Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp.
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | https://repositorio.unifesp.br/xmlui/handle/11600/62315 https://doi.org/10.1007/s42770-020-00253-w |
Resumo: | In recent years, the intensification of the use of immunosuppressive therapies has increased the incidence of invasive infections caused by opportunistic fungi. Considering that, the spread of azole resistance and amphotericin B (AmB) inefficiency against some clinical and environmental isolates has been described. Thus, to avoid a global problem when controlling fungal infections and critical failures in medicine, and food security, new approaches for drug target identification and for the development of new treatments that are more effective against pathogenic fungi are desired. Recent studies indicate that protein acetylation is present in hundreds of proteins of different cellular compartments and is involved in several biological processes, i.e., metabolism, translation, gene expression regulation, and oxidative stress response, from prokaryotes and eukaryotes, including fungi, dem- onstrating that lysine acetylation plays an important role in essential mechanisms. Lysine acetyltransferases (KATs) and lysine deacetylases (KDACs), the two enzyme families responsible for regulating protein acetylation levels, have been explored as drug targets for the treatment of several human diseases and infections. Aspergilli have on average 8 KAT genes and 11 KDAC genes in their genomes. This review aims to summarize the available knowledge about Aspergillus spp. azole resistance mechanisms and the role of lysine acetylation in the control of biological processes in fungi. We also want to discuss the lysine acetylation as a potential target for fungal infection treatment and drug target discovery. |
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Wassano, Natália SayuriLeite, Ariely Barbosa [UNIFESP]Reichert-Lima, FranquelineSchreiber, Angelica ZaninelliMoretti, Nilmar S. [UNIFESP]Damasio, Andréhttp://lattes.cnpq.br/21314727262026872021-11-26T21:42:52Z2021-11-26T21:42:52Z2020https://repositorio.unifesp.br/xmlui/handle/11600/62315https://doi.org/10.1007/s42770-020-00253-wIn recent years, the intensification of the use of immunosuppressive therapies has increased the incidence of invasive infections caused by opportunistic fungi. Considering that, the spread of azole resistance and amphotericin B (AmB) inefficiency against some clinical and environmental isolates has been described. Thus, to avoid a global problem when controlling fungal infections and critical failures in medicine, and food security, new approaches for drug target identification and for the development of new treatments that are more effective against pathogenic fungi are desired. Recent studies indicate that protein acetylation is present in hundreds of proteins of different cellular compartments and is involved in several biological processes, i.e., metabolism, translation, gene expression regulation, and oxidative stress response, from prokaryotes and eukaryotes, including fungi, dem- onstrating that lysine acetylation plays an important role in essential mechanisms. Lysine acetyltransferases (KATs) and lysine deacetylases (KDACs), the two enzyme families responsible for regulating protein acetylation levels, have been explored as drug targets for the treatment of several human diseases and infections. Aspergilli have on average 8 KAT genes and 11 KDAC genes in their genomes. This review aims to summarize the available knowledge about Aspergillus spp. azole resistance mechanisms and the role of lysine acetylation in the control of biological processes in fungi. We also want to discuss the lysine acetylation as a potential target for fungal infection treatment and drug target discovery.