Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity

Autores
Carrica, Mariela del Carmen; Craig, Patricio Oliver; Alonso, Silvia del Valle; Goldbaum, Fernando Alberto; Cravero, Silvio Lorenzo Pedro
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The bacterial genus Brucella consists of a group of facultative intracellular pathogens which produces abortion and infertility in animals and a chronic debilitating febrile illness in humans. BMFP is a basic protein of Brucella abortus that belongs to a highly conserved group of homologue proteins of unknown structure and function in proteobacteria (COG2960). In this study, we report the structural and biochemical characterization of this protein. We found that BMFP has two structural domains: a carboxylterminal coiled-coil domain through which the protein self-associates as a trimer and a natively disordered amino-terminal domain which has propensity to adopt an amphipathic R-helical structure. This natively unfolded domain undergoes a structural rearrangement from unfolded to R-helix in the presence of high ionic strength, acidic pH, detergents, and phospholipid vesicles. Moreover, we demonstrated that the interaction of BMFP with phospholipid vesicles promotes in vitro membrane fusion. These results contribute to the elucidation of the structural and functional properties of this protein and its homologues present in most proteobacteria
Fil: Carrica, Mariela del Carmen. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Craig, Patricio Oliver. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Alonso, Silvia del Valle. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Goldbaum, Fernando Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Cravero, Silvio Lorenzo Pedro. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina
Materia
Bmfp
Trimeric
Coiled Coil
Membrane Fusion
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/29536
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/29536
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network_name_str CONICET Digital (CONICET)
spelling Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic ActivityCarrica, Mariela del CarmenCraig, Patricio OliverAlonso, Silvia del ValleGoldbaum, Fernando AlbertoCravero, Silvio Lorenzo PedroBmfpTrimericCoiled CoilMembrane Fusionhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3The bacterial genus Brucella consists of a group of facultative intracellular pathogens which produces abortion and infertility in animals and a chronic debilitating febrile illness in humans. BMFP is a basic protein of Brucella abortus that belongs to a highly conserved group of homologue proteins of unknown structure and function in proteobacteria (COG2960). In this study, we report the structural and biochemical characterization of this protein. We found that BMFP has two structural domains: a carboxylterminal coiled-coil domain through which the protein self-associates as a trimer and a natively disordered amino-terminal domain which has propensity to adopt an amphipathic R-helical structure. This natively unfolded domain undergoes a structural rearrangement from unfolded to R-helix in the presence of high ionic strength, acidic pH, detergents, and phospholipid vesicles. Moreover, we demonstrated that the interaction of BMFP with phospholipid vesicles promotes in vitro membrane fusion. These results contribute to the elucidation of the structural and functional properties of this protein and its homologues present in most proteobacteriaFil: Carrica, Mariela del Carmen. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Craig, Patricio Oliver. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Alonso, Silvia del Valle. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Goldbaum, Fernando Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Cravero, Silvio Lorenzo Pedro. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; ArgentinaAmerican Chemical Society2008-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/29536Carrica, Mariela del Carmen; Craig, Patricio Oliver; Alonso, Silvia del Valle; Goldbaum, Fernando Alberto; Cravero, Silvio Lorenzo Pedro; Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity; American Chemical Society; Biochemistry; 47; 31; 12-2008; 8165-81750006-2960CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/bi800462yinfo:eu-repo/semantics/altIdentifier/doi/10.1021/bi800462yinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:08:15Zoai:ri.conicet.gov.ar:11336/29536instacron: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:34982025-09-03 10:08:16.076CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity
title Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity
spellingShingle Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity
Carrica, Mariela del Carmen
Bmfp
Trimeric
Coiled Coil
Membrane Fusion
