Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli
Background: Gram negative bacteria possess different secretion systems to export proteins to the extracellular medium. The simplest one, type I secretion system (T1SS), forms a channel across the cell envelope to export proteins in a single step. Peptides secreted by the T1SSs comprise a group of an...
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| Format: | article |
| Language: | English |
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2024
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| Online Access: | https://hdl.handle.net/20.500.12008/51083 |
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| _version_ | 1868890101974564864 |
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| author | Flórez Cardona, Valeria |
| author2 | Marizcurrena, Juan José Laviña, Magela Azpiroz Hernández, María Fernanda |
| author2_role | author author author |
| author_browse | Azpiroz Hernández, María Fernanda Flórez Cardona, Valeria Laviña, Magela Marizcurrena, Juan José |
| author_facet | Flórez Cardona, Valeria Marizcurrena, Juan José Laviña, Magela Azpiroz Hernández, María Fernanda |
| author_role | author |
| collection | COLIBRI |
| dc.contributor.none.fl_str_mv | Flórez Cardona Valeria, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. Marizcurrena Juan José, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. Laviña Magela, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. Azpiroz Hernández María Fernanda, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. |
| dc.creator.none.fl_str_mv | Flórez Cardona, Valeria Marizcurrena, Juan José Laviña, Magela Azpiroz Hernández, María Fernanda |
| dc.date.none.fl_str_mv | 2024 2025-08-18T16:49:49Z 2025-08-18T16:49:49Z |
| dc.format.none.fl_str_mv | 14 h application/pdf |
| dc.identifier.none.fl_str_mv | Flórez Cardona, V, Marizcurrena, J, Laviña, M [y otro autor]. "Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli". Microbial Cell Factories. [en línea] 2024, 23: 273. 14 h. DOI: 10.1186/s12934-024-02552-5 1475-2859 https://hdl.handle.net/20.500.12008/51083 10.1186/s12934-024-02552-5 |
| dc.language.none.fl_str_mv | en eng |
| dc.publisher.none.fl_str_mv | BMC |
| dc.relation.none.fl_str_mv | Microbial Cell Factories, 2024, 23: 273. |
| dc.rights.none.fl_str_mv | info:eu-repo/semantics/openAccess Licencia Creative Commons Atribución - No Comercial - Sin Derivadas (CC - By-NC-ND 4.0) |
| dc.source.none.fl_str_mv | reponame:COLIBRI instname:Universidad de la República instacron:Universidad de la República |
| dc.subject.none.fl_str_mv | Type I secretion system Microcin V Human parathyroid hormone Recombinant peptide secretion in Escherichia coli |
| dc.title.none.fl_str_mv | Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli |
| dc.type.none.fl_str_mv | Artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
| description | Background: Gram negative bacteria possess different secretion systems to export proteins to the extracellular medium. The simplest one, type I secretion system (T1SS), forms a channel across the cell envelope to export proteins in a single step. Peptides secreted by the T1SSs comprise a group of antibiotics, called class II microcins, which carry an amino terminal secretion domain that is processed concomitantly with export. Mature microcins range in size from 60 to 90 amino acids and differ in their sequences. Microcin T1SSs show a high versatility in relation to the peptides they are able to secrete, being mainly limited by the length of the substrates. Different bioactive peptides unrelated to bacteriocins could be secreted by microcin V (MccV) T1SS, while retaining their biological activity. Results: In this work heterologous secretion of two variants of human parathyroid hormone (PTH) by MccV T1SS was evaluated. PTH is a bioactive peptide of 84 amino acids (PTH84), which is involved in the maintenance of bone homeostasis. Currently, a drug corresponding to the active fraction of the hormone, which resides in its first 34 amino acids (PTH34), is commercially produced as a recombinant peptide in Escherichia coli. However, research continues to improve this recombinant production. Here, gene fusions encoding hybrid peptides composed of the MccV secretion domain attached to each hormone variant were constructed and expressed in the presence of microcin T1SS in E. coli cells. Both PTH peptides (PTH34 and PTH84) were recovered from the culture supernatants and could be confirmed to lack the MccV secretion domain, i.e. microcin T1SS efficiently recognised, processed and secreted both PTH variants. Furthermore, the secreted peptides were stable in the extracellular medium unlike their unprocessed counterparts present in the intracellular space. Conclusion: The successful secretion of PTH variants using MccV T1SS could be considered as a new alternative for their production, since they would be recovered directly from the extracellular space without additional sequences. Furthermore, it would be a new example revealing the potential of microcin type I secretion systems to be conceived as a novel strategy for the production of recombinant peptides in E. coli. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | anni_7963e1ebb2ae930e640e6d22cae0082a |
| identifier_str_mv | Flórez Cardona, V, Marizcurrena, J, Laviña, M [y otro autor]. "Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli". Microbial Cell Factories. [en línea] 2024, 23: 273. 14 h. DOI: 10.1186/s12934-024-02552-5 1475-2859 10.1186/s12934-024-02552-5 |
