Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium spp

Autores
Abdian, Patricia Lorena; Malori, María Soledad; Caramelo, Julio J.; Maglio Checchi, Abi; Russo, Daniela M.; Zorreguieta, Angeles; Berretta, Marcelo Facundo; Benintende, Graciela Beatriz
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Rhizobium adhering proteins or ‘Raps’ are secreted proteins identified in a very restricted group of rhizobial strains, specifically those belonging to R. leguminosarum and R. etli. The distinctive feature of members of the Rap family is the presence of one or two cadherin-like domains or CHDLs that are also present in numerous extracellular bacterial and archaeal proteins and were proposed to confer carbohydrate binding ability. We have previously made an in-depth characterization of RapA2, a calciumbinding lectin, composed by two CHDLs, involved in biofilm matrix remodelling in R. leguminosarum bv. viciae 3841. In this study, CHDLs derived from RapA2 were analysed in detail, finding significant structural and functional differences despite their considerable sequence similarity. Only the carboxy-terminal CHDL retained properties similar to those displayed by RapA2. Our findings were used to obtain a novel fluorescent probe to study biofilm matrix development by confocal laser scanning microscopy, and also to shed some light on the role of the ubiquitous CHDL domains in bacterial secreted proteins.
Instituto de Microbiología y Zoología Agrícola (IMYZA)
Fil: Abdian, Patricia Lorena. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Abdian, Patricia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Malori, María Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; Argentina
Fil: Caramelo, Julio J. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; Argentina
Fil: Maglio Checchi, Abi. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Maglio Checchi, Abi. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Russo, Daniela M. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; Argentina
Fil: Zorreguieta, Angeles. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; Argentina
Fil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Berretta, Marcelo Facundo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Benintende, Graciela Beatriz. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fuente
Microbiology 168 (12) : 1284 (Diciembre 2022)
Materia
Rhizobium
Biofilmes (microbiología)
Lectinas
Biofilms (microbiology)
Lectins
Biofilm Matrix
GFP-fusion protein
Rizobios
Biopelículas
Exopolysaccharide
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/16624
Acceder
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oai_identifier_str oai:localhost:20.500.12123/16624
network_acronym_str INTADig
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network_name_str INTA Digital (INTA)
spelling Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium sppAbdian, Patricia LorenaMalori, María SoledadCaramelo, Julio J.Maglio Checchi, AbiRusso, Daniela M.Zorreguieta, AngelesBerretta, Marcelo FacundoBenintende, Graciela BeatrizRhizobiumBiofilmes (microbiología)LectinasBiofilms (microbiology)LectinsBiofilm MatrixGFP-fusion proteinRizobiosBiopelículasExopolysaccharideRhizobium adhering proteins or ‘Raps’ are secreted proteins identified in a very restricted group of rhizobial strains, specifically those belonging to R. leguminosarum and R. etli. The distinctive feature of members of the Rap family is the presence of one or two cadherin-like domains or CHDLs that are also present in numerous extracellular bacterial and archaeal proteins and were proposed to confer carbohydrate binding ability. We have previously made an in-depth characterization of RapA2, a calciumbinding lectin, composed by two CHDLs, involved in biofilm matrix remodelling in R. leguminosarum bv. viciae 3841. In this study, CHDLs derived from RapA2 were analysed in detail, finding significant structural and functional differences despite their considerable sequence similarity. Only the carboxy-terminal CHDL retained properties similar to those displayed by RapA2. Our findings were used to obtain a novel fluorescent probe to study biofilm matrix development by confocal laser scanning microscopy, and also to shed some light on the role of the ubiquitous CHDL domains in bacterial secreted proteins.Instituto de Microbiología y Zoología Agrícola (IMYZA)Fil: Abdian, Patricia Lorena. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; ArgentinaFil: Abdian, Patricia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Malori, María Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; ArgentinaFil: Caramelo, Julio J. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; ArgentinaFil: Maglio Checchi, Abi. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; ArgentinaFil: Maglio Checchi, Abi. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Russo, Daniela M. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; ArgentinaFil: Zorreguieta, Angeles. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; ArgentinaFil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; ArgentinaFil: Berretta, Marcelo Facundo. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Benintende, Graciela Beatriz. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; ArgentinaMicrobiology Society2024-02-15T14:00:39Z2024-02-15T14:00:39Z2022-12-13info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/16624https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.0012841350-08721465-2080https://doi.org/10.1099/mic.0.001284Microbiology 168 (12) : 1284 (Diciembre 2022)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2025-10-23T11:18:40Zoai:localhost:20.500.12123/16624instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-10-23 11:18:41.294INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium spp
title Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium spp
spellingShingle Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium spp
Abdian, Patricia Lorena
Rhizobium
Biofilmes (microbiología)
Lectinas
Biofilms (microbiology)
Lectins
Biofilm Matrix
GFP-fusion protein
Rizobios
Biopelículas
Exopolysaccharide
title_short Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium spp
title_full Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium spp
title_fullStr Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium spp
title_full_unstemmed Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium spp
title_sort Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium spp
dc.creator.none.fl_str_mv Abdian, Patricia Lorena
Malori, María Soledad
Caramelo, Julio J.
