%0 Journal Article %A Reyes-López, Magda %A Bermúdez-Cruz, Rosa María %A Avila, Eva E. %A de la Garza, Mireya %T Acetaldehyde/alcohol dehydrogenase-2 (EhADH2) and clathrin are involved in internalization of human transferrin by Entamoeba histolytica %D 2011 %J Microbiology, %V 157 %N 1 %P 209-219 %@ 1465-2080 %R https://doi.org/10.1099/mic.0.040063-0 %K Tf, transferrin %K GAPDH, glyceraldehyde-3-phosphate dehydrogenase %K HRP, horseradish peroxidase %K TRITC, tetramethylrhodamine isothiocyanate %K TfR, transferrin receptor %K EhADH2, Entamoeba histolytica acetaldehyde/alcohol dehydrogenase-2 %K Ab, antibody %K holoTf, holotransferrin %K Lf, lactoferrin %K ECM, extracellular matrix %K EhTfbp, Entamoeba histolytica holoTf-binding protein %I Microbiology Society, %X Transferrin (Tf) is a host glycoprotein capable of binding two ferric-iron ions to become holotransferrin (holoTf), which transports iron in to all cells. Entamoeba histolytica is a parasitic protozoan able to use holoTf as a sole iron source in vitro. The mechanism by which this parasite scavenges iron from holoTf is unknown. An E. histolytica holoTf-binding protein (EhTfbp) was purified by using an anti-human transferrin receptor (TfR) monoclonal antibody. EhTfbp was identified by MS/MS analysis and database searches as E. histolytica acetaldehyde/alcohol dehydrogenase-2 (EhADH2), an iron-dependent enzyme. Both EhTfbp and EhADH2 bound holoTf and were recognized by the anti-human TfR antibody, indicating that they correspond to the same protein. It was found that the amoebae internalized holoTf through clathrin-coated pits, suggesting that holoTf endocytosis could be important for the parasite during colonization and invasion of the intestinal mucosa and liver. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.040063-0