Isolation of a 220-Kilodalton Protein With Lectin Properties From a Virulent Strain of Entamoeba histolytica

A 220-kilodalton (kDa) protein with lectin properties was isolated from Entamoeba histolytica strain HM1:IMSS and was purified by Sepharose 4B chromatography and electroelution from 5% SDS-polyacrylamide gels. The protein contains 9% carbohydrate by weight; is rich in hydrophobic residues; and is ve...

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Bibliographic Details
Published in:The Journal of infectious diseases 1987-11, Vol.156 (5), p.790-797
Main Authors: Rosales-Encina, José Luis, Meza, Isaura, López-De-León, Alfredo, Talamás-Rohana, Patricia, Rojkind, Marcos
Format: Article
Language:English
Subjects:
Adhesiveness
Amino Acids - analysis
Animals
Antibodies
Carbohydrates - pharmacology
Cell membranes
Cells, Cultured
Cellulose nitrate
Cultured cells
Entamoeba histolytica
Entamoeba histolytica - metabolism
Entamoeba histolytica - pathogenicity
Entamoeba histolytica - physiology
Erythrocytes
Gels
Hemagglutination - drug effects
Lectins
Membrane Proteins - analysis
Membrane Proteins - isolation & purification
Membrane Proteins - pharmacology
Molecular Weight
Protein Binding
Room temperature
Sugars
Trophozoites
Virulence
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Summary:A 220-kilodalton (kDa) protein with lectin properties was isolated from Entamoeba histolytica strain HM1:IMSS and was purified by Sepharose 4B chromatography and electroelution from 5% SDS-polyacrylamide gels. The protein contains 9% carbohydrate by weight; is rich in hydrophobic residues; and is very immunogenic in mice, hamsters, and rabbits. The protein binds to fixed monolayers of MDCK cells and inhibits trophozoite attachment to the cultured cells. The 220-kDa protein agglutinates human erythrocytes, and agglutination is inhibited by micro molar concentrations of hyaluronic acid, chitin, chitinderived products (chitotriose), and antibodies to the purified protein. The 220-kDa protein is recognized by an antibody to the membrane but not by antibodies to other subcellular fractions. We therefore suggest that this 220-kDa protein with lectin properties is a component of the plasma membrane and could be one of the putative “receptor” molecules involved in cell and/or matrix attachment.
ISSN:0022-1899
1537-6613
DOI:10.1093/infdis/156.5.790