<i>Lactobacillus kefiri</i> shows inter-strain variations in the amino acid sequence of the S-layer proteins
- Autores
- Malamud, Mariano; Carasi, Paula; Bronsoms, Sílvia; Trejo, Sebastián Alejandro; Serradell, María de los Ángeles
- Año de publicación
- 2017
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The S-layer is a proteinaceous envelope constituted by subunits that self-assemble to form a two-dimensional lattice that covers the surface of different species of Bacteria and Archaea, and it could be involved in cell recognition of microbes among other several distinct functions. In this work, both proteomic and genomic approaches were used to gain knowledge about the sequences of the S-layer protein (SLPs) encoding genes expressed by six aggregative and sixteen non-aggregative strains of potentially probiotic Lactobacillus kefiri Peptide mass fingerprint (PMF) analysis confirmed the identity of SLPs extracted from L. kefiri, and based on the homology with phylogenetically related species, primers located outside and inside the SLP-genes were employed to amplify genomic DNA. The O-glycosylation site SASSAS was found in all L. kefiri SLPs. Ten strains were selected for sequencing of the complete genes. The total length of the mature proteins varies from 492 to 576 amino acids, and all SLPs have a calculated pI between 9.37 and 9.60. The N-terminal region is relatively conserved and shows a high percentage of positively charged amino acids. Major differences among strains are found in the C-terminal region. Different groups could be distinguished regarding the mature SLPs and the similarities observed in the PMF spectra. Interestingly, SLPs of the aggregative strains are 100% homologous, although these strains were isolated from different kefir grains. This knowledge provides relevant data for better understanding of the mechanisms involved in SLPs functionality and could contribute to the development of products of biotechnological interest from potentially probiotic bacteria.
Facultad de Ciencias Exactas
Instituto Multidisciplinario de Biología Celular - Materia
-
Biología
Lactobacillus kefiri
Surface properties
Glycoproteins
S-layer proteins - 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:10915/133566
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<i>Lactobacillus kefiri</i> shows inter-strain variations in the amino acid sequence of the S-layer proteinsMalamud, MarianoCarasi, PaulaBronsoms, SílviaTrejo, Sebastián AlejandroSerradell, María de los ÁngelesBiologíaLactobacillus kefiriSurface propertiesGlycoproteinsS-layer proteinsThe S-layer is a proteinaceous envelope constituted by subunits that self-assemble to form a two-dimensional lattice that covers the surface of different species of <i>Bacteria</i> and <i>Archaea</i>, and it could be involved in cell recognition of microbes among other several distinct functions. In this work, both proteomic and genomic approaches were used to gain knowledge about the sequences of the S-layer protein (SLPs) encoding genes expressed by six aggregative and sixteen non-aggregative strains of potentially probiotic <i>Lactobacillus kefiri</i> Peptide mass fingerprint (PMF) analysis confirmed the identity of SLPs extracted from <i>L. kefiri</i>, and based on the homology with phylogenetically related species, primers located outside and inside the SLP-genes were employed to amplify genomic DNA. The O-glycosylation site SASSAS was found in all <i>L. kefiri</i> SLPs. Ten strains were selected for sequencing of the complete genes. The total length of the mature proteins varies from 492 to 576 amino acids, and all SLPs have a calculated pI between 9.37 and 9.60. The N-terminal region is relatively conserved and shows a high percentage of positively charged amino acids. Major differences among strains are found in the C-terminal region. Different groups could be distinguished regarding the mature SLPs and the similarities observed in the PMF spectra. Interestingly, SLPs of the aggregative strains are 100% homologous, although these strains were isolated from different kefir grains. This knowledge provides relevant data for better understanding of the mechanisms involved in SLPs functionality and could contribute to the development of products of biotechnological interest from potentially probiotic bacteria.Facultad de Ciencias ExactasInstituto Multidisciplinario de Biología Celular2017-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf515-530http://sedici.unlp.edu.ar/handle/10915/133566enginfo:eu-repo/semantics/altIdentifier/issn/1572-9699info:eu-repo/semantics/altIdentifier/issn/0003-6072info:eu-repo/semantics/altIdentifier/doi/10.1007/s10482-016-0820-4info:eu-repo/semantics/altIdentifier/pmid/28004217info: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:UNLP2025-09-29T11:31:53Zoai:sedici.unlp.edu.ar:10915/133566Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:31:53.292SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
<i>Lactobacillus kefiri</i> shows inter-strain variations in the amino acid sequence of the S-layer proteins |
title |
<i>Lactobacillus kefiri</i> shows inter-strain variations in the amino acid sequence of the S-layer proteins |
spellingShingle |
<i>Lactobacillus kefiri</i> shows inter-strain variations in the amino acid sequence of the S-layer proteins Malamud, Mariano Biología Lactobacillus kefiri Surface properties Glycoproteins S-layer proteins |
title_short |
