Cell surface proteins of Entamoeba histolytica
Identifieur interne : 001B84 ( Main/Exploration ); précédent : 001B83; suivant : 001B85Cell surface proteins of Entamoeba histolytica
Auteurs : B. J. Mann [États-Unis] ; W. A. Petri Jr [États-Unis]Source :
- Parasitology Today [ 0169-4758 ] ; 1991.
English descriptors
- Teeft :
- Abscess, Amebic, Amebic adherence, Amino, Amino acid, Amino acid sequences, Amino acid substitutions, Amino acids, Amino terminus, Cdna, Cdna clone, Critical role, Cytoplasmic domain, Different genes encoding, Different members, Fibronectin receptor, Fusion protein, Galactose, Galactose lectin, Genes encoding, Hgl2, Hgll, Histolytica, Histolytica strains, Indirect immunofluorescence, Lectin, Liver abscess, Monoclonal, Monoclonal antibodies, Nonpathogenic, Nonpathogenic strains, Orfi fusion protein antiserum, Pathogenic, Pathogenic strain, Potential glycosylation sites, Potential sites, Residue numbers, Subunit.
Abstract
Abstract: To ask what is new in Entamoeba histolytica research, one need look no further than the surface of this protozoan parasite. In the past year the cloning and partial characterization of five different surface antigens have been reported, a remarkable result of international research efforts against amebiosis. One of these proteins is the first protective immunogen identified in the animal model of amebic liver abscess. Barbara Mann and William Petri review these recent results, propose a nomenclature for the gene family of E. histolytica galactose lectins and discuss the roles of the different surface proteins in adhesion.
Url:
DOI: 10.1016/0169-4758(91)90125-8
Affiliations:
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Le document en format XML
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<profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Abscess</term>
<term>Amebic</term>
<term>Amebic adherence</term>
<term>Amino</term>
<term>Amino acid</term>
<term>Amino acid sequences</term>
<term>Amino acid substitutions</term>
<term>Amino acids</term>
<term>Amino terminus</term>
<term>Cdna</term>
<term>Cdna clone</term>
<term>Critical role</term>
<term>Cytoplasmic domain</term>
<term>Different genes encoding</term>
<term>Different members</term>
<term>Fibronectin receptor</term>
<term>Fusion protein</term>
<term>Galactose</term>
<term>Galactose lectin</term>
<term>Genes encoding</term>
<term>Hgl2</term>
<term>Hgll</term>
<term>Histolytica</term>
<term>Histolytica strains</term>
<term>Indirect immunofluorescence</term>
<term>Lectin</term>
<term>Liver abscess</term>
<term>Monoclonal</term>
<term>Monoclonal antibodies</term>
<term>Nonpathogenic</term>
<term>Nonpathogenic strains</term>
<term>Orfi fusion protein antiserum</term>
<term>Pathogenic</term>
<term>Pathogenic strain</term>
<term>Potential glycosylation sites</term>
<term>Potential sites</term>
<term>Residue numbers</term>
<term>Subunit</term>
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<front><div type="abstract" xml:lang="en">Abstract: To ask what is new in Entamoeba histolytica research, one need look no further than the surface of this protozoan parasite. In the past year the cloning and partial characterization of five different surface antigens have been reported, a remarkable result of international research efforts against amebiosis. One of these proteins is the first protective immunogen identified in the animal model of amebic liver abscess. Barbara Mann and William Petri review these recent results, propose a nomenclature for the gene family of E. histolytica galactose lectins and discuss the roles of the different surface proteins in adhesion.</div>
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