title_short Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity
title_full Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity
title_fullStr Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity
title_full_unstemmed Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity
title_sort Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity
dc.creator.none.fl_str_mv Carrica, Mariela del Carmen
Craig, Patricio Oliver
Alonso, Silvia del Valle
Goldbaum, Fernando Alberto
Cravero, Silvio Lorenzo Pedro
author Carrica, Mariela del Carmen
author_facet Carrica, Mariela del Carmen
Craig, Patricio Oliver
Alonso, Silvia del Valle
Goldbaum, Fernando Alberto
Cravero, Silvio Lorenzo Pedro
author_role author
author2 Craig, Patricio Oliver
Alonso, Silvia del Valle
Goldbaum, Fernando Alberto
Cravero, Silvio Lorenzo Pedro
author2_role author
author
author
author
dc.subject.none.fl_str_mv Bmfp
Trimeric
Coiled Coil
Membrane Fusion
topic Bmfp
Trimeric
Coiled Coil
Membrane Fusion
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv The bacterial genus Brucella consists of a group of facultative intracellular pathogens which produces abortion and infertility in animals and a chronic debilitating febrile illness in humans. BMFP is a basic protein of Brucella abortus that belongs to a highly conserved group of homologue proteins of unknown structure and function in proteobacteria (COG2960). In this study, we report the structural and biochemical characterization of this protein. We found that BMFP has two structural domains: a carboxylterminal coiled-coil domain through which the protein self-associates as a trimer and a natively disordered amino-terminal domain which has propensity to adopt an amphipathic R-helical structure. This natively unfolded domain undergoes a structural rearrangement from unfolded to R-helix in the presence of high ionic strength, acidic pH, detergents, and phospholipid vesicles. Moreover, we demonstrated that the interaction of BMFP with phospholipid vesicles promotes in vitro membrane fusion. These results contribute to the elucidation of the structural and functional properties of this protein and its homologues present in most proteobacteria
Fil: Carrica, Mariela del Carmen. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Craig, Patricio Oliver. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Alonso, Silvia del Valle. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Goldbaum, Fernando Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Cravero, Silvio Lorenzo Pedro. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina
description The bacterial genus Brucella consists of a group of facultative intracellular pathogens which produces abortion and infertility in animals and a chronic debilitating febrile illness in humans. BMFP is a basic protein of Brucella abortus that belongs to a highly conserved group of homologue proteins of unknown structure and function in proteobacteria (COG2960). In this study, we report the structural and biochemical characterization of this protein. We found that BMFP has two structural domains: a carboxylterminal coiled-coil domain through which the protein self-associates as a trimer and a natively disordered amino-terminal domain which has propensity to adopt an amphipathic R-helical structure. This natively unfolded domain undergoes a structural rearrangement from unfolded to R-helix in the presence of high ionic strength, acidic pH, detergents, and phospholipid vesicles. Moreover, we demonstrated that the interaction of BMFP with phospholipid vesicles promotes in vitro membrane fusion. These results contribute to the elucidation of the structural and functional properties of this protein and its homologues present in most proteobacteria
publishDate 2008
dc.date.none.fl_str_mv 2008-12
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/11336/29536
Carrica, Mariela del Carmen; Craig, Patricio Oliver; Alonso, Silvia del Valle; Goldbaum, Fernando Alberto; Cravero, Silvio Lorenzo Pedro; Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity; American Chemical Society; Biochemistry; 47; 31; 12-2008; 8165-8175
0006-2960
CONICET Digital
CONICET
url http://hdl.handle.net/11336/29536
identifier_str_mv Carrica, Mariela del Carmen; Craig, Patricio Oliver; Alonso, Silvia del Valle; Goldbaum, Fernando Alberto; Cravero, Silvio Lorenzo Pedro; Brucella abortus MFP: A Trimeric Coiled-Coil Protein with Membrane Fusogenic Activity; American Chemical Society; Biochemistry; 47; 31; 12-2008; 8165-8175
0006-2960
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://pubs.acs.org/doi/abs/10.1021/bi800462y
info:eu-repo/semantics/altIdentifier/doi/10.1021/bi800462y
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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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score 13.13397

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