RT info:eu-repo/semantics/article
T1 Ebulin l is internalized in cells by both clathrin-dependent and -independent mechanisms and does not require clathrin or dynamin for intoxication
A1 Iglesias Álvarez, María del Rosario
A1 Ferreras Rodríguez, José Miguel
A1 Llorente, Alicia
A1 Citores González, Lucía
K1 Apoptosis
K1 Proteins - Synthesis
K1 Proteinas
K1 Ribosomes - Structure
K1 Cell membranes
K1 Lectins
K1 Toxins
K1 Toxinas
K1 Toxicology
K1 Ribosome-inactivating protein
K1 Proteínas inactivadoras de ribosomas
K1 rRNA N-glycosylase
K1 2302 Bioquímica
K1 3214 Toxicología
AB Ebulin l is an A-B toxin, and despite the presence of a B chain, this toxin displays much less toxicity to cells than the potent A-B toxin ricin. Here, we studied the binding, mechanisms of endocytosis, and intracellular pathway followed by ebulin l and compared it with ricin. COS-1 cells and HeLa cells with inducible synthesis of a mutant dynamin (K44A) were used in this study. The transport of these toxins was measured using radioactively or fluorescently labeled toxins. The data show that ebulin l binds to cells to a lesser extent than ricin. Moreover, the expression of mutant dynamin does not affect the endocytosis, degradation, or toxicity of ebulin l. However, the inhibition of clathrin-coated pit formation by acidification of the cytosol reduced ebulin l endocytosis but not toxicity. Remarkably, unlike ricin, ebulin l is not transported through the Golgi apparatus to intoxicate the cells and ebulin l induces apoptosis as the predominant cell death mechanism. Therefore, after binding to cells, ebulin l is taken up by clathrin-dependent and -independent endocytosis into the endosomal/lysosomal system, but there is no apparent role for clathrin and dynamin in productive intracellular routing leading to intoxication.
PB MDPI
SN 2072-6651
YR 2021
FD 2021
LK https://uvadoc.uva.es/handle/10324/59917
UL https://uvadoc.uva.es/handle/10324/59917
LA eng
NO Toxins, 2021, Vol. 13, Nº. 2, 10
NO Producción Científica
DS UVaDOC
RD 12-jul-2024