Cell wall modifications during osmotic stress in Lactobacillus casei

Autores
Piuri, Mariana; Sanchez, Carmen; Ruzal, Sandra Mónica
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Aims: To study the modification of the cell wall of Lactobacillus casei ATCC 393 grown in high salt conditions. Methods and Results: Differences in the overall structure of cell wall between growth in high salt (MRS + 1 mol l -1 NaCl; N condition) and control (MRS; C condition) conditions were determined by transmission electronic microscopy and analytical procedures. Lactobacillus casei cells grown in N condition were significantly larger than cells grown under unstressed C condition. Increased sensitivity to mutanolysin and antibiotics with target in the cell wall was observed in N condition. Purified cell wall also showed the increased sensitivity to lysis by mutanolysin. Analysis of peptidoglycan (PG) from stressed cells showed that modification was at the structural level in accordance with a decreased PG cross-link involving penicillin-binding proteins (PBP). Nine PBP were first described in this species and these proteins were expressed in low percentages or presented a modified pattern of saturation with penicillin G (Pen G) during growth in high salt. Three of the essential PBP were fully saturated in N condition at lower Pen G concentrations than in C condition, suggesting differences in functionality in vivo. Conclusions: The results show that growth in high salt modified the structural properties of the cell wall. Significance and Impact of Study: Advances in understanding the adaptation to high osmolarity, in particular those involving sensitivity to lysis of lactic acid bacteria.
Fil: Piuri, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Sanchez, Carmen. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Ruzal, Sandra Mónica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Materia
LACTOBACILLUS CASEI
OSMOTIC STRESS
PBP
PEPTIDOGLYCAN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/98637

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spelling Cell wall modifications during osmotic stress in Lactobacillus caseiPiuri, MarianaSanchez, CarmenRuzal, Sandra MónicaLACTOBACILLUS CASEIOSMOTIC STRESSPBPPEPTIDOGLYCANAims: To study the modification of the cell wall of Lactobacillus casei ATCC 393 grown in high salt conditions. Methods and Results: Differences in the overall structure of cell wall between growth in high salt (MRS + 1 mol l -1 NaCl; N condition) and control (MRS; C condition) conditions were determined by transmission electronic microscopy and analytical procedures. Lactobacillus casei cells grown in N condition were significantly larger than cells grown under unstressed C condition. Increased sensitivity to mutanolysin and antibiotics with target in the cell wall was observed in N condition. Purified cell wall also showed the increased sensitivity to lysis by mutanolysin. Analysis of peptidoglycan (PG) from stressed cells showed that modification was at the structural level in accordance with a decreased PG cross-link involving penicillin-binding proteins (PBP). Nine PBP were first described in this species and these proteins were expressed in low percentages or presented a modified pattern of saturation with penicillin G (Pen G) during growth in high salt. Three of the essential PBP were fully saturated in N condition at lower Pen G concentrations than in C condition, suggesting differences in functionality in vivo. Conclusions: The results show that growth in high salt modified the structural properties of the cell wall. Significance and Impact of Study: Advances in understanding the adaptation to high osmolarity, in particular those involving sensitivity to lysis of lactic acid bacteria.Fil: Piuri, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Sanchez, Carmen. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Ruzal, Sandra Mónica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaWiley Blackwell Publishing, Inc2005-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/98637Piuri, Mariana; Sanchez, Carmen; Ruzal, Sandra Mónica; Cell wall modifications during osmotic stress in Lactobacillus casei; Wiley Blackwell Publishing, Inc; Journal of Applied Microbiology; 98; 1; 12-2005; 84-951364-5072CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://sfamjournals.onlinelibrary.wiley.com/doi/full/10.1111/j.1365-2672.2004.02428.xinfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2672.2004.02428.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:42:14Zoai:ri.conicet.gov.ar:11336/98637instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:42:14.952CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Cell wall modifications during osmotic stress in Lactobacillus casei
title Cell wall modifications during osmotic stress in Lactobacillus casei
spellingShingle Cell wall modifications during osmotic stress in Lactobacillus casei
Piuri, Mariana
LACTOBACILLUS CASEI
OSMOTIC STRESS
PBP
PEPTIDOGLYCAN
