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dc.contributor.author
Palomino, Maria Mercedes
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dc.contributor.author
Allievi, Mariana Claudia
dc.contributor.author
Gründling, Angelika
dc.contributor.author
Sanchez, Carmen
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dc.contributor.author
Ruzal, Sandra Monica
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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
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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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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
Biología Celular, Microbiología
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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
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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
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1099/mic.0.070607-0
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