Unnexins: Homologs of innexin proteins in Trypanosomatidae parasites

Vista sencilla de ítem
dc.contributor.authorGüiza, Juan
dc.contributor.authorGarcía, Aníbal
dc.contributor.authorArriagada, Javiera
dc.contributor.authorGutiérrez, Camila
dc.contributor.authorGonzález, Jorge
dc.contributor.authorMárquez-Miranda, Valeria
dc.contributor.authorAlegría-Arcos, Melissa
dc.contributor.authorDuarte, Yorley
dc.contributor.authorRojas, Maximiliano
dc.contributor.authorGonzález-Nilo, Fernando
dc.contributor.authorSáez, Juan C.
dc.contributor.authorVega, José L.
dc.date.accessioned2022-11-30T02:46:25Z
dc.date.available2022-11-30T02:46:25Z
dc.date.issued2022
dc.description.abstractLarge-pore channels, including those formed by connexin, pannexin, innexin proteins, are part of a broad family of plasma membrane channels found in vertebrates and invertebrates, which share topology features. Despite their relevance in parasitic diseases such as Chagas and malaria, it was unknown whether these large-pore channels are present in unicellular organisms. We identified 14 putative proteins in Trypanosomatidae parasites as presumptive homologs of innexin proteins. All proteins possess the canonical motif of the innexin family, a pentapeptide YYQWV, and 10 of them share a classical membrane topology of large-pore channels. A sequence similarity network analysis confirmed their closeness to innexin proteins. A bioinformatic model showed that a homolog of Trypanosoma cruzi (T. cruzi) could presumptively form a stable octamer channel with a highly positive electrostatic potential in the internal cavities and extracellular entrance due to the notable predominance of residues such as Arg or Lys. In vitro dye uptake assays showed that divalent cations-free solution increases YO-PRO-1 uptake and hyperosmotic stress increases DAPI uptake in epimastigotes of T. cruzi. Those effects were sensitive to probenecid. Furthermore, probenecid reduced the proliferation and transformation of T. cruzi. Moreover, probenecid or carbenoxolone increased the parasite sensitivity to antiparasitic drugs commonly used in therapy against Chagas. Our study suggests the existence of innexin homologs in unicellular organisms, which could be protein subunits of new large-pore channels in unicellular organisms.en_ES
dc.facultadFacultad de Cienciasen_ES
dc.file.nameGuiza_Unn2022.pdf
dc.identifier.doihttps://doi.org/10.1002/jcp.30626
dc.identifier.urihttp://repositoriobibliotecas.uv.cl/handle/uvscl/7362
dc.languageen
dc.publisherWiley
dc.rights© 2021 Wiley Periodicals LLC
dc.sourceJournal of Cellular Physiology
dc.subjectNEGLECTED TROPICAL DISEASESen_ES
dc.subjectCHAGAS DISEASESen_ES
dc.subjectSLEEPING SICKNESSen_ES
dc.titleUnnexins: Homologs of innexin proteins in Trypanosomatidae parasites
dc.typeArticulo
uv.departamentoCentro Interdisciplinario de Neurociencia de Valparaiso
uv.notageneralNo disponible para descarga

Archivos

Bloque original
Mostrando 1 - 1 de 1
Miniatura
Nombre:
Guiza_Unn2022_noaccesible_.pdf
Tamaño:
2.27 MB
Formato:
Adobe Portable Document Format
Descripción:
Descargar

Colecciones

Artículos investigadores UV