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Entamoeba histolytica Contains a β1 Integrin‐like Molecule Similar to Fibronectin Receptors from Eukaryotic Cells
Author(s) -
TalamásRohana Patricia,
HernándezRamirez Veronica I.,
PerezGarcía Javier N.,
VenturaJuárez Javier
Publication year - 1998
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.1998.tb04549.x
Subject(s) - fibronectin , entamoeba histolytica , biology , polyclonal antibodies , extracellular matrix , integrin , receptor , microbiology and biotechnology , extracellular , cell surface receptor , western blot , antibody , biochemistry , gene , immunology
Entamoeba histolytica trophozoites do interact with extracellular matrix components in order to invade and finally destroy tissue. An important step in this interaction involves the binding of a 140‐kDa membrane protein that binds to fibronectin. The similarity of this amoebic receptor to fibronectin receptors from higher eukaryotic cells was defined by indirect immunofluorescence, western blot and immunohistochemistry. using polyclonal monospecific antibodies raised against the amoebic protein. These results suggest that lower eukaryotic cells have and use a β1 integrin‐like molecule as well as mechanisms similar to those present in higher eukaryotic cells during interaction with extracellular matrix components.