| instacron_str | Universidad de la República |
| institution | Universidad de la República |
| instname_str | Universidad de la República |
| language | eng |
| language_invalid_str_mv | en |
| network_acronym_str | anni |
| network_name_str | oai-lr-anni |
| oai_identifier_str | oai:colibri.udelar.edu.uy:20.500.12008/51083 |
| publishDate | 2024 |
| publishDateSort | 2024 |
| publisher.none.fl_str_mv | BMC |
| reponame_str | COLIBRI |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | Licencia Creative Commons Atribución - No Comercial - Sin Derivadas (CC - By-NC-ND 4.0) |
| spelling | Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coliFlórez Cardona, ValeriaMarizcurrena, Juan JoséLaviña, MagelaAzpiroz Hernández, María FernandaType I secretion systemMicrocin VHuman parathyroid hormoneRecombinant peptide secretion in Escherichia coliBackground: Gram negative bacteria possess different secretion systems to export proteins to the extracellular medium. The simplest one, type I secretion system (T1SS), forms a channel across the cell envelope to export proteins in a single step. Peptides secreted by the T1SSs comprise a group of antibiotics, called class II microcins, which carry an amino terminal secretion domain that is processed concomitantly with export. Mature microcins range in size from 60 to 90 amino acids and differ in their sequences. Microcin T1SSs show a high versatility in relation to the peptides they are able to secrete, being mainly limited by the length of the substrates. Different bioactive peptides unrelated to bacteriocins could be secreted by microcin V (MccV) T1SS, while retaining their biological activity. Results: In this work heterologous secretion of two variants of human parathyroid hormone (PTH) by MccV T1SS was evaluated. PTH is a bioactive peptide of 84 amino acids (PTH84), which is involved in the maintenance of bone homeostasis. Currently, a drug corresponding to the active fraction of the hormone, which resides in its first 34 amino acids (PTH34), is commercially produced as a recombinant peptide in Escherichia coli. However, research continues to improve this recombinant production. Here, gene fusions encoding hybrid peptides composed of the MccV secretion domain attached to each hormone variant were constructed and expressed in the presence of microcin T1SS in E. coli cells. Both PTH peptides (PTH34 and PTH84) were recovered from the culture supernatants and could be confirmed to lack the MccV secretion domain, i.e. microcin T1SS efficiently recognised, processed and secreted both PTH variants. Furthermore, the secreted peptides were stable in the extracellular medium unlike their unprocessed counterparts present in the intracellular space. Conclusion: The successful secretion of PTH variants using MccV T1SS could be considered as a new alternative for their production, since they would be recovered directly from the extracellular space without additional sequences. Furthermore, it would be a new example revealing the potential of microcin type I secretion systems to be conceived as a novel strategy for the production of recombinant peptides in E. coli.BMCFlórez Cardona Valeria, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.Marizcurrena Juan José, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.Laviña Magela, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.Azpiroz Hernández María Fernanda, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.2025-08-18T16:49:49Z2025-08-18T16:49:49Z2024Artículoinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion14 happlication/pdfFlórez Cardona, V, Marizcurrena, J, Laviña, M [y otro autor]. "Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli". Microbial Cell Factories. [en línea] 2024, 23: 273. 14 h. DOI: 10.1186/s12934-024-02552-51475-2859https://hdl.handle.net/20.500.12008/5108310.1186/s12934-024-02552-5reponame:COLIBRIinstname:Universidad de la Repúblicainstacron:Universidad de la RepúblicaenengMicrobial Cell Factories, 2024, 23: 273.Las obras depositadas en el Repositorio se rigen por la Ordenanza de los Derechos de la Propiedad Intelectual de la Universidad de la República.(Res. Nº 91 de C.D.C. de 8/III/1994 – D.O. 7/IV/1994) y por la Ordenanza del Repositorio Abierto de la Universidad de la República (Res. Nº 16 de C.D.C. de 07/10/2014)info:eu-repo/semantics/openAccessLicencia Creative Commons Atribución - No Comercial - Sin Derivadas (CC - By-NC-ND 4.0)oai:colibri.udelar.edu.uy:20.500.12008/510832026-04-14T10:10:56Z |
| spellingShingle | Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli Flórez Cardona, Valeria Type I secretion system Microcin V Human parathyroid hormone Recombinant peptide secretion in Escherichia coli |
| status_str | publishedVersion |
| title | Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli |
| title_full | Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli |
| title_fullStr | Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli |
| title_full_unstemmed | Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli |
| title_short | Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli |
| title_sort | Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli |
| topic | Type I secretion system Microcin V Human parathyroid hormone Recombinant peptide secretion in Escherichia coli |
| url | https://hdl.handle.net/20.500.12008/51083 |