NDLI: Identification of the 150-kDa surface antigen of Entamoeba histolytica as a galactose- and N -acetyl-d-galactosamine-inhibitable lectin

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Identification of the 150-kDa surface antigen of Entamoeba histolytica as a galactose- and N -acetyl-d-galactosamine-inhibitable lectin

Content Provider	Springer Nature Link
Author	Cheng, Xun Jia Tsukamoto, Hideo Kaneda, Yoshimasa Tachibana, Hiroshi
Copyright Year	1998
Abstract	A monoclonal antibody that reacts with a 150-kDa protein of Entamoeba histolytica on Western immunoblotting under nonreducing conditions inhibits the adherence and cytotoxicity of the ameba to mammalian cells in vitro. Affinity purification of solubilized trophozoites using the monoclonal antibody and electophoresis yielded three glycoproteins with molecular masses of 150, 170, and 260 kDa, suggesting the existence of either a common epitope or the close association of these proteins. The 260-kDa fraction was identified as the well-known galactose (Gal)- and N-acetyl-d-galactosamine (GalNAc)-inhibitable lectin. The 150- and 170-kDa fractions seemed to exist as part of a 380-kDa native protein with an isoelectric point of pH␣6.9. The N-terminal amino acid sequence of the 150-kDa protein was unique, indicating that the protein was not a degraded product of the 260-kDa lectin. By gel filtration, the 260-kDa lectin and the 150/170-kDa protein could be separated. When Chinese hamster ovary cells were pretreated with the fraction consisting of the 150/170-kDa protein the adherence of trophozoites to Chinese hamster ovary cells was competitively inhibited to a level equivalent to that observed for the 260-kDa lectin. The inhibitory effect was lost in the presence of Gal and GalNAc but was not influenced by the presence of glucose. These results demonstrate that the 150/170-kDa protein is a Gal/GalNAc-inhibitable lectin. The existence of a sugar-binding domain in the protein was confirmed by Gal-affinity chromatography.
Starting Page	632
Ending Page	639
Page Count	8
File Format	PDF
ISSN	09320113
Journal	Parasitology Research
Volume Number	84
Issue Number	8
e-ISSN	14321955
Language	English
Publisher	Springer-Verlag
Publisher Date	1998-07-27
Publisher Place	Berlin/Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Veterinary Parasitology Insect Science

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Subunit structure of the galactose and N-acetyl-D-galactosamine-inhibitable adherence lectin of Entamoeba histolytica.

Subunit structure of the galactose and N-acetyl-D-galactosamine-inhibitable adherence lectin of Entamoeba histolytica.

Differentiation of Entamoeba histolytica from E. dispar facilitated by monoclonal antibodies against a 150-kDa surface antigen

Protection of hamsters from amebic liver abscess formation by a monoclonal antibody to a 150-kDa surface lectin of Entamoeba histolytica

Galactose-specific adhesin and cytotoxicity of Entamoeba histolytica

Protection of hamsters from amebic liver abscess formation by immunization with the 150- and 170-kDa surface antigens of Entamoeba histolytica

Identification of the Entamoeba histolytica Galactose-Inhibitable Lectin Epitopes Recognized by Human Immunoglobulin A Antibodies following Cure of Amebic Liver Abscess

Humoral and mucosal iga antibody response to a recombinant 52-kda cysteine-rich portion of the entamoeba histolytica galactose-inhibitable lectin correlates with detection of native 170-kda lectin antigen in serum of patients.

Humoral and Mucosal IgA Antibody Response to a Recombinant 52-kDa Cysteine-Rich Portion of the Entamoeba histolytica Galactose-Inhibitable Lectin Correlates with Detection of Native 170-kDa Lectin Antigen in Serum of Patients with Amebic Colitis

Identification of the 150-kDa surface antigen of Entamoeba histolytica as a galactose- and N -acetyl-d-galactosamine-inhibitable lectin

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