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)FAPESP: 2018/09948-0CNPq: 424729/2018engSBMBrazilian Journal of MicrobiologyDrug resistanceLysine acetylationKATsKDACsAspergillus spp.Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp.info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPEscola Paulista de Medicina (EPM)Microbiologia e ImunologiaOutraMicrobiologia, Imunologia e ParasitologiaORIGINALWassano et al 2020.pdfWassano et al 2020.pdfapplication/pdf561945${dspace.ui.url}/bitstream/11600/62315/1/Wassano%20et%20al%202020.pdfbfee305105672305e21fa89831d68259MD51open 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bGEgbGVnaXNsYcOnw6NvIGF1dG9yYWwsIMOpIHByb2liaWRvLiAgCgo3LiBBdGVzdGEgcXVlIGEgT2JyYSBzdWJtZXRpZGEgbsOjbyBjb250w6ltIHF1YWxxdWVyIGluZm9ybWHDp8OjbyBjb25maWRlbmNpYWwgc3VhIG91IGRlIHRlcmNlaXJvcy4KCjguIEF0ZXN0YSBxdWUgbyB0cmFiYWxobyBzdWJtZXRpZG8gw6kgb3JpZ2luYWwgZSBmb2kgZWxhYm9yYWRvIHJlc3BlaXRhbmRvIG9zIHByaW5jw61waW9zIGRhIG1vcmFsIGUgZGEgw6l0aWNhIGUgbsOjbyB2aW9sb3UgcXVhbHF1ZXIgZGlyZWl0byBkZSBwcm9wcmllZGFkZSBpbnRlbGVjdHVhbCwgc29iIHBlbmEgZGUgcmVzcG9uZGVyIGNpdmlsLCBjcmltaW5hbCwgw6l0aWNhIGUgcHJvZmlzc2lvbmFsbWVudGUgcG9yIG1ldXMgYXRvczsKCjkuIEF0ZXN0YSBxdWUgYSB2ZXJzw6NvIGRvIHRyYWJhbGhvIHByZXNlbnRlIG5vIGFycXVpdm8gc3VibWV0aWRvIMOpIGEgdmVyc8OjbyBkZWZpbml0aXZhIHF1ZSBpbmNsdWkgYXMgYWx0ZXJhw6fDtWVzIGRlY29ycmVudGVzIGRhIGRlZmVzYSwgc29saWNpdGFkYXMgcGVsYSBiYW5jYSwgc2UgaG91dmUgYWxndW1hLCBvdSBzb2xpY2l0YWRhcyBwb3IgcGFydGUgZGUgb3JpZW50YcOnw6NvIGRvY2VudGUgcmVzcG9uc8OhdmVsOwoKMTAuIENvbmNlZGUgw6AgVW5pdmVyc2lkYWRlIEZlZGVyYWwgZGUgU8OjbyBQYXVsbyAoVU5JRkVTUCkgbyBkaXJlaXRvIG7Do28gZXhjbHVzaXZvIGRlIHJlYWxpemFyIHF1YWlzcXVlciBhbHRlcmHDp8O1ZXMgbmEgbcOtZGlhIG91IG5vIGZvcm1hdG8gZG8gYXJxdWl2byBwYXJhIHByb3DDs3NpdG9zIGRlIHByZXNlcnZhw6fDo28gZGlnaXRhbCwgZGUgYWNlc3NpYmlsaWRhZGUgZSBkZSBtZWxob3IgaWRlbnRpZmljYcOnw6NvIGRvIHRyYWJhbGhvIHN1Ym1ldGlkbywgZGVzZGUgcXVlIG7Do28gc2VqYSBhbHRlcmFkbyBzZXUgY29udGXDumRvIGludGVsZWN0dWFsLgoKQW8gY29uY2x1aXIgYXMgZXRhcGFzIGRvIHByb2Nlc3NvIGRlIHN1Ym1pc3PDo28gZGUgYXJxdWl2b3Mgbm8gUmVwb3NpdMOzcmlvIEluc3RpdHVjaW9uYWwgVU5JRkVTUCwgYXRlc3RvIHF1ZSBsaSBlIGNvbmNvcmRlaSBpbnRlZ3JhbG1lbnRlIGNvbSBvcyB0ZXJtb3MgYWNpbWEgZGVsaW1pdGFkb3MsIHNlbSBmYXplciBxdWFscXVlciByZXNlcnZhIGUgbm92YW1lbnRlIGNvbmZpcm1hbmRvIHF1ZSBjdW1wcm8gb3MgcmVxdWlzaXRvcyBpbmRpY2Fkb3Mgbm9zIGl0ZW5zIG1lbmNpb25hZG9zIGFudGVyaW9ybWVudGUuCgpIYXZlbmRvIHF1YWxxdWVyIGRpc2NvcmTDom5jaWEgZW0gcmVsYcOnw6NvIGEgcHJlc2VudGUgbGljZW7Dp2Egb3UgbsOjbyBzZSB2ZXJpZmljYW5kbyBvIGV4aWdpZG8gbm9zIGl0ZW5zIGFudGVyaW9yZXMsIHZvY8OqIGRldmUgaW50ZXJyb21wZXIgaW1lZGlhdGFtZW50ZSBvIHByb2Nlc3NvIGRlIHN1Ym1pc3PDo28uIEEgY29udGludWlkYWRlIGRvIHByb2Nlc3NvIGVxdWl2YWxlIMOgIGNvbmNvcmTDom5jaWEgZSDDoCBhc3NpbmF0dXJhIGRlc3RlIGRvY3VtZW50bywgY29tIHRvZGFzIGFzIGNvbnNlcXXDqm5jaWFzIG5lbGUgcHJldmlzdGFzLCBzdWplaXRhbmRvLXNlIG8gc2lnbmF0w6FyaW8gYSBzYW7Dp8O1ZXMgY2l2aXMgZSBjcmltaW5haXMgY2FzbyBuw6NvIHNlamEgdGl0dWxhciBkb3MgZGlyZWl0b3MgYXV0b3JhaXMgcGF0cmltb25pYWlzIGUvb3UgY29uZXhvcyBhcGxpY8OhdmVpcyDDoCBPYnJhIGRlcG9zaXRhZGEgZHVyYW50ZSBlc3RlIHByb2Nlc3NvLCBvdSBjYXNvIG7Do28gdGVuaGEgb2J0aWRvIHByw6l2aWEgZSBleHByZXNzYSBhdXRvcml6YcOnw6NvIGRvIHRpdHVsYXIgcGFyYSBvIGRlcMOzc2l0byBlIHRvZG9zIG9zIHVzb3MgZGEgT2JyYSBlbnZvbHZpZG9zLgoKU2UgdGl2ZXIgcXVhbHF1ZXIgZMO6dmlkYSBxdWFudG8gYW9zIHRlcm1vcyBkZSBsaWNlbmNpYW1lbnRvIGUgcXVhbnRvIGFvIHByb2Nlc3NvIGRlIHN1Ym1pc3PDo28sIGVudHJlIGVtIGNvbnRhdG8gY29tIGEgYmlibGlvdGVjYSBkbyBzZXUgY2FtcHVzIChjb25zdWx0ZSBlbTogaHR0cHM6Ly9iaWJsaW90ZWNhcy51bmlmZXNwLmJyL2JpYmxpb3RlY2FzLWRhLXJlZGUpLiAKClPDo28gUGF1bG8sIFdlZCBOb3YgMjQgMjM6MTg6NTQgVVRDIDIwMjEuCg==Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-05-22T04:29:48Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.pt_BR.fl_str_mv |
Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp. |
title |
Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp. |
spellingShingle |
Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp. Wassano, Natália Sayuri Drug resistance Lysine acetylation KATs KDACs Aspergillus spp. |
