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Identification and partial purification of an Entamoeba histolytica membrane protein that binds fibronectin
P Talamás-Rohana1, J L Rosales-Encina, M C Gutiérrez
1Departamento de Patología Experimental, Centro de Investigación y de Estudios Avanzados, México DF, México.
Abstract:
A 37 kDa protein has been described as a putative receptor for fibronectin (Fn) on E. histolytica trophozoites (1). We have now identified a membrane protein that binds biotinylated fibronectin (BFn) with an apparent molecular weight of 140 kDa. Using BFn we were able to follow this protein during partial purification through DEAE-cellulose and Fn-Sepharose chromatography. Antisera prepared against a peptide corresponding to the deduced amino acid sequence for the putative receptor binding site for human Fn (2) recognized a protein with the same molecular weight. The purified protein was also recognized by this sera. We propose that this protein may function as a Fn receptor and will explore the possibility for it being an integrin.
Insights
Researchers identified a 140 kDa membrane protein that binds fibronectin (Fn) on E. histolytica trophozoites. This protein may function as a fibronectin receptor, potentially an integrin.
Area of Science:
- Cell biology
- Parasitology
- Molecular biology
Background:
- A previously identified 37 kDa protein was suggested as a fibronectin (Fn) receptor on E. histolytica trophozoites.
- The precise molecular identity and function of fibronectin receptors in E. histolytica remain incompletely understood.
Purpose of the Study:
- To identify and characterize the fibronectin receptor on E. histolytica trophozoites.
- To investigate the potential role of a 140 kDa membrane protein as a fibronectin receptor.
Main Methods:
- Binding assays using biotinylated fibronectin (BFn).
- Protein purification using DEAE-cellulose and Fn-Sepharose chromatography.
- Immunological detection using antisera against a peptide sequence of the putative Fn receptor.
Main Results:
- A 140 kDa membrane protein was identified that specifically binds BFn.
- This 140 kDa protein was successfully purified using chromatographic techniques.
- Antisera raised against a specific peptide sequence recognized and confirmed the identity of the purified 140 kDa protein.
Conclusions:
- A 140 kDa membrane protein is identified as a strong candidate for the fibronectin receptor in E. histolytica.
- Further investigation is warranted to confirm if this protein is an integrin and elucidate its precise function.