Heterogeneity of S-layer proteins from aggregating and non-aggregating <i>Lactobacillus kefir</i> strains

Autores
Mobili, Pablo; Serradell, María de los Ángeles; Trejo, Sebastián Alejandro; Avilés Puigvert, Francesc Xavier; Abraham, Analía Graciela; De Antoni, Graciela Liliana
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Since the presence of S-layer protein conditioned the autoaggregation capacity of some strains of Lactobacillus kefir, S-layer proteins from aggregating and non-aggregating L. kefir strains were characterized by immunochemical reactivity, MALDI-TOF spectrometry and glycosylation analysis. Two anti-S-layer monoclonal antibodies (Mab5F8 and Mab1F8) were produced; in an indirect enzyme-linked immunosorbent assay Mab1F8 recognized S-layer proteins from all L. kefir tested while Mab5F8 recognized only S-layer proteins from aggregating strains. Periodic Acid-Schiff staining of proteins after polyacrylamide gel electrophoresis under denaturing conditions revealed that all L. kefir S-layer proteins tested were glycosylated. Growth of bacteria in the presence of the N-glycosylation inhibitor tunicamycin suggested the presence of glycosydic chains O-linked to the protein backbone. MALDI-TOF peptide map fingerprint for S-layer proteins from 12 L. kefir strains showed very similar patterns for the aggregating strains, different from those for the non-aggregating ones. No positive match with other protein spectra in MSDB Database was found. Our results revealed a high heterogeneity among S-layer proteins from different L. kefir strains but also suggested a correlation between the structure of these S-layer glycoproteins and the aggregation properties of whole bacterial cells.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Materia
Ciencias Exactas
Química
Glycosylation
Immunochemistry
Lactobacillus kefir
S-layer
Spectrometry
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/144625

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oai_identifier_str oai:sedici.unlp.edu.ar:10915/144625
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network_name_str SEDICI (UNLP)
spelling Heterogeneity of S-layer proteins from aggregating and non-aggregating <i>Lactobacillus kefir</i> strainsMobili, PabloSerradell, María de los ÁngelesTrejo, Sebastián AlejandroAvilés Puigvert, Francesc XavierAbraham, Analía GracielaDe Antoni, Graciela LilianaCiencias ExactasQuímicaGlycosylationImmunochemistryLactobacillus kefirS-layerSpectrometrySince the presence of S-layer protein conditioned the autoaggregation capacity of some strains of <i>Lactobacillus kefir</i>, S-layer proteins from aggregating and non-aggregating <i>L. kefir</i> strains were characterized by immunochemical reactivity, MALDI-TOF spectrometry and glycosylation analysis. Two anti-S-layer monoclonal antibodies (Mab5F8 and Mab1F8) were produced; in an indirect enzyme-linked immunosorbent assay Mab1F8 recognized S-layer proteins from all <i>L. kefir</i> tested while Mab5F8 recognized only S-layer proteins from aggregating strains. Periodic Acid-Schiff staining of proteins after polyacrylamide gel electrophoresis under denaturing conditions revealed that all <i>L. kefir</i> S-layer proteins tested were glycosylated. Growth of bacteria in the presence of the N-glycosylation inhibitor tunicamycin suggested the presence of glycosydic chains O-linked to the protein backbone. MALDI-TOF peptide map fingerprint for S-layer proteins from 12 <i>L. kefir</i> strains showed very similar patterns for the aggregating strains, different from those for the non-aggregating ones. No positive match with other protein spectra in MSDB Database was found. Our results revealed a high heterogeneity among S-layer proteins from different <i>L. kefir</i> strains but also suggested a correlation between the structure of these S-layer glycoproteins and the aggregation properties of whole bacterial cells.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2009-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf363-372http://sedici.unlp.edu.ar/handle/10915/144625enginfo:eu-repo/semantics/altIdentifier/issn/1572-9699info:eu-repo/semantics/altIdentifier/issn/0003-6072info:eu-repo/semantics/altIdentifier/doi/10.1007/s10482-009-9322-yinfo:eu-repo/semantics/altIdentifier/pmid/19306111info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T11:04:29Zoai:sedici.unlp.edu.ar:10915/144625Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:04:29.359SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Heterogeneity of S-layer proteins from aggregating and non-aggregating <i>Lactobacillus kefir</i> strains
title Heterogeneity of S-layer proteins from aggregating and non-aggregating <i>Lactobacillus kefir</i> strains
spellingShingle Heterogeneity of S-layer proteins from aggregating and non-aggregating <i>Lactobacillus kefir</i> strains
Mobili, Pablo
Ciencias Exactas
Química
Glycosylation
Immunochemistry