title_short |
Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp. |
title_full |
Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp. |
title_fullStr |
Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp. |
title_full_unstemmed |
Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp. |
title_sort |
Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp. |
author |
Wassano, Natália Sayuri |
author_facet |
Wassano, Natália Sayuri Leite, Ariely Barbosa [UNIFESP] Reichert-Lima, Franqueline Schreiber, Angelica Zaninelli Moretti, Nilmar S. [UNIFESP] Damasio, André |
author_role |
author |
author2 |
Leite, Ariely Barbosa [UNIFESP] Reichert-Lima, Franqueline Schreiber, Angelica Zaninelli Moretti, Nilmar S. [UNIFESP] Damasio, André |
author2_role |
author author author author author |
dc.contributor.authorLattes.pt_BR.fl_str_mv |
http://lattes.cnpq.br/2131472726202687 |
dc.contributor.author.fl_str_mv |
Wassano, Natália Sayuri Leite, Ariely Barbosa [UNIFESP] Reichert-Lima, Franqueline Schreiber, Angelica Zaninelli Moretti, Nilmar S. [UNIFESP] Damasio, André |
dc.subject.por.fl_str_mv |
Drug resistance Lysine acetylation KATs KDACs Aspergillus spp. |
topic |
Drug resistance Lysine acetylation KATs KDACs Aspergillus spp. |
description |
In recent years, the intensification of the use of immunosuppressive therapies has increased the incidence of invasive infections caused by opportunistic fungi. Considering that, the spread of azole resistance and amphotericin B (AmB) inefficiency against some clinical and environmental isolates has been described. Thus, to avoid a global problem when controlling fungal infections and critical failures in medicine, and food security, new approaches for drug target identification and for the development of new treatments that are more effective against pathogenic fungi are desired. Recent studies indicate that protein acetylation is present in hundreds of proteins of different cellular compartments and is involved in several biological processes, i.e., metabolism, translation, gene expression regulation, and oxidative stress response, from prokaryotes and eukaryotes, including fungi, dem- onstrating that lysine acetylation plays an important role in essential mechanisms. Lysine acetyltransferases (KATs) and lysine deacetylases (KDACs), the two enzyme families responsible for regulating protein acetylation levels, have been explored as drug targets for the treatment of several human diseases and infections. Aspergilli have on average 8 KAT genes and 11 KDAC genes in their genomes. This review aims to summarize the available knowledge about Aspergillus spp. azole resistance mechanisms and the role of lysine acetylation in the control of biological processes in fungi. We also want to discuss the lysine acetylation as a potential target for fungal infection treatment and drug target discovery. |
publishDate |
2020 |
dc.date.issued.fl_str_mv |
2020 |
dc.date.accessioned.fl_str_mv |
2021-11-26T21:42:52Z |
dc.date.available.fl_str_mv |
2021-11-26T21:42:52Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://repositorio.unifesp.br/xmlui/handle/11600/62315 |
dc.identifier.doi.pt_BR.fl_str_mv |
https://doi.org/10.1007/s42770-020-00253-w |
url |
https://repositorio.unifesp.br/xmlui/handle/11600/62315 https://doi.org/10.1007/s42770-020-00253-w |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.pt_BR.fl_str_mv |
Brazilian Journal of Microbiology |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
SBM |
publisher.none.fl_str_mv |
SBM |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
bitstream.url.fl_str_mv |
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MD5 MD5 MD5 MD5 |
repository.name.fl_str_mv |
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repository.mail.fl_str_mv |
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1802764237585514496 |