Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum

Autores
Torkko, Juha M.; Primo, Maria Evangelina; Dirkx, Ronald; Friedrich, Anne; Viehrig, Antje; Vergari, Elisa; Borgonovo, Barbara; Sönmez, Anke; Wegbrod, Carolin; Lachnit, Martina; Münster, Carla; Sica, Mauricio Pablo; Ermacora, Mario Roberto; Solimena, Michele
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The type 1 diabetes autoantigen ICA512/IA-2/RPTPN is a receptor protein tyrosine phosphatase of the insulin secretory granules (SGs) which regulates the size of granule stores, possibly via cleavage/signaling of its cytosolic tail. The role of its extracellular region remains unknown. Structural studies indicated that β2- or β4-strands in the mature ectodomain (ME ICA512) form dimers in vitro. Here we show that ME ICA512 prompts proICA512 dimerization in the endoplasmic reticulum. Perturbation of ME ICA512 β2-strand N-glycosylation upon S508A replacement allows for proICA512 dimerization, O-glycosylation, targeting to granules, and conversion, which are instead precluded upon G553D replacement in the ME ICA512 β4-strand. S508A/G553D and N506A/G553D double mutants dimerize but remain in the endoplasmic reticulum. Removal of the N-terminal fragment (ICA512-NTF) preceding ME ICA512 allows an ICA512-ΔNTF G553D mutant to exit the endoplasmic reticulum, and ICA512-ΔNTF is constitutively delivered to the cell surface. The signal for SG sorting is located within the NTF RESP18 homology domain (RESP18-HD), whereas soluble NTF is retained in the endoplasmic reticulum. Hence, we propose that the ME ICA512 β2-strand fosters proICA512 dimerization until NTF prevents N506 glycosylation. Removal of this constraint allows for proICA512 β4-strand-induced dimerization, exit from the endoplasmic reticulum, O-glycosylation, and RESP18-HD-mediated targeting to granules.
Fil: Torkko, Juha M.. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; Alemania
Fil: Primo, Maria Evangelina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Dirkx, Ronald. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania
Fil: Friedrich, Anne. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania
Fil: Viehrig, Antje. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania
Fil: Vergari, Elisa. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; Alemania
Fil: Borgonovo, Barbara. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. Max Planck Institute of Molecular Cell Biology and Genetics; Alemania
Fil: Sönmez, Anke. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania
Fil: Wegbrod, Carolin. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; Alemania
Fil: Lachnit, Martina. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; Alemania
Fil: Münster, Carla. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania
Fil: Sica, Mauricio Pablo. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Ermacora, Mario Roberto. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Solimena, Michele. Max Planck Institute of Molecular Cell Biology and Genetics; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; Alemania
Materia
DIABETES
ICA512
INSULIN
SECRESION GRANULES
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/37786
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulumTorkko, Juha M.Primo, Maria EvangelinaDirkx, RonaldFriedrich, AnneViehrig, AntjeVergari, ElisaBorgonovo, BarbaraSönmez, AnkeWegbrod, CarolinLachnit, MartinaMünster, CarlaSica, Mauricio PabloErmacora, Mario RobertoSolimena, MicheleDIABETESICA512INSULINSECRESION GRANULEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The type 1 diabetes autoantigen ICA512/IA-2/RPTPN is a receptor protein tyrosine phosphatase of the insulin secretory granules (SGs) which regulates the size of granule stores, possibly via cleavage/signaling of its cytosolic tail. The role of its extracellular region remains unknown. Structural studies indicated that β2- or β4-strands in the mature ectodomain (ME ICA512) form dimers in vitro. Here we show that ME ICA512 prompts proICA512 dimerization in the endoplasmic reticulum. Perturbation of ME ICA512 β2-strand N-glycosylation upon S508A replacement allows for proICA512 dimerization, O-glycosylation, targeting to granules, and conversion, which are instead precluded upon G553D replacement in the ME ICA512 β4-strand. S508A/G553D and N506A/G553D double mutants dimerize but remain in the endoplasmic reticulum. Removal of the N-terminal fragment (ICA512-NTF) preceding ME ICA512 allows an ICA512-ΔNTF G553D mutant to exit the endoplasmic reticulum, and ICA512-ΔNTF is constitutively delivered to the cell surface. The signal for SG sorting is located within the NTF RESP18 homology domain (RESP18-HD), whereas soluble NTF is retained in the endoplasmic reticulum. Hence, we propose that the ME ICA512 β2-strand fosters proICA512 dimerization until NTF prevents N506 glycosylation. Removal of this constraint allows for proICA512 β4-strand-induced dimerization, exit from the endoplasmic reticulum, O-glycosylation, and RESP18-HD-mediated targeting to granules.Fil: Torkko, Juha M.. