fil
Fil: Allievi, Mariana Claudia. Consejo Nacional de Invest.cientif.y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Instituto de Quimica Biologica de la Facultad de Cs. Exactas y Naturales; Argentina;  
dc.description.fil
Fil: Gründling, Angelika. Imperial College Of Science And Technology; Reino Unido;  
dc.description.fil
Fil: Sanchez, Carmen. Consejo Nacional de Invest.cientif.y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Instituto de Quimica Biologica de la Facultad de Cs. Exactas y Naturales; Argentina;  
dc.description.fil
Fil: Ruzal, Sandra Monica. Consejo Nacional de Invest.cientif.y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Instituto de Quimica Biologica de la Facultad de Cs. Exactas y Naturales; Argentina;  
dc.journal.title
Microbiology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1099/mic.0.070607-0