TY - JOUR
T1 - Entamoeba dispar
T2 - Molecular characterization of the galactose/N-acetyl-D-galactosamine lectin
AU - Pillai, Dylan R.
AU - Kobayashi, Seiki
AU - Kain, Kevin C.
N1 - Funding Information:
This work was supported by Grant MT-12665 from the Medical Research Council of Canada (K.C.K.). K.C.K. is a recipient of a career award from the Ontario Ministry of Health and a Canada Research Chair. D.R.P. is funded by a MD/PhD Studentship from the Medical Research Council of Canada. We thank Dr. William Petri (University of Virginia) for the gift of monoclonal antibodies 1G7 and 8A3 and Dr. Kris Chadee (McGill University) for the gift of monoclonal antibody 3F4.
PY - 2001
Y1 - 2001
N2 - Amebiasis contributes to approximately 50 million cases of life-threatening dysentery world-wide. Comparison of the lectins from Entamoeba histolytica (pathogenic) and Entamoeba dispar (nonpathogenic) was undertaken to elucidate the differential roles of this molecule in invasion versus colonization. Surface lectin was less abundant on axenic E. dispar than on axenic E. histolytica, commensurate with differences in lectin (heavy and light subunits) RNA when assessed by semiquantitative RT-PCR. The 1G7 epitope, which falls within the immunodominant and immuno-protective cysteine-rich region (480-900), was absent on axenic E. dispar. Indirect immunofluorescence, transient transection of COS7, and immunoprecipitation demonstrated that the 1G7 epitope was conserved in the nonpathogenic lectin homologue but not exposed on live E. dispar trophozoites. Hg12 (E. histolytica) and Dhg12 (E. dispar) lectin homologues demonstrated comparable high-affinity binding to multivalent GalNAc19BSA. These data provide evidence for relative gene and conformational regulation of the E. dispar lectin.
AB - Amebiasis contributes to approximately 50 million cases of life-threatening dysentery world-wide. Comparison of the lectins from Entamoeba histolytica (pathogenic) and Entamoeba dispar (nonpathogenic) was undertaken to elucidate the differential roles of this molecule in invasion versus colonization. Surface lectin was less abundant on axenic E. dispar than on axenic E. histolytica, commensurate with differences in lectin (heavy and light subunits) RNA when assessed by semiquantitative RT-PCR. The 1G7 epitope, which falls within the immunodominant and immuno-protective cysteine-rich region (480-900), was absent on axenic E. dispar. Indirect immunofluorescence, transient transection of COS7, and immunoprecipitation demonstrated that the 1G7 epitope was conserved in the nonpathogenic lectin homologue but not exposed on live E. dispar trophozoites. Hg12 (E. histolytica) and Dhg12 (E. dispar) lectin homologues demonstrated comparable high-affinity binding to multivalent GalNAc19BSA. These data provide evidence for relative gene and conformational regulation of the E. dispar lectin.
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U2 - 10.1006/expr.2001.4672
DO - 10.1006/expr.2001.4672
M3 - Article
C2 - 11888250
AN - SCOPUS:0035728214
SN - 0014-4894
VL - 99
SP - 226
EP - 234
JO - Experimental Parasitology
JF - Experimental Parasitology
IS - 4
ER -