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; AlemaniaFil: Primo, Maria Evangelina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; ArgentinaFil: Dirkx, Ronald. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; AlemaniaFil: Friedrich, Anne. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; AlemaniaFil: Viehrig, Antje. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; AlemaniaFil: Vergari, Elisa. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; AlemaniaFil: Borgonovo, Barbara. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. Max Planck Institute of Molecular Cell Biology and Genetics; AlemaniaFil: Sönmez, Anke. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; AlemaniaFil: Wegbrod, Carolin. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; AlemaniaFil: Lachnit, Martina. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; AlemaniaFil: Münster, Carla. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; AlemaniaFil: Sica, Mauricio Pablo. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; ArgentinaFil: Ermacora, Mario Roberto. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; ArgentinaFil: Solimena, Michele. Max Planck Institute of Molecular Cell Biology and Genetics; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; AlemaniaAmerican Society for Microbiology2015-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/37786Torkko, Juha M.; Primo, Maria Evangelina; Dirkx, Ronald; Friedrich, Anne; Viehrig, Antje; et al.; Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum; American Society for Microbiology; Molecular and Cellular Biology; 35; 6; 1-2015; 914-9270270-7306CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1128/MCB.00994-14info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4333099/info:eu-repo/semantics/altIdentifier/url/http://mcb.asm.org/content/35/6/914.longinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:24:12Zoai:ri.conicet.gov.ar:11336/37786instacron: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 10:24:12.944CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum
title Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum
spellingShingle Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum
Torkko, Juha M.
DIABETES
ICA512
INSULIN
SECRESION GRANULES
title_short Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum
title_full Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum
title_fullStr Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum
title_full_unstemmed Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum
title_sort Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum
dc.creator.none.fl_str_mv Torkko, Juha M.
Primo, Maria Evangelina
Dirkx, Ronald
Friedrich, Anne
Viehrig, Antje
Vergari, Elisa
Borgonovo, Barbara
Sönmez, Anke
Wegbrod, Carolin
Lachnit, Martina
Münster, Carla
Sica, Mauricio Pablo
Ermacora, Mario Roberto
Solimena, Michele
author Torkko, Juha M.
author_facet Torkko, Juha M.
Primo, Maria Evangelina
Dirkx, Ronald
Friedrich, Anne
Viehrig, Antje
Vergari, Elisa
Borgonovo, Barbara
Sönmez, Anke
Wegbrod, Carolin
Lachnit, Martina
Münster, Carla
Sica, Mauricio Pablo
Ermacora, Mario Roberto
Solimena, Michele
author_role author
author2 Primo, Maria Evangelina
Dirkx, Ronald
Friedrich, Anne
Viehrig, Antje
Vergari, Elisa
Borgonovo, Barbara
Sönmez, Anke
Wegbrod, Carolin
Lachnit, Martina
Münster, Carla
Sica, Mauricio Pablo
Ermacora, Mario Roberto
Solimena, Michele
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv DIABETES
ICA512
INSULIN
SECRESION GRANULES
topic DIABETES
ICA512
INSULIN
SECRESION GRANULES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The type 1 diabetes autoantigen ICA512/IA-2/RPTPN is a receptor protein tyrosine phosphatase of the insulin secretory granules (SGs) which regulates the size of granule stores, possibly via cleavage/signaling of its cytosolic tail. The role of its extracellular region remains unknown. Structural studies indicated that β2- or β4-strands in the mature ectodomain (ME ICA512) form dimers in vitro. Here we show that ME ICA512 prompts proICA512 dimerization in the endoplasmic reticulum. Perturbation of ME ICA512 β2-strand N-glycosylation upon S508A replacement allows for proICA512 dimerization, O-glycosylation, targeting to granules, and conversion, which are instead precluded upon G553D replacement in the ME ICA512 β4-strand. S508A/G553D and N506A/G553D double mutants dimerize but remain in the endoplasmic reticulum. Removal of the N-terminal fragment (ICA512-NTF) preceding ME ICA512 allows an ICA512-ΔNTF G553D mutant to exit the endoplasmic reticulum, and ICA512-ΔNTF is constitutively delivered to the cell surface. The signal for SG sorting is located within the NTF RESP18 homology domain (RESP18-HD), whereas soluble NTF is retained in the endoplasmic reticulum. Hence, we propose that the ME ICA512 β2-strand fosters proICA512 dimerization until NTF prevents N506 glycosylation. Removal of this constraint allows for proICA512 β4-strand-induced dimerization, exit from the endoplasmic reticulum, O-glycosylation, and RESP18-HD-mediated targeting to granules.
