TY - JOUR
T1 - A Toll/IL-1R/resistance domain-containing thioredoxin regulates phagocytosis in Entamoeba histolytica
AU - Mancilla-Herrera, Ismael
AU - Méndez-Tenorio, Alfonso
AU - Wong-Baeza, Isabel
AU - Jiménez-Uribe, Alexis P.
AU - Alcántara-Hernández, Marcela
AU - Ocadiz-Ruiz, Ramon
AU - Moreno-Eutimio, Mario A.
AU - Arriaga-Pizano, Lourdes A.
AU - Lápez-Macías, Constantino
AU - González-Y-Merchand, Jorge
AU - Isibasi, Armando
N1 - Funding Information:
This work was supported by Mexican Social Security Institute (IMSS) health research founding (FIS/IMSS/PROT/MD09/732). Mancilla-Herrera received a scholarship by CONACyT (216244). Authors thanks to Ph. D Mario Rodriguez (Departamento de Infectómica y Patogénesis Molecular. Centro de Investigación y de Estudios Avanzados del IPN. A.P. 14–740 México, DF 07360, México) for technical advices, and Hisaki E. for the graphical design.
PY - 2012
Y1 - 2012
N2 - Background: Entamoeba histolytica is a protozoan parasite that infects humans and causes amebiasis affecting developing countries. Phagocytosis of epithelial cells, erythrocytes, leucocytes, and commensal microbiota bacteria is a major pathogenic mechanism used by this parasite. A Toll/IL-1R/Resistance (TIR) domain-containing protein is required in phagocytosis in the social ameba Dictyostelium discoideum, an ameba closely related to Entamoeba histolytica in phylogeny. In insects and vertebrates, TIR domain-containing proteins regulate phagocytic and cell activation. Therefore, we investigated whether E. histolytica expresses TIR domain-containing molecules that may be involved in the phagocytosis of erythrocytes and bacteria. Methods. Using in silico analysis we explored in Entamoeba histolytica databases for TIR domain containing sequences. After silencing TIR domain containing sequences in trophozoites by siRNA we evaluated phagocytosis of erythrocytes and bacteria. Results: We identified an E. histolytica thioredoxin containing a TIR-like domain. The secondary and tertiary structure of this sequence exhibited structural similarity to TIR domain family. Thioredoxin transcripts silenced in E. histolytica trophozoites decreased erythrocytes and E. coli phagocytosis. Conclusion: TIR domain-containing thioredoxin of E. histolytica could be an important element in erythrocytes and bacteria phagocytosis.
AB - Background: Entamoeba histolytica is a protozoan parasite that infects humans and causes amebiasis affecting developing countries. Phagocytosis of epithelial cells, erythrocytes, leucocytes, and commensal microbiota bacteria is a major pathogenic mechanism used by this parasite. A Toll/IL-1R/Resistance (TIR) domain-containing protein is required in phagocytosis in the social ameba Dictyostelium discoideum, an ameba closely related to Entamoeba histolytica in phylogeny. In insects and vertebrates, TIR domain-containing proteins regulate phagocytic and cell activation. Therefore, we investigated whether E. histolytica expresses TIR domain-containing molecules that may be involved in the phagocytosis of erythrocytes and bacteria. Methods. Using in silico analysis we explored in Entamoeba histolytica databases for TIR domain containing sequences. After silencing TIR domain containing sequences in trophozoites by siRNA we evaluated phagocytosis of erythrocytes and bacteria. Results: We identified an E. histolytica thioredoxin containing a TIR-like domain. The secondary and tertiary structure of this sequence exhibited structural similarity to TIR domain family. Thioredoxin transcripts silenced in E. histolytica trophozoites decreased erythrocytes and E. coli phagocytosis. Conclusion: TIR domain-containing thioredoxin of E. histolytica could be an important element in erythrocytes and bacteria phagocytosis.
KW - Bacteria phagocytosis
KW - Entamoeba histolytica phagocytosis
KW - Erythrocytes phagocytosis
KW - Toll/IL-1R/resistance domain
UR - http://www.scopus.com/inward/record.url?scp=84867126224&partnerID=8YFLogxK
U2 - 10.1186/1756-3305-5-224
DO - 10.1186/1756-3305-5-224
M3 - Artículo
SN - 1756-3305
VL - 5
JO - Parasites and Vectors
JF - Parasites and Vectors
IS - 1
M1 - 224
ER -