Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.4.3 (phospholipase C)
 18,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lipophosphoglycan has recently been demonstrated on the cell surface of Entamoeba histolytica strain HM-1:IMSS. A monoclonal antibody against this molecule had failed to react with some other strains of E. histolytica, including the strain Rahman. To determine if a structurally distinct lipophosphoglycan existed in Rahman, [3H]galactose-labeled glycoconjugates were electrophoresed through sodium dodecyl sulfate polyacrylamide gel electrophoresis. The electrophoretic pattern in Rahman was very different compared to that obtained with strains HM-1:IMSS and 200:NIH. A number of experiments including sensitivity to mild acid, nitrous acid and phosphoinositol-specific phospholipase C suggest that the Rahman glycoconjugate is indeed a lipophosphoglycan-like molecule but distinctly different from that of HM-1:IMSS. Mild acid-treated glycoconjugates from Rahman and HM-1:IMSS revealed the presence of neutral trisaccharides and monosaccharides in Rahman but not in HM-1:IMSS. Human immune sera from amoebiasis patients and a polyclonal antibody against HM-1:IMSS lipophosphoglycan both recognized Rahman glycoconjugate. Thus, while lipophosphoglycan molecules from the two strains share common epitopes, they are clearly distinct from each other. Molecules bearing resemblance to lipophosphoglycan could not be detected in other Entamoeba species, namely Entamoeba invadens and Entamoeba moshkovskii.
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PMID:Lipophosphoglycan is present in distinctly different form in different Entamoeba histolytica strains and absent in Entamoeba moshkovskii and Entamoeba invadens. 758 37

A panel of monoclonal antibodies was raised from mice immunized with a membrane preparation from Entamoeba histolytica, the pathogenic species causing invasive amebiasis in humans. Antibody EH5 gave a polydisperse band in immunoblots from membrane preparations from different E. histolytica strains, and a much weaker signal from two strains of the nonpathogenic species Entamoeba dispar. Although the exact chemical structure of the EH5 antigen is not yet known, the ability of the antigen to be metabolically radiolabeled with [32P]phosphate or [3H]glucose, its sensitivity to digestion by mild acid and phosphatidylinositol-specific phospholipase C, and its specific extraction from E. histolytica trophozoites by a method used to prepare lipophosphoglycans from Leishmania showed that it could be classified as an amebal lipophosphoglycan. Confocal immunofluorescence and immunogold labeling of trophozoites localized the antigen on the outer face of the plasma membrane and on the inner face of internal vesicle membranes. Antibody EH5 strongly agglutinated amebas in a similar way to concanavalin A (Con A), and Con A bound to immunoaffinity-purified EH5 antigen. Therefore, surface lipophosphoglycans may play an important role in the preferential agglutination of pathogenic amebas by Con A. The protective ability of antibody EH5 was tested in a passive immunization experiment in a severe combined immunodeficient (SCID) mouse model. Intrahepatic challenge of animals after administration of an isotype-matched control antibody or without treatment led to the development of a liver abscess in all cases, whereas 11 out of 12 animals immunized with the EH5 antibody developed no liver abscess. Our results demonstrate the importance and, for the first time, the protective capacity of glycan antigens on the surface of the amebas.
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PMID:Protection against invasive amebiasis by a single monoclonal antibody directed against a lipophosphoglycan antigen localized on the surface of Entamoeba histolytica. 934 13