Fil: Torkko, Juha M.. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; Alemania
Fil: Primo, Maria Evangelina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Dirkx, Ronald. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania
Fil: Friedrich, Anne. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania
Fil: Viehrig, Antje. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania
Fil: Vergari, Elisa. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; Alemania
Fil: Borgonovo, Barbara. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. Max Planck Institute of Molecular Cell Biology and Genetics; Alemania
Fil: Sönmez, Anke. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania
Fil: Wegbrod, Carolin. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; Alemania
Fil: Lachnit, Martina. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; Alemania
Fil: Münster, Carla. German Center for Diabetes Research; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania
Fil: Sica, Mauricio Pablo. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Ermacora, Mario Roberto. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Fil: Solimena, Michele. Max Planck Institute of Molecular Cell Biology and Genetics; Alemania. Uniklinikum Carl Gustav Carus. Paul Langerhans Institute Dresden; Alemania. German Center for Diabetes Research; Alemania
description The type 1 diabetes autoantigen ICA512/IA-2/RPTPN is a receptor protein tyrosine phosphatase of the insulin secretory granules (SGs) which regulates the size of granule stores, possibly via cleavage/signaling of its cytosolic tail. The role of its extracellular region remains unknown. Structural studies indicated that β2- or β4-strands in the mature ectodomain (ME ICA512) form dimers in vitro. Here we show that ME ICA512 prompts proICA512 dimerization in the endoplasmic reticulum. Perturbation of ME ICA512 β2-strand N-glycosylation upon S508A replacement allows for proICA512 dimerization, O-glycosylation, targeting to granules, and conversion, which are instead precluded upon G553D replacement in the ME ICA512 β4-strand. S508A/G553D and N506A/G553D double mutants dimerize but remain in the endoplasmic reticulum. Removal of the N-terminal fragment (ICA512-NTF) preceding ME ICA512 allows an ICA512-ΔNTF G553D mutant to exit the endoplasmic reticulum, and ICA512-ΔNTF is constitutively delivered to the cell surface. The signal for SG sorting is located within the NTF RESP18 homology domain (RESP18-HD), whereas soluble NTF is retained in the endoplasmic reticulum. Hence, we propose that the ME ICA512 β2-strand fosters proICA512 dimerization until NTF prevents N506 glycosylation. Removal of this constraint allows for proICA512 β4-strand-induced dimerization, exit from the endoplasmic reticulum, O-glycosylation, and RESP18-HD-mediated targeting to granules.
publishDate 2015
dc.date.none.fl_str_mv 2015-01
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/11336/37786
Torkko, Juha M.; Primo, Maria Evangelina; Dirkx, Ronald; Friedrich, Anne; Viehrig, Antje; et al.; Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum; American Society for Microbiology; Molecular and Cellular Biology; 35; 6; 1-2015; 914-927
0270-7306
CONICET Digital
CONICET
url http://hdl.handle.net/11336/37786
identifier_str_mv Torkko, Juha M.; Primo, Maria Evangelina; Dirkx, Ronald; Friedrich, Anne; Viehrig, Antje; et al.; Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum; American Society for Microbiology; Molecular and Cellular Biology; 35; 6; 1-2015; 914-927
0270-7306
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1128/MCB.00994-14
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4333099/
info:eu-repo/semantics/altIdentifier/url/http://mcb.asm.org/content/35/6/914.long
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv 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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