Maglio Checchi, Abi
Russo, Daniela M.
Zorreguieta, Angeles
Berretta, Marcelo Facundo
Benintende, Graciela Beatriz
author Abdian, Patricia Lorena
author_facet Abdian, Patricia Lorena
Malori, María Soledad
Caramelo, Julio J.
Maglio Checchi, Abi
Russo, Daniela M.
Zorreguieta, Angeles
Berretta, Marcelo Facundo
Benintende, Graciela Beatriz
author_role author
author2 Malori, María Soledad
Caramelo, Julio J.
Maglio Checchi, Abi
Russo, Daniela M.
Zorreguieta, Angeles
Berretta, Marcelo Facundo
Benintende, Graciela Beatriz
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Rhizobium
Biofilmes (microbiología)
Lectinas
Biofilms (microbiology)
Lectins
Biofilm Matrix
GFP-fusion protein
Rizobios
Biopelículas
Exopolysaccharide
topic Rhizobium
Biofilmes (microbiología)
Lectinas
Biofilms (microbiology)
Lectins
Biofilm Matrix
GFP-fusion protein
Rizobios
Biopelículas
Exopolysaccharide
dc.description.none.fl_txt_mv Rhizobium adhering proteins or ‘Raps’ are secreted proteins identified in a very restricted group of rhizobial strains, specifically those belonging to R. leguminosarum and R. etli. The distinctive feature of members of the Rap family is the presence of one or two cadherin-like domains or CHDLs that are also present in numerous extracellular bacterial and archaeal proteins and were proposed to confer carbohydrate binding ability. We have previously made an in-depth characterization of RapA2, a calciumbinding lectin, composed by two CHDLs, involved in biofilm matrix remodelling in R. leguminosarum bv. viciae 3841. In this study, CHDLs derived from RapA2 were analysed in detail, finding significant structural and functional differences despite their considerable sequence similarity. Only the carboxy-terminal CHDL retained properties similar to those displayed by RapA2. Our findings were used to obtain a novel fluorescent probe to study biofilm matrix development by confocal laser scanning microscopy, and also to shed some light on the role of the ubiquitous CHDL domains in bacterial secreted proteins.
Instituto de Microbiología y Zoología Agrícola (IMYZA)
Fil: Abdian, Patricia Lorena. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Abdian, Patricia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Malori, María Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; Argentina
Fil: Caramelo, Julio J. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; Argentina
Fil: Maglio Checchi, Abi. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Maglio Checchi, Abi. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Russo, Daniela M. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; Argentina
Fil: Zorreguieta, Angeles. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir; Argentina
Fil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Berretta, Marcelo Facundo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Benintende, Graciela Beatriz. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
description Rhizobium adhering proteins or ‘Raps’ are secreted proteins identified in a very restricted group of rhizobial strains, specifically those belonging to R. leguminosarum and R. etli. The distinctive feature of members of the Rap family is the presence of one or two cadherin-like domains or CHDLs that are also present in numerous extracellular bacterial and archaeal proteins and were proposed to confer carbohydrate binding ability. We have previously made an in-depth characterization of RapA2, a calciumbinding lectin, composed by two CHDLs, involved in biofilm matrix remodelling in R. leguminosarum bv. viciae 3841. In this study, CHDLs derived from RapA2 were analysed in detail, finding significant structural and functional differences despite their considerable sequence similarity. Only the carboxy-terminal CHDL retained properties similar to those displayed by RapA2. Our findings were used to obtain a novel fluorescent probe to study biofilm matrix development by confocal laser scanning microscopy, and also to shed some light on the role of the ubiquitous CHDL domains in bacterial secreted proteins.
publishDate 2022
dc.date.none.fl_str_mv 2022-12-13
2024-02-15T14:00:39Z
2024-02-15T14:00:39Z
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/20.500.12123/16624
https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.001284
1350-0872
1465-2080
https://doi.org/10.1099/mic.0.001284
url http://hdl.handle.net/20.500.12123/16624
https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.001284
https://doi.org/10.1099/mic.0.001284
identifier_str_mv 1350-0872
1465-2080
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Microbiology Society
publisher.none.fl_str_mv Microbiology Society
dc.source.none.fl_str_mv Microbiology 168 (12) : 1284 (Diciembre 2022)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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score 12.928904

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