title_short Cell wall modifications during osmotic stress in Lactobacillus casei
title_full Cell wall modifications during osmotic stress in Lactobacillus casei
title_fullStr Cell wall modifications during osmotic stress in Lactobacillus casei
title_full_unstemmed Cell wall modifications during osmotic stress in Lactobacillus casei
title_sort Cell wall modifications during osmotic stress in Lactobacillus casei
dc.creator.none.fl_str_mv Piuri, Mariana
Sanchez, Carmen
Ruzal, Sandra Mónica
author Piuri, Mariana
author_facet Piuri, Mariana
Sanchez, Carmen
Ruzal, Sandra Mónica
author_role author
author2 Sanchez, Carmen
Ruzal, Sandra Mónica
author2_role author
author
dc.subject.none.fl_str_mv LACTOBACILLUS CASEI
OSMOTIC STRESS
PBP
PEPTIDOGLYCAN
topic LACTOBACILLUS CASEI
OSMOTIC STRESS
PBP
PEPTIDOGLYCAN
dc.description.none.fl_txt_mv Aims: To study the modification of the cell wall of Lactobacillus casei ATCC 393 grown in high salt conditions. Methods and Results: Differences in the overall structure of cell wall between growth in high salt (MRS + 1 mol l -1 NaCl; N condition) and control (MRS; C condition) conditions were determined by transmission electronic microscopy and analytical procedures. Lactobacillus casei cells grown in N condition were significantly larger than cells grown under unstressed C condition. Increased sensitivity to mutanolysin and antibiotics with target in the cell wall was observed in N condition. Purified cell wall also showed the increased sensitivity to lysis by mutanolysin. Analysis of peptidoglycan (PG) from stressed cells showed that modification was at the structural level in accordance with a decreased PG cross-link involving penicillin-binding proteins (PBP). Nine PBP were first described in this species and these proteins were expressed in low percentages or presented a modified pattern of saturation with penicillin G (Pen G) during growth in high salt. Three of the essential PBP were fully saturated in N condition at lower Pen G concentrations than in C condition, suggesting differences in functionality in vivo. Conclusions: The results show that growth in high salt modified the structural properties of the cell wall. Significance and Impact of Study: Advances in understanding the adaptation to high osmolarity, in particular those involving sensitivity to lysis of lactic acid bacteria.
Fil: Piuri, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Sanchez, Carmen. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Ruzal, Sandra Mónica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
description Aims: To study the modification of the cell wall of Lactobacillus casei ATCC 393 grown in high salt conditions. Methods and Results: Differences in the overall structure of cell wall between growth in high salt (MRS + 1 mol l -1 NaCl; N condition) and control (MRS; C condition) conditions were determined by transmission electronic microscopy and analytical procedures. Lactobacillus casei cells grown in N condition were significantly larger than cells grown under unstressed C condition. Increased sensitivity to mutanolysin and antibiotics with target in the cell wall was observed in N condition. Purified cell wall also showed the increased sensitivity to lysis by mutanolysin. Analysis of peptidoglycan (PG) from stressed cells showed that modification was at the structural level in accordance with a decreased PG cross-link involving penicillin-binding proteins (PBP). Nine PBP were first described in this species and these proteins were expressed in low percentages or presented a modified pattern of saturation with penicillin G (Pen G) during growth in high salt. Three of the essential PBP were fully saturated in N condition at lower Pen G concentrations than in C condition, suggesting differences in functionality in vivo. Conclusions: The results show that growth in high salt modified the structural properties of the cell wall. Significance and Impact of Study: Advances in understanding the adaptation to high osmolarity, in particular those involving sensitivity to lysis of lactic acid bacteria.
publishDate 2005
dc.date.none.fl_str_mv 2005-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/98637
Piuri, Mariana; Sanchez, Carmen; Ruzal, Sandra Mónica; Cell wall modifications during osmotic stress in Lactobacillus casei; Wiley Blackwell Publishing, Inc; Journal of Applied Microbiology; 98; 1; 12-2005; 84-95
1364-5072
CONICET Digital
CONICET
url http://hdl.handle.net/11336/98637
identifier_str_mv Piuri, Mariana; Sanchez, Carmen; Ruzal, Sandra Mónica; Cell wall modifications during osmotic stress in Lactobacillus casei; Wiley Blackwell Publishing, Inc; Journal of Applied Microbiology; 98; 1; 12-2005; 84-95
1364-5072
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2672.2004.02428.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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application/pdf
application/pdf
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dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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