<i>Lactobacillus kefiri</i> shows inter-strain variations in the amino acid sequence of the S-layer proteins |
title_full |
<i>Lactobacillus kefiri</i> shows inter-strain variations in the amino acid sequence of the S-layer proteins |
title_fullStr |
<i>Lactobacillus kefiri</i> shows inter-strain variations in the amino acid sequence of the S-layer proteins |
title_full_unstemmed |
<i>Lactobacillus kefiri</i> shows inter-strain variations in the amino acid sequence of the S-layer proteins |
title_sort |
<i>Lactobacillus kefiri</i> shows inter-strain variations in the amino acid sequence of the S-layer proteins |
dc.creator.none.fl_str_mv |
Malamud, Mariano Carasi, Paula Bronsoms, Sílvia Trejo, Sebastián Alejandro Serradell, María de los Ángeles |
author |
Malamud, Mariano |
author_facet |
Malamud, Mariano Carasi, Paula Bronsoms, Sílvia Trejo, Sebastián Alejandro Serradell, María de los Ángeles |
author_role |
author |
author2 |
Carasi, Paula Bronsoms, Sílvia Trejo, Sebastián Alejandro Serradell, María de los Ángeles |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Biología Lactobacillus kefiri Surface properties Glycoproteins S-layer proteins |
topic |
Biología Lactobacillus kefiri Surface properties Glycoproteins S-layer proteins |
dc.description.none.fl_txt_mv |
The S-layer is a proteinaceous envelope constituted by subunits that self-assemble to form a two-dimensional lattice that covers the surface of different species of <i>Bacteria</i> and <i>Archaea</i>, and it could be involved in cell recognition of microbes among other several distinct functions. In this work, both proteomic and genomic approaches were used to gain knowledge about the sequences of the S-layer protein (SLPs) encoding genes expressed by six aggregative and sixteen non-aggregative strains of potentially probiotic <i>Lactobacillus kefiri</i> Peptide mass fingerprint (PMF) analysis confirmed the identity of SLPs extracted from <i>L. kefiri</i>, and based on the homology with phylogenetically related species, primers located outside and inside the SLP-genes were employed to amplify genomic DNA. The O-glycosylation site SASSAS was found in all <i>L. kefiri</i> SLPs. Ten strains were selected for sequencing of the complete genes. The total length of the mature proteins varies from 492 to 576 amino acids, and all SLPs have a calculated pI between 9.37 and 9.60. The N-terminal region is relatively conserved and shows a high percentage of positively charged amino acids. Major differences among strains are found in the C-terminal region. Different groups could be distinguished regarding the mature SLPs and the similarities observed in the PMF spectra. Interestingly, SLPs of the aggregative strains are 100% homologous, although these strains were isolated from different kefir grains. This knowledge provides relevant data for better understanding of the mechanisms involved in SLPs functionality and could contribute to the development of products of biotechnological interest from potentially probiotic bacteria. Facultad de Ciencias Exactas Instituto Multidisciplinario de Biología Celular |
description |
The S-layer is a proteinaceous envelope constituted by subunits that self-assemble to form a two-dimensional lattice that covers the surface of different species of <i>Bacteria</i> and <i>Archaea</i>, and it could be involved in cell recognition of microbes among other several distinct functions. In this work, both proteomic and genomic approaches were used to gain knowledge about the sequences of the S-layer protein (SLPs) encoding genes expressed by six aggregative and sixteen non-aggregative strains of potentially probiotic <i>Lactobacillus kefiri</i> Peptide mass fingerprint (PMF) analysis confirmed the identity of SLPs extracted from <i>L. kefiri</i>, and based on the homology with phylogenetically related species, primers located outside and inside the SLP-genes were employed to amplify genomic DNA. The O-glycosylation site SASSAS was found in all <i>L. kefiri</i> SLPs. Ten strains were selected for sequencing of the complete genes. The total length of the mature proteins varies from 492 to 576 amino acids, and all SLPs have a calculated pI between 9.37 and 9.60. The N-terminal region is relatively conserved and shows a high percentage of positively charged amino acids. Major differences among strains are found in the C-terminal region. Different groups could be distinguished regarding the mature SLPs and the similarities observed in the PMF spectra. Interestingly, SLPs of the aggregative strains are 100% homologous, although these strains were isolated from different kefir grains. This knowledge provides relevant data for better understanding of the mechanisms involved in SLPs functionality and could contribute to the development of products of biotechnological interest from potentially probiotic bacteria. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-04 |
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 |
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publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/133566 |
url |
http://sedici.unlp.edu.ar/handle/10915/133566 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
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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) |
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openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
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