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...
- 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/
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UDEA2 |
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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 |
dc.type.coarversion.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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 |
dc.type.redcol.spa.fl_str_mv |
https://purl.org/redcol/resource_type/ART |
dc.type.local.spa.fl_str_mv |
Artículo de investigación |
format |
http://purl.org/coar/resource_type/c_2df8fbb1 |
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 |
dc.rights.uri.*.fl_str_mv |
http://creativecommons.org/licenses/by-nc/2.5/co/ |
dc.rights.accessrights.spa.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 |
dc.rights.creativecommons.spa.fl_str_mv |
https://creativecommons.org/licenses/by-nc/4.0/ |
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 https://creativecommons.org/licenses/by-nc/4.0/ |
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 http://bibliotecadigital.udea.edu.co/bitstream/10495/24122/2/license_rdf http://bibliotecadigital.udea.edu.co/bitstream/10495/24122/3/license.txt |
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d6e363fefd4b58d1cc15ed962176c377 c0c92b0ffc8b7d22d9cf56754a416a76 8a4605be74aa9ea9d79846c1fba20a33 |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 |
repository.name.fl_str_mv |
Repositorio Institucional Universidad de Antioquia |
repository.mail.fl_str_mv |
andres.perez@udea.edu.co |
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1812173152074072064 |
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= |