Entamoeba histolytica: monoclonal antibody against the beta1 integrin-like molecule (140 kDa) inhibits cell adhesion to extracellular matrix components.

@article{Sengupta2001EntamoebaHM,
  title={Entamoeba histolytica: monoclonal antibody against the beta1 integrin-like molecule (140 kDa) inhibits cell adhesion to extracellular matrix components.},
  author={Krishanu Sengupta and Ver{\'o}nica Ivonne Hern{\'a}ndez-Ram{\'i}rez and Amelia Campos Rios and Ricardo Mondrag{\'o}n and Patricia Talam{\'a}s-Rohana},
  journal={Experimental parasitology},
  year={2001},
  volume={98 2},
  pages={83-9}
}
We describe a monoclonal antibody (3C10) against the beta1 integrin-like molecule which immunoprecipitates two polypeptides of 140 and 155 kDa from detergent-soluble extract of Entamoeba histolytica. The 140-kDa polypeptide has been described as a beta subunit of the amoebic fibronectin receptor as it is recognized by an anti-integrin beta1 (human) monoclonal antibody in immunoblot assay. The receptor molecules were localized with the 3C10 monoclonal antibody in intracellular and surface… CONTINUE READING