Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in Rhizobium spp
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...
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| Format: | info:ar-repo/semantics/artículo |
| Language: | Inglés |
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Microbiology Society
2024
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| Online Access: | 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 |
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| author | Abdian, Patricia Lorena Malori, María Soledad Caramelo, Julio J. Maglio Checchi, Abi Russo, Daniela M. Zorreguieta, Angeles Berretta, Marcelo Facundo Benintende, Graciela Beatriz |
| author_browse | Abdian, Patricia Lorena Benintende, Graciela Beatriz Berretta, Marcelo Facundo Caramelo, Julio J. Maglio Checchi, Abi Malori, María Soledad Russo, Daniela M. Zorreguieta, Angeles |
| 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_sort | Abdian, Patricia Lorena |
| collection | INTA Digital |
| 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. |
| format | info:ar-repo/semantics/artículo |
| id | INTA16624 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2024 |
| publishDateRange | 2024 |
| publishDateSort | 2024 |
| publisher | Microbiology Society |
| publisherStr | Microbiology Society |
| record_format | dspace |
| spelling | INTA166242024-02-15T14:23:38Z 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 Malori, María Soledad Caramelo, Julio J. Maglio Checchi, Abi Russo, Daniela M. Zorreguieta, Angeles Berretta, Marcelo Facundo Benintende, Graciela Beatriz Rhizobium Biofilmes (microbiología) Lectinas Biofilms (microbiology) Lectins Biofilm Matrix GFP-fusion protein Rizobios Biopelículas Exopolysaccharide 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 2024-02-15T14:00:39Z 2024-02-15T14:00:39Z 2022-12-13 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 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 eng 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) application/pdf Microbiology Society Microbiology 168 (12) : 1284 (Diciembre 2022) |
| spellingShingle | Rhizobium Biofilmes (microbiología) Lectinas Biofilms (microbiology) Lectins Biofilm Matrix GFP-fusion protein Rizobios Biopelículas Exopolysaccharide Abdian, Patricia Lorena Malori, María Soledad Caramelo, Julio J. Maglio Checchi, Abi Russo, Daniela M. Zorreguieta, Angeles Berretta, Marcelo Facundo Benintende, Graciela Beatriz 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 |
| 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_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_sort | fusion of a bacterial cadherin like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in rhizobium spp |
| topic | Rhizobium Biofilmes (microbiología) Lectinas Biofilms (microbiology) Lectins Biofilm Matrix GFP-fusion protein Rizobios Biopelículas Exopolysaccharide |
| 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 |
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