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dc.contributor.authorPérez-Reytor, Diliana Celeste
dc.contributor.authorPavón, Alequis
dc.contributor.authorLópez-Joven, Carmen
dc.contributor.authorRamírez-Araya, Sebastián
dc.contributor.authorPeña-Varas, Carlos
dc.contributor.authorPlaza, Nicolás
dc.contributor.authorAlegría-Arcos, Melissa
dc.contributor.authorCorsini, Gino
dc.contributor.authorJaña, Víctor
dc.contributor.authorPavez, Leonardo
dc.contributor.authordel Pozo, Talía
dc.contributor.authorBastías, Roberto
dc.contributor.authorBlondel, Carlos J.
dc.contributor.authorRamírez, David
dc.contributor.authorGarcía, Katherine P.
dc.date.accessioned2020-10-20T19:10:38Z
dc.date.available2020-10-20T19:10:38Z
dc.date.issued2020-09-24
dc.identifier10.3389/fcimb.2020.00482
dc.identifier.issn22352988
dc.identifier.urihttps://hdl.handle.net/20.500.12728/7063
dc.description.abstractVibrio parahaemolyticus non-toxigenic strains are responsible for about 10% of acute gastroenteritis associated with this species, suggesting they harbor unique virulence factors. Zonula occludens toxin (Zot), firstly described in Vibrio cholerae, is a secreted toxin that increases intestinal permeability. Recently, we identified Zot-encoding genes in the genomes of highly cytotoxic Chilean V. parahaemolyticus strains, including the non-toxigenic clinical strain PMC53.7. To gain insights into a possible role of Zot in V. parahaemolyticus, we analyzed whether it could be responsible for cytotoxicity. However, we observed a barely positive correlation between Caco-2 cell membrane damage and Zot mRNA expression during PMC53.7 infection and non-cytotoxicity induction in response to purified PMC53.7-Zot. Unusually, we observed a particular actin disturbance on cells infected with PMC53.7. Based on this observation, we decided to compare the sequence of PMC53.7-Zot with Zot of human pathogenic species such as V. cholerae, Campylobacter concisus, Neisseria meningitidis, and other V. parahaemolyticus strains, using computational tools. The PMC53.7-Zot was compared with other toxins and identified as an endotoxin with conserved motifs in the N-terminus and a variable C-terminal region and without FCIGRL peptide. Notably, the C-terminal diversity among Zots meant that not all of them could be identified as toxins. Structurally, PMC53.7-Zot was modeled as a transmembrane protein. Our results suggested that it has partial 3D structure similarity with V. cholerae-Zot. Probably, the PMC53.7-Zot would affect the actin cytoskeletal, but, in the absence of FCIGRL, the mechanisms of actions must be elucidated.es_ES
dc.language.isoenes_ES
dc.publisherFrontiers Media S.A.es_ES
dc.subjectCampylobacter concisuses_ES
dc.subjectintestinal permeabilityes_ES
dc.subjectnon-toxigenic strainses_ES
dc.subjectProtein structure predictiones_ES
dc.subjectVibrio choleraees_ES
dc.subjectVibrio parahaemolyticuses_ES
dc.subjectZonula occludens toxines_ES
dc.subjectZotes_ES
dc.titleAnalysis of the Zonula occludens Toxin Found in the Genome of the Chilean Non-toxigenic Vibrio parahaemolyticus Strain PMC53.7es_ES
dc.typeArticlees_ES


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