Identification and partial purification of an Entamoeba histolytica membrane protein that binds fibronectin.
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.
Talamás-Rohana
P
P
Departamento de Patología Experimental, Centro de Investigación y de Estudios Avanzados, México DF, México.
Rosales-Encina
J L
JL
Gutiérrez
M C
MC
Hernández
V I
VI
D000595:Amino Acid Sequence; D000818:Animals; D000918:Antibody Specificity; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004748:Entamoeba histolytica / Q000737:chemistry* / Q000254:growth & development / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism*; D016023:Integrins; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000276:immunology; D015800:Protozoan Proteins / Q000302:isolation & purification* / Q000378:metabolism
D002352:Carrier Proteins; D005353:Fibronectins; D016023:Integrins; D010446:Peptide Fragments; D015800:Protozoan Proteins