Lactobacillus kefir
S-layer
Spectrometry
title_short Heterogeneity of S-layer proteins from aggregating and non-aggregating <i>Lactobacillus kefir</i> strains
title_full Heterogeneity of S-layer proteins from aggregating and non-aggregating <i>Lactobacillus kefir</i> strains
title_fullStr Heterogeneity of S-layer proteins from aggregating and non-aggregating <i>Lactobacillus kefir</i> strains
title_full_unstemmed Heterogeneity of S-layer proteins from aggregating and non-aggregating <i>Lactobacillus kefir</i> strains
title_sort Heterogeneity of S-layer proteins from aggregating and non-aggregating <i>Lactobacillus kefir</i> strains
dc.creator.none.fl_str_mv Mobili, Pablo
Serradell, María de los Ángeles
Trejo, Sebastián Alejandro
Avilés Puigvert, Francesc Xavier
Abraham, Analía Graciela
De Antoni, Graciela Liliana
author Mobili, Pablo
author_facet Mobili, Pablo
Serradell, María de los Ángeles
Trejo, Sebastián Alejandro
Avilés Puigvert, Francesc Xavier
Abraham, Analía Graciela
De Antoni, Graciela Liliana
author_role author
author2 Serradell, María de los Ángeles
Trejo, Sebastián Alejandro
Avilés Puigvert, Francesc Xavier
Abraham, Analía Graciela
De Antoni, Graciela Liliana
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Química
Glycosylation
Immunochemistry
Lactobacillus kefir
S-layer
Spectrometry
topic Ciencias Exactas
Química
Glycosylation
Immunochemistry
Lactobacillus kefir
S-layer
Spectrometry
dc.description.none.fl_txt_mv Since the presence of S-layer protein conditioned the autoaggregation capacity of some strains of <i>Lactobacillus kefir</i>, S-layer proteins from aggregating and non-aggregating <i>L. kefir</i> strains were characterized by immunochemical reactivity, MALDI-TOF spectrometry and glycosylation analysis. Two anti-S-layer monoclonal antibodies (Mab5F8 and Mab1F8) were produced; in an indirect enzyme-linked immunosorbent assay Mab1F8 recognized S-layer proteins from all <i>L. kefir</i> tested while Mab5F8 recognized only S-layer proteins from aggregating strains. Periodic Acid-Schiff staining of proteins after polyacrylamide gel electrophoresis under denaturing conditions revealed that all <i>L. kefir</i> S-layer proteins tested were glycosylated. Growth of bacteria in the presence of the N-glycosylation inhibitor tunicamycin suggested the presence of glycosydic chains O-linked to the protein backbone. MALDI-TOF peptide map fingerprint for S-layer proteins from 12 <i>L. kefir</i> strains showed very similar patterns for the aggregating strains, different from those for the non-aggregating ones. No positive match with other protein spectra in MSDB Database was found. Our results revealed a high heterogeneity among S-layer proteins from different <i>L. kefir</i> strains but also suggested a correlation between the structure of these S-layer glycoproteins and the aggregation properties of whole bacterial cells.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
description Since the presence of S-layer protein conditioned the autoaggregation capacity of some strains of <i>Lactobacillus kefir</i>, S-layer proteins from aggregating and non-aggregating <i>L. kefir</i> strains were characterized by immunochemical reactivity, MALDI-TOF spectrometry and glycosylation analysis. Two anti-S-layer monoclonal antibodies (Mab5F8 and Mab1F8) were produced; in an indirect enzyme-linked immunosorbent assay Mab1F8 recognized S-layer proteins from all <i>L. kefir</i> tested while Mab5F8 recognized only S-layer proteins from aggregating strains. Periodic Acid-Schiff staining of proteins after polyacrylamide gel electrophoresis under denaturing conditions revealed that all <i>L. kefir</i> S-layer proteins tested were glycosylated. Growth of bacteria in the presence of the N-glycosylation inhibitor tunicamycin suggested the presence of glycosydic chains O-linked to the protein backbone. MALDI-TOF peptide map fingerprint for S-layer proteins from 12 <i>L. kefir</i> strains showed very similar patterns for the aggregating strains, different from those for the non-aggregating ones. No positive match with other protein spectra in MSDB Database was found. Our results revealed a high heterogeneity among S-layer proteins from different <i>L. kefir</i> strains but also suggested a correlation between the structure of these S-layer glycoproteins and the aggregation properties of whole bacterial cells.
publishDate 2009
dc.date.none.fl_str_mv 2009-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/144625
url http://sedici.unlp.edu.ar/handle/10915/144625
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1572-9699
info:eu-repo/semantics/altIdentifier/issn/0003-6072
info:eu-repo/semantics/altIdentifier/doi/10.1007/s10482-009-9322-y
info:eu-repo/semantics/altIdentifier/pmid/19306111
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
363-372
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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