Analysis of the Zonula occludens Toxin Found in the Genome of the Chilean Non-toxigenic Vibrio parahaemolyticus Strain PMC53.7
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Pérez Reytor, Diliana.
Pavón, Alequis
López Joven, Carmen.
Ramírez Araya, Sebastián.
Peña Varas, Carlos.
Plaza, Nicolás
Alegría Arcos, Melissa Constanza.
Corsini, Gino
Jaña Garay, Víctor Manuel.
Pavez, Leonardo
Pozo Delgado, Talia Del
Bastías, Roberto
Blondel, Carlos J.
Ramírez, David
García, Katherine
Pavón, Alequis
López Joven, Carmen.
Ramírez Araya, Sebastián.
Peña Varas, Carlos.
Plaza, Nicolás
Alegría Arcos, Melissa Constanza.
Corsini, Gino
Jaña Garay, Víctor Manuel.
Pavez, Leonardo
Pozo Delgado, Talia Del
Bastías, Roberto
Blondel, Carlos J.
Ramírez, David
García, Katherine
Datos de publicación (Editorial):
"Lixing Huang, Jimei University, China"
Materias (Palabras claves):
Fecha de publicación:
2020
Resumen:
Vibrio 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.
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