EspFu-mediated actin assembly enhances enteropathogenic escherichia coli adherence and activates host cell inflammatory signaling pathways

Full metadata record
DC FieldValueLanguage
dc.contributorLab. Bacteriologiapt_BR
dc.contributorLETA - Laboratório de Toxinologia Aplicadapt_BR
dc.contributor.authorMartins, Fernando Henriquept_BR
dc.contributor.authorKumar, Ashwanipt_BR
dc.contributor.authorAbe, Cecilia Maript_BR
dc.contributor.authorCarvalho, Eneaspt_BR
dc.contributor.authorNishiyama Junior, Milton Yutakapt_BR
dc.contributor.authorXing, Chaopt_BR
dc.contributor.authorSperandio, Vanessapt_BR
dc.contributor.authorElias, Waldir Pereirapt_BR
dc.date.accessioned2020-07-09T21:27:28Z-
dc.date.available2020-07-09T21:27:28Z-
dc.date.issued2020pt_BR
dc.identifier.citationMartins FH, Kumar A, Abe CM, Carvalho E, Nishiyama Junior MY, Xing C, et al. EspFu-mediated actin assembly enhances enteropathogenic escherichia coli adherence and activates host cell inflammatory signaling pathways. mBio. 2020 Apr;11(2):e00617-20. doi:10.1128/mBio.00617-20.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/3012-
dc.description.abstractThe translocation of effectors into the host cell through type 3 secretion systems (T3SS) is a sophisticated strategy employed by pathogenic bacteria to subvert host responses and facilitate colonization. Enteropathogenic Escherichia coli (EPEC) and enterohemorrhagic E. coli (EHEC) utilize the Tir and EspFu (also known as TccP) effectors to remodel the host cytoskeleton, culminating in the formation of attaching and effacing (AE) lesions on enterocytes. While some EPEC strains require tyrosine phosphorylation of Tir and recruitment of the host Nck to trigger actin polymerization, EHEC and certain EPEC strains, whose Tir is not phosphorylated, rely on the effector EspFu for efficient actin remodeling. Here, we investigated the role played by Tir-Nck and Tir-EspFu actin polymerization pathways during the infection of epithelial cells, as well as the host transcriptional response to the AE lesion formation induced by EPEC. We found that EspFu-mediated actin assembly promotes bacterial attachment and epithelial colonization more efficiently than Tir-Nck. Moreover, we showed that both actin polymerization mechanisms can activate inflammatory pathways and reverse the anti-inflammatory response induced by EPEC in epithelial cells. However, this activity is remarkably more evident in infections with EspFuexpressing EPEC strains. This study demonstrates the complex interactions between effector-mediated actin remodeling and inflammation. Different strains carry different combinations of these two effectors, highlighting the plasticity of pathogenic E. coli enteric infections. IMPORTANCE EPEC is among the leading causes of diarrheal disease worldwide. The colonization of the gut mucosa by EPEC results in actin pedestal formation at the site of bacterial attachment. These pedestals are referred to as attaching and effacing (AE) lesions. Here, we exploit the different molecular mechanisms used by EPEC to induce AE lesions on epithelial cells, showing that the effector EspFu is associated with increased bacterial attachment and enhanced epithelial colonization compared to the Tir-Nck pathway. Moreover, we also showed that actin pedestal formation can counterbalance the anti-inflammatory activity induced by EPEC, especially when driven by EspFu. Collectively, our findings provide new insights into virulence mechanisms employed by EPEC to colonize epithelial cells, as well as the host response to this enteric pathogen.pt_BR
dc.description.sponsorshipNational Institutes of Health (NIH)pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.format.extente00617-20pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofmBiopt_BR
dc.rightsOpen Accesspt_BR
dc.titleEspFu-mediated actin assembly enhances enteropathogenic escherichia coli adherence and activates host cell inflammatory signaling pathwayspt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1128/mBio.00617-20pt_BR
dc.identifier.urlhttps://doi.org/10.1128/mBio.00617-20pt_BR
dc.contributor.externalUniversity of Texas Southwestern Medical Center¦¦Estados Unidospt_BR
dc.identifier.citationvolume11pt_BR
dc.identifier.citationissue2pt_BR
dc.subject.keywordenteropathogenic E. colpt_BR
dc.subject.keywordEspFu/TccPpt_BR
dc.subject.keywordTir phosphorylationpt_BR
dc.subject.keywordpedestal formationpt_BR
dc.subject.keywordinflammationpt_BR
dc.relation.ispartofabbreviatedmBiopt_BR
dc.identifier.citationabntv. 11, n. 2, e00617-20, abr. 2020pt_BR
dc.identifier.citationvancouver2020 Apr;11(2):e00617-20pt_BR
dc.contributor.butantanMartins, Fernando Henrique|:Aluno|:Lab. Bacteriologia|:PrimeiroAutorpt_BR
dc.contributor.butantanAbe, Cecília Mari|:Pesquisador|:Lab. Bacteriologia|:pt_BR
dc.contributor.butantanCarvalho, Eneas|:Pesquisador|:Lab. Bacteriologia|:pt_BR
dc.contributor.butantanNishiyama Junior, Milton Yutaka|:Pesquisador|:Laboratório Especial de Toxinologia Aplicada (LETA)|:pt_BR
dc.contributor.butantanElias, Waldir Pereira|:Pesquisador|:Lab. Bacteriologia|:pt_BR
dc.sponsorship.butantanCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)¦¦001pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦08/52196-8pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦11/14103-0pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦13/17403-0pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦16/08401-2pt_BR
dc.sponsorship.butantanNational Institutes of Health (NIH)¦¦AI0530167pt_BR
dc.sponsorship.butantanNational Institutes of Health (NIH)¦¦AI05135pt_BR
dc.sponsorship.butantanNational Institutes of Health (NIH)¦¦AI077613pt_BR
dc.sponsorship.butantanNational Institutes of Health (NIH)¦¦572 AI114511pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.openairetypeArticle-
item.fulltextCom Texto completo-
item.grantfulltextopen-
item.languageiso639-1English-
crisitem.author.dept#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.dept#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.dept#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.dept#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.dept#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.dept#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.dept#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.dept#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.orcid#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.orcid#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.orcid0000-0003-0218-9372-
crisitem.author.orcid0000-0002-8052-0975-
crisitem.author.orcid0000-0002-2410-0562-
crisitem.author.orcid#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.orcid#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.orcid0000-0003-3470-5706-
crisitem.author.parentorg#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.parentorg#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.author.parentorg#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.journal.journalissn#PLACEHOLDER_PARENT_METADATA_VALUE#-
crisitem.journal.journaleissn#PLACEHOLDER_PARENT_METADATA_VALUE#-
Appears in Collections:Artigos de periódicos


Files in This Item:

10.1128.mBio.00617-20.pdf
Size: 6.32 MB
Format: Adobe PDF
View/Open
Show simple item record

The access to the publications deposited in this repository respects the licenses from journals and publishers.