Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners
- Autores
- Malamud, Mariano; Cavallero, Gustavo Javier; Casabuono, Adriana Cristina; Lepenies, Bernd; Serradell, María de los Ángeles; Couto, Alicia Susana
- Año de publicación
- 2020
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- S-layer (glyco)-proteins (SLPs) form a nanostructured envelope that covers the surface of different prokaryotes and show immunomodulatory activity. Previously, we have demonstrated that the S-layer glycoprotein from probiotic Lactobacillus kefiri CIDCA 8348 (SLP-8348) is recognized by Mincle (macrophage inducible C-type lectin receptor) and its adjuvanticity depends on the integrity of its glycans. However, the glycan´s structure has not been described so far. Herein, we analyze the glycosylation pattern of three SLPs, SLP-8348, SLP-8321, and SLP-5818, and explore how these patterns impacts their recognition by Ctype lectin receptors (CLRs) and the immunomodulatory effect of the L. kefiri SLPs on antigen-presenting cells. HPAEC-PAD performed after β-elimination showed glucose as the major component in the O-glycans of the three SLPs, however, some differences in the length of hexose chains were observed. No N-glycosylation signals were detected in SLP-8348 and SLP-8321, but SLP5818 was observed to have two sites carrying complex N-glycans based on a site-specific analysis and a glycomic workflow of the permethylated glycans. SLP-8348 was previously shown to enhance LPS-induced activation on both RAW264.7 macrophages and murine BMDCs; we now show SLP-8321 and SLP-5818 have a similar effect regardless of the differences in their glycosylation patterns. Studies performed with BMDCs from CLR-deficient mice revealed that the immunostimulatory activity of SLP-8321 depends on its recognition by Mincle, whereas SLP-5818’s effects are dependent on SignR3 (murine ortholog of human DC-SIGN). These findings encourage further investigation of both the potential application of these SLPs as new adjuvants and the protein glycosylation mechanisms in these bacteria.
Fil: Malamud, Mariano. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Cátedra de Microbiología General; Argentina. University of Veterinary Medicine Hannover; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Cavallero, Gustavo Javier. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono | Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono; Argentina
Fil: Casabuono, Adriana Cristina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono | Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono; Argentina
Fil: Lepenies, Bernd. University of Veterinary Medicine Hannover; Alemania
Fil: Serradell, María de los Ángeles. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Cátedra de Microbiología General; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Couto, Alicia Susana. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono | Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono; Argentina - Materia
-
LACTOBACILLUS KEFIRI
S-LAYER PROTEINS
GLYCOSYLATION - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/140048
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Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partnersMalamud, MarianoCavallero, Gustavo JavierCasabuono, Adriana CristinaLepenies, BerndSerradell, María de los ÁngelesCouto, Alicia SusanaLACTOBACILLUS KEFIRIS-LAYER PROTEINSGLYCOSYLATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1S-layer (glyco)-proteins (SLPs) form a nanostructured envelope that covers the surface of different prokaryotes and show immunomodulatory activity. Previously, we have demonstrated that the S-layer glycoprotein from probiotic Lactobacillus kefiri CIDCA 8348 (SLP-8348) is recognized by Mincle (macrophage inducible C-type lectin receptor) and its adjuvanticity depends on the integrity of its glycans. However, the glycan´s structure has not been described so far. Herein, we analyze the glycosylation pattern of three SLPs, SLP-8348, SLP-8321, and SLP-5818, and explore how these patterns impacts their recognition by Ctype lectin receptors (CLRs) and the immunomodulatory effect of the L. kefiri SLPs on antigen-presenting cells. HPAEC-PAD performed after β-elimination showed glucose as the major component in the O-glycans of the three SLPs, however, some differences in the length of hexose chains were observed. No N-glycosylation signals were detected in SLP-8348 and SLP-8321, but SLP5818 was observed to have two sites carrying complex N-glycans based on a site-specific analysis and a glycomic workflow of the permethylated glycans. SLP-8348 was previously shown to enhance LPS-induced activation on both RAW264.7 macrophages and murine BMDCs; we now show SLP-8321 and SLP-5818 have a similar effect regardless of the differences in their glycosylation patterns. Studies performed with BMDCs from CLR-deficient mice revealed that the immunostimulatory activity of SLP-8321 depends on its recognition by Mincle, whereas SLP-5818’s effects are dependent on SignR3 (murine ortholog of human DC-SIGN). These findings encourage further investigation of both the potential application of these SLPs as new adjuvants and the protein glycosylation mechanisms in these bacteria.Fil: Malamud, Mariano. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Cátedra de Microbiología General; Argentina. University of Veterinary Medicine Hannover; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Cavallero, Gustavo Javier. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono | Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono; ArgentinaFil: Casabuono, Adriana Cristina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono | Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono; ArgentinaFil: Lepenies, Bernd. University of Veterinary Medicine Hannover; AlemaniaFil: Serradell, María de los Ángeles. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Cátedra de Microbiología General; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Couto, Alicia Susana. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono | Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono; ArgentinaAmerican Society for Biochemistry and Molecular Biology2020-10-13info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/140048Malamud, Mariano; Cavallero, Gustavo Javier; Casabuono, Adriana Cristina; Lepenies, Bernd; Serradell, María de los Ángeles; et al.; Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 295; 42; 13-10-2020; 14430-144440021-92581083-351XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/lookup/doi/10.1074/jbc.RA120.013934info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.RA120.013934info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:29:44Zoai:ri.conicet.gov.ar:11336/140048instacron: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 10:29:45.02CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners |
title |
Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners |
spellingShingle |
Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners Malamud, Mariano LACTOBACILLUS KEFIRI S-LAYER PROTEINS GLYCOSYLATION |
title_short |
Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners |
title_full |
Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners |
title_fullStr |
Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners |
title_full_unstemmed |
Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners |
title_sort |
Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners |
dc.creator.none.fl_str_mv |
Malamud, Mariano Cavallero, Gustavo Javier Casabuono, Adriana Cristina Lepenies, Bernd Serradell, María de los Ángeles Couto, Alicia Susana |
author |
Malamud, Mariano |
author_facet |
Malamud, Mariano Cavallero, Gustavo Javier Casabuono, Adriana Cristina Lepenies, Bernd Serradell, María de los Ángeles Couto, Alicia Susana |
author_role |
author |
author2 |
Cavallero, Gustavo Javier Casabuono, Adriana Cristina Lepenies, Bernd Serradell, María de los Ángeles Couto, Alicia Susana |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
LACTOBACILLUS KEFIRI S-LAYER PROTEINS GLYCOSYLATION |
topic |
LACTOBACILLUS KEFIRI S-LAYER PROTEINS GLYCOSYLATION |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
S-layer (glyco)-proteins (SLPs) form a nanostructured envelope that covers the surface of different prokaryotes and show immunomodulatory activity. Previously, we have demonstrated that the S-layer glycoprotein from probiotic Lactobacillus kefiri CIDCA 8348 (SLP-8348) is recognized by Mincle (macrophage inducible C-type lectin receptor) and its adjuvanticity depends on the integrity of its glycans. However, the glycan´s structure has not been described so far. Herein, we analyze the glycosylation pattern of three SLPs, SLP-8348, SLP-8321, and SLP-5818, and explore how these patterns impacts their recognition by Ctype lectin receptors (CLRs) and the immunomodulatory effect of the L. kefiri SLPs on antigen-presenting cells. HPAEC-PAD performed after β-elimination showed glucose as the major component in the O-glycans of the three SLPs, however, some differences in the length of hexose chains were observed. No N-glycosylation signals were detected in SLP-8348 and SLP-8321, but SLP5818 was observed to have two sites carrying complex N-glycans based on a site-specific analysis and a glycomic workflow of the permethylated glycans. SLP-8348 was previously shown to enhance LPS-induced activation on both RAW264.7 macrophages and murine BMDCs; we now show SLP-8321 and SLP-5818 have a similar effect regardless of the differences in their glycosylation patterns. Studies performed with BMDCs from CLR-deficient mice revealed that the immunostimulatory activity of SLP-8321 depends on its recognition by Mincle, whereas SLP-5818’s effects are dependent on SignR3 (murine ortholog of human DC-SIGN). These findings encourage further investigation of both the potential application of these SLPs as new adjuvants and the protein glycosylation mechanisms in these bacteria. Fil: Malamud, Mariano. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Cátedra de Microbiología General; Argentina. University of Veterinary Medicine Hannover; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina Fil: Cavallero, Gustavo Javier. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono | Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono; Argentina Fil: Casabuono, Adriana Cristina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono | Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono; Argentina Fil: Lepenies, Bernd. University of Veterinary Medicine Hannover; Alemania Fil: Serradell, María de los Ángeles. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Cátedra de Microbiología General; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina Fil: Couto, Alicia Susana. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono | Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono. Subsede del Centro de Investigaciones en Hidratos de Carbono; Argentina |
description |
S-layer (glyco)-proteins (SLPs) form a nanostructured envelope that covers the surface of different prokaryotes and show immunomodulatory activity. Previously, we have demonstrated that the S-layer glycoprotein from probiotic Lactobacillus kefiri CIDCA 8348 (SLP-8348) is recognized by Mincle (macrophage inducible C-type lectin receptor) and its adjuvanticity depends on the integrity of its glycans. However, the glycan´s structure has not been described so far. Herein, we analyze the glycosylation pattern of three SLPs, SLP-8348, SLP-8321, and SLP-5818, and explore how these patterns impacts their recognition by Ctype lectin receptors (CLRs) and the immunomodulatory effect of the L. kefiri SLPs on antigen-presenting cells. HPAEC-PAD performed after β-elimination showed glucose as the major component in the O-glycans of the three SLPs, however, some differences in the length of hexose chains were observed. No N-glycosylation signals were detected in SLP-8348 and SLP-8321, but SLP5818 was observed to have two sites carrying complex N-glycans based on a site-specific analysis and a glycomic workflow of the permethylated glycans. SLP-8348 was previously shown to enhance LPS-induced activation on both RAW264.7 macrophages and murine BMDCs; we now show SLP-8321 and SLP-5818 have a similar effect regardless of the differences in their glycosylation patterns. Studies performed with BMDCs from CLR-deficient mice revealed that the immunostimulatory activity of SLP-8321 depends on its recognition by Mincle, whereas SLP-5818’s effects are dependent on SignR3 (murine ortholog of human DC-SIGN). These findings encourage further investigation of both the potential application of these SLPs as new adjuvants and the protein glycosylation mechanisms in these bacteria. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-10-13 |
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/11336/140048 Malamud, Mariano; Cavallero, Gustavo Javier; Casabuono, Adriana Cristina; Lepenies, Bernd; Serradell, María de los Ángeles; et al.; Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 295; 42; 13-10-2020; 14430-14444 0021-9258 1083-351X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/140048 |
identifier_str_mv |
Malamud, Mariano; Cavallero, Gustavo Javier; Casabuono, Adriana Cristina; Lepenies, Bernd; Serradell, María de los Ángeles; et al.; Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 295; 42; 13-10-2020; 14430-14444 0021-9258 1083-351X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/lookup/doi/10.1074/jbc.RA120.013934 info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.RA120.013934 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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1844614304575258624 |
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13.070432 |