Analysis of the Zonula occludens Toxin Found in the Genome of the Chilean Non-toxigenic Vibrio parahaemolyticus Strain PMC53.7

dc.contributor.authorPerez-Reytor, D.
dc.contributor.authorPavon, A.
dc.contributor.authorLopez-Joven, C.
dc.contributor.authorRamirez-Araya, S.
dc.contributor.authorPena-Varas, C.
dc.contributor.authorPlaza, N.
dc.contributor.authorAlegria-Arcos, M.
dc.contributor.authorCorsini, G.
dc.contributor.authorJana, V.
dc.contributor.authorPavez, L.
dc.contributor.authordel Pozo, T.
dc.contributor.authorBastias, R.
dc.contributor.authorBlondel, C.J.
dc.contributor.authorRamirez, D.
dc.contributor.authorGarcia, K.
dc.date.accessioned2021-07-28T14:46:00Z
dc.date.available2021-07-28T14:46:00Z
dc.date.issued2020-09
dc.descriptionIndexación: Scopus.es
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. © Copyright © 2020 Pérez-Reytor, Pavón, Lopez-Joven, Ramírez-Araya, Peña-Varas, Plaza, Alegría-Arcos, Corsini, Jaña, Pavez, del Pozo, Bastías, Blondel, Ramírez and García.es
dc.description.urihttps://www.frontiersin.org/articles/10.3389/fcimb.2020.00482/full
dc.identifier.citationFrontiers in Cellular and Infection MicrobiologyOpen AccessVolume 1024 September 2020 Article number 482es
dc.identifier.doi10.3389/fcimb.2020.00482
dc.identifier.issn2235-2988
dc.identifier.urihttp://repositorio.unab.cl/xmlui/handle/ria/19533
dc.language.isoenes
dc.publisherFrontiers Media S.A.es
dc.rights.licenseAttribution 4.0 International (CC BY 4.0)
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectCampylobacter concisuses
dc.subjectintestinal permeabilityes
dc.subjectnon-toxigenic strainses
dc.subjectProtein structure predictiones
dc.subjectVibrio choleraees
dc.subjectVibrio parahaemolyticuses
dc.subjectZonula occludens toxines
dc.subjectZotes
dc.titleAnalysis of the Zonula occludens Toxin Found in the Genome of the Chilean Non-toxigenic Vibrio parahaemolyticus Strain PMC53.7es
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