The hydrolase PbHAD32 participates in the adherence of Paracoccidioides brasiliensis conidia to epithelial lung cells

ABSTRACT: Adherence of the dimorphic pathogenic fungus Paracoccidioides brasiliensis to lung epithelial cells is considered an essential event for the establishment of infection. We have previously shown that the PbHAD32 hydrolase is important in this early stage of the host-P. brasiliensis yeast ce...

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Autores:
Hernández Ruiz, Orville
Almeida Ramalho, Agostinho Joao
Tamayo Ossa, Diana Patricia
Torres Gómez, Isaura Patricia
García Cepero, Ana María
López García, Ángela María
Restrepo Moreno, Ángela
McEwen Ochoa, Juan Guillermo
Tipo de recurso:
Article of investigation
Fecha de publicación:
2012
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/24122
Acceso en línea:
http://hdl.handle.net/10495/24122
Palabra clave:
Paracoccidioides
Expresión Génica
Gene Expression
Regulación hacia Abajo
Down-Regulation
Rights
openAccess
License
http://creativecommons.org/licenses/by-nc/2.5/co/
id UDEA2_0a5b6333ed0dc39a8e6661f16af09b17
oai_identifier_str oai:bibliotecadigital.udea.edu.co:10495/24122
network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
dc.title.spa.fl_str_mv The hydrolase PbHAD32 participates in the adherence of Paracoccidioides brasiliensis conidia to epithelial lung cells
title The hydrolase PbHAD32 participates in the adherence of Paracoccidioides brasiliensis conidia to epithelial lung cells
spellingShingle The hydrolase PbHAD32 participates in the adherence of Paracoccidioides brasiliensis conidia to epithelial lung cells
Paracoccidioides
Expresión Génica
Gene Expression
Regulación hacia Abajo
Down-Regulation
title_short The hydrolase PbHAD32 participates in the adherence of Paracoccidioides brasiliensis conidia to epithelial lung cells
title_full The hydrolase PbHAD32 participates in the adherence of Paracoccidioides brasiliensis conidia to epithelial lung cells
title_fullStr The hydrolase PbHAD32 participates in the adherence of Paracoccidioides brasiliensis conidia to epithelial lung cells
title_full_unstemmed The hydrolase PbHAD32 participates in the adherence of Paracoccidioides brasiliensis conidia to epithelial lung cells
title_sort The hydrolase PbHAD32 participates in the adherence of Paracoccidioides brasiliensis conidia to epithelial lung cells
dc.creator.fl_str_mv Hernández Ruiz, Orville
Almeida Ramalho, Agostinho Joao
Tamayo Ossa, Diana Patricia
Torres Gómez, Isaura Patricia
García Cepero, Ana María
López García, Ángela María
Restrepo Moreno, Ángela
McEwen Ochoa, Juan Guillermo
dc.contributor.author.none.fl_str_mv Hernández Ruiz, Orville
Almeida Ramalho, Agostinho Joao
Tamayo Ossa, Diana Patricia
Torres Gómez, Isaura Patricia
García Cepero, Ana María
López García, Ángela María
Restrepo Moreno, Ángela
McEwen Ochoa, Juan Guillermo
dc.subject.decs.none.fl_str_mv Paracoccidioides
Expresión Génica
Gene Expression
Regulación hacia Abajo
Down-Regulation
topic Paracoccidioides
Expresión Génica
Gene Expression
Regulación hacia Abajo
Down-Regulation
description ABSTRACT: Adherence of the dimorphic pathogenic fungus Paracoccidioides brasiliensis to lung epithelial cells is considered an essential event for the establishment of infection. We have previously shown that the PbHAD32 hydrolase is important in this early stage of the host-P. brasiliensis yeast cells interaction. The aim of this study was to further elucidate the role of PbHAD32 in conidial thermodimorphism and their interaction with lung epithelial cells. Analysis of the PbHAD32 gene expression revealed higher mRNA levels during the conidia to mycelia (C – M) germination when compared to the conidia to yeast (C – Y) transition. Moreover, PbHAD32 was consistently expressed at higher levels upon infection of lung epithelial cells, but to a greater extent when conidia germinated to produce mycelia. Interestingly, at this particular transitional stage, more conidia adhered to epithelial cells than when they were transiting to the yeast form. Altogether our data further corroborates the importance of PbHAD32 during initial adherence to host cells and suggest that the 32-KDa hydrolase may also participate at different stages of the C – M and C – Y conversions.
