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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/144625
Ver los metadatos del registro completo
id |
SEDICI_092b7e573cc5070842e36e3b2800d425 |
---|---|
oai_identifier_str |
oai:sedici.unlp.edu.ar:10915/144625 |
network_acronym_str |
SEDICI |
repository_id_str |
1329 |
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 |
repository.mail.fl_str_mv |
alira@sedici.unlp.edu.ar |
_version_ |
1842260543825510400 |
score |
13.13397 |