publishDate 2012
dc.date.issued.none.fl_str_mv 2012
dc.date.accessioned.none.fl_str_mv 2021-11-15T20:06:46Z
dc.date.available.none.fl_str_mv 2021-11-15T20:06:46Z
dc.type.spa.fl_str_mv info:eu-repo/semantics/article
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dc.type.hasversion.spa.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.coar.spa.fl_str_mv http://purl.org/coar/resource_type/c_2df8fbb1
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dc.type.local.spa.fl_str_mv Artículo de investigación
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status_str publishedVersion
dc.identifier.issn.none.fl_str_mv 1369-3786
dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/10495/24122
dc.identifier.doi.none.fl_str_mv 10.3109/13693786.2011.619583
dc.identifier.eissn.none.fl_str_mv 1460-2709
identifier_str_mv 1369-3786
10.3109/13693786.2011.619583
1460-2709
url http://hdl.handle.net/10495/24122
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.ispartofjournalabbrev.spa.fl_str_mv Med. Mycol.
dc.rights.spa.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc/2.5/co/
http://purl.org/coar/access_right/c_abf2
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dc.format.extent.spa.fl_str_mv 5
dc.format.mimetype.spa.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Oxford University Press
dc.publisher.group.spa.fl_str_mv Biología Celular y Molecular CIB U. de A. U. del Rosario
Micología Médica y Experimental
dc.publisher.place.spa.fl_str_mv Oxford, Inglaterra
institution Universidad de Antioquia
bitstream.url.fl_str_mv http://bibliotecadigital.udea.edu.co/bitstream/10495/24122/1/HernandezOrville_2012_HydrolaseAdherence.pdf
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spelling Hernández Ruiz, OrvilleAlmeida Ramalho, Agostinho JoaoTamayo Ossa, Diana PatriciaTorres Gómez, Isaura PatriciaGarcía Cepero, Ana MaríaLópez García, Ángela MaríaRestrepo Moreno, ÁngelaMcEwen Ochoa, Juan Guillermo2021-11-15T20:06:46Z2021-11-15T20:06:46Z20121369-3786http://hdl.handle.net/10495/2412210.3109/13693786.2011.6195831460-2709ABSTRACT: Adherence of the dimorphic pathogenic fungus Paracoccidioides brasiliensis to lung epithelial cells is considered an essential event for the establishment of infection. We have previously shown that the PbHAD32 hydrolase is important in this early stage of the host-P. brasiliensis yeast cells interaction. The aim of this study was to further elucidate the role of PbHAD32 in conidial thermodimorphism and their interaction with lung epithelial cells. Analysis of the PbHAD32 gene expression revealed higher mRNA levels during the conidia to mycelia (C – M) germination when compared to the conidia to yeast (C – Y) transition. Moreover, PbHAD32 was consistently expressed at higher levels upon infection of lung epithelial cells, but to a greater extent when conidia germinated to produce mycelia. Interestingly, at this particular transitional stage, more conidia adhered to epithelial cells than when they were transiting to the yeast form. Altogether our data further corroborates the importance of PbHAD32 during initial adherence to host cells and suggest that the 32-KDa hydrolase may also participate at different stages of the C – M and C – Y conversions.COL0013709COL00009625application/pdfengOxford University PressBiología Celular y Molecular CIB U. de A. U. del RosarioMicología Médica y ExperimentalOxford, Inglaterrainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARTArtículo de investigaciónhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc/2.5/co/http://purl.org/coar/access_right/c_abf2https://creativecommons.org/licenses/by-nc/4.0/The hydrolase PbHAD32 participates in the adherence of Paracoccidioides brasiliensis conidia to epithelial lung cellsParacoccidioidesExpresión GénicaGene ExpressionRegulación hacia AbajoDown-RegulationMed. Mycol.Medical Mycology533537505ORIGINALHernandezOrville_2012_HydrolaseAdherence.pdfHernandezOrville_2012_HydrolaseAdherence.pdfArtículo de investigaciónapplication/pdf218527http://bibliotecadigital.udea.edu.co/bitstream/10495/24122/1/HernandezOrville_2012_HydrolaseAdherence.pdfd6e363fefd4b58d1cc15ed962176c377MD51CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8933http://bibliotecadigital.udea.edu.co/bitstream/10495/24122/2/license_rdfc0c92b0ffc8b7d22d9cf56754a416a76MD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81748http://bibliotecadigital.udea.edu.co/bitstream/10495/24122/3/license.txt8a4605be74aa9ea9d79846c1fba20a33MD5310495/24122oai:bibliotecadigital.udea.edu.co:10495/241222022-04-22 10:21:53.607Repositorio Institucional Universidad de Antioquiaandres.perez@udea.edu.coTk9URTogUExBQ0UgWU9VUiBPV04gTElDRU5TRSBIRVJFClRoaXMgc2FtcGxlIGxpY2Vuc2UgaXMgcHJvdmlkZWQgZm9yIGluZm9ybWF0aW9uYWwgcHVycG9zZXMgb25seS4KCk5PTi1FWENMVVNJVkUgRElTVFJJQlVUSU9OIExJQ0VOU0UKCkJ5IHNpZ25pbmcgYW5kIHN1Ym1pdHRpbmcgdGhpcyBsaWNlbnNlLCB5b3UgKHRoZSBhdXRob3Iocykgb3IgY29weXJpZ2h0Cm93bmVyKSBncmFudHMgdG8gRFNwYWNlIFVuaXZlcnNpdHkgKERTVSkgdGhlIG5vbi1leGNsdXNpdmUgcmlnaHQgdG8gcmVwcm9kdWNlLAp0cmFuc2xhdGUgKGFzIGRlZmluZWQgYmVsb3cpLCBhbmQvb3IgZGlzdHJpYnV0ZSB5b3VyIHN1Ym1pc3Npb24gKGluY2x1ZGluZwp0aGUgYWJzdHJhY3QpIHdvcmxkd2lkZSBpbiBwcmludCBhbmQgZWxlY3Ryb25pYyBmb3JtYXQgYW5kIGluIGFueSBtZWRpdW0sCmluY2x1ZGluZyBidXQgbm90IGxpbWl0ZWQgdG8gYXVkaW8gb3IgdmlkZW8uCgpZb3UgYWdyZWUgdGhhdCBEU1UgbWF5LCB3aXRob3V0IGNoYW5naW5nIHRoZSBjb250ZW50LCB0cmFuc2xhdGUgdGhlCnN1Ym1pc3Npb24gdG8gYW55IG1lZGl1bSBvciBmb3JtYXQgZm9yIHRoZSBwdXJwb3NlIG9mIHByZXNlcnZhdGlvbi4KCllvdSBhbHNvIGFncmVlIHRoYXQgRFNVIG1heSBrZWVwIG1vcmUgdGhhbiBvbmUgY29weSBvZiB0aGlzIHN1Ym1pc3Npb24gZm9yCnB1cnBvc2VzIG9mIHNlY3VyaXR5LCBiYWNrLXVwIGFuZCBwcmVzZXJ2YXRpb24uCgpZb3UgcmVwcmVzZW50IHRoYXQgdGhlIHN1Ym1pc3Npb24gaXMgeW91ciBvcmlnaW5hbCB3b3JrLCBhbmQgdGhhdCB5b3UgaGF2ZQp0aGUgcmlnaHQgdG8gZ3JhbnQgdGhlIHJpZ2h0cyBjb250YWluZWQgaW4gdGhpcyBsaWNlbnNlLiBZb3UgYWxzbyByZXByZXNlbnQKdGhhdCB5b3VyIHN1Ym1pc3Npb24gZG9lcyBub3QsIHRvIHRoZSBiZXN0IG9mIHlvdXIga25vd2xlZGdlLCBpbmZyaW5nZSB1cG9uCmFueW9uZSdzIGNvcHlyaWdodC4KCklmIHRoZSBzdWJtaXNzaW9uIGNvbnRhaW5zIG1hdGVyaWFsIGZvciB3aGljaCB5b3UgZG8gbm90IGhvbGQgY29weXJpZ2h0LAp5b3UgcmVwcmVzZW50IHRoYXQgeW91IGhhdmUgb2J0YWluZWQgdGhlIHVucmVzdHJpY3RlZCBwZXJtaXNzaW9uIG9mIHRoZQpjb3B5cmlnaHQgb3duZXIgdG8gZ3JhbnQgRFNVIHRoZSByaWdodHMgcmVxdWlyZWQgYnkgdGhpcyBsaWNlbnNlLCBhbmQgdGhhdApzdWNoIHRoaXJkLXBhcnR5IG93bmVkIG1hdGVyaWFsIGlzIGNsZWFybHkgaWRlbnRpZmllZCBhbmQgYWNrbm93bGVkZ2VkCndpdGhpbiB0aGUgdGV4dCBvciBjb250ZW50IG9mIHRoZSBzdWJtaXNzaW9uLgoKSUYgVEhFIFNVQk1JU1NJT04gSVMgQkFTRUQgVVBPTiBXT1JLIFRIQVQgSEFTIEJFRU4gU1BPTlNPUkVEIE9SIFNVUFBPUlRFRApCWSBBTiBBR0VOQ1kgT1IgT1JHQU5JWkFUSU9OIE9USEVSIFRIQU4gRFNVLCBZT1UgUkVQUkVTRU5UIFRIQVQgWU9VIEhBVkUKRlVMRklMTEVEIEFOWSBSSUdIVCBPRiBSRVZJRVcgT1IgT1RIRVIgT0JMSUdBVElPTlMgUkVRVUlSRUQgQlkgU1VDSApDT05UUkFDVCBPUiBBR1JFRU1FTlQuCgpEU1Ugd2lsbCBjbGVhcmx5IGlkZW50aWZ5IHlvdXIgbmFtZShzKSBhcyB0aGUgYXV0aG9yKHMpIG9yIG93bmVyKHMpIG9mIHRoZQpzdWJtaXNzaW9uLCBhbmQgd2lsbCBub3QgbWFrZSBhbnkgYWx0ZXJhdGlvbiwgb3RoZXIgdGhhbiBhcyBhbGxvd2VkIGJ5IHRoaXMKbGljZW5zZSwgdG8geW91ciBzdWJtaXNzaW9uLgo=