Lectin mammalian

C-type lectins Characterized by a Ca +-dependent carbohydrate recognition domain (CRD) includes the mammalian asialoglycoprotein receptor, the selectins, and the mannosebinding protein... 

TES-32 is the most abundant single protein product secreted by the parasite. It is also heavily labelled by surface iodination of live larvae (Maizels et al., 1984, 1987), and is known by monoclonal antibody reactivity to be expressed in the cuticular matrix of the larval parasite (Page et al, 1992a). TES-32 was cloned by matching peptide sequence derived from gel-purified protein to an expressed sequence tag (EST) dataset of randomly selected clones from a larval cDNA library (Loukas et al., 1999). Because of the high level of expression of TES-32 mRNA, clones encoding this protein were repeatedly sequenced and deposited in the dataset (Tetteh et al., 1999). Full sequence determination showed a major domain with similarity to mammalian C-type (calcium-dependent) lectins (C-TLs), together with shorter N-terminal tracts rich in cysteine and threonine residues. Native TES-32 was then shown to bind to immobilized monosaccharides in a calcium-dependent manner (Loukas et al., 1999). 

The deprotected lactosides were evaluated as inhibitors against lectin binding in a solid-phase inhibition assay with immobilized ASF on the surface of microtiter plate wells, mimicking cell-surface presentation, while mammalian galectins-1, -3, and -5 were in solution. Strong multivalency effects and selectivity were observed for the... 

Bloc, A. et al., An invertebrate defense molecule activates membrane conductance in mammalian cells by means of its lectin-like domain, Dev. Comp. Immunol., 26, 35, 2002. 

There are many glycosylation mutants of cultured mammalian cells and yeast. They have been selected as rare survivors of treatments that kill cells expressing a particular carbohydrate or glycoprotein at the cell surface. For example, plants produce a variety of proteins, called lectins, which bind to cell surface oligosaccharides. Lectins are toxic to mammalian cells. They can be used to select for mutants that no longer bind the lectin because they lack a particular carbohydrate at the cell surface. Such glycosylation mutants have low amounts of glycoproteins that require carbohydrates for stable expression. 

Duclermortier, P., Lardans, V., Serra, E., Trottein, F. and Dissous, C. (1 999) Biomphalaria glabrata embryonic cells express a protein with a domain homologous to the lectin domain of mammalian selectins. Parasitology Research 85, 481-486. 

Stanley, P. "Surface Carbohydrate Alterations of Mutant Mammalian Cells Selected for Resistance to Plant Lectins". Lennarz, W.J. Ed. In "Biochemistry of Proteoglycans and Glycoproteins", Plenum Publishing Co., New York, (in press). 

Kilpatrick, D. C., Pusztai, A., Grant, G., et al. Tomato lectin resists digestion in the mammalian alimentary canal and binds to intestinal villi without deleterious effects. 

Because they are easily accessible, glycans displayed on the surface of mammalian cells provide enormous opportunities to bind to many microbial pathogens, ranging from viruses to molecular toxins and from pathogenic bacteria to parasites. In multivalent binding, multiple interactions between ligands and various receptors are common (Fig. 16.1). One representative example is ricin—a versatile and durable A-B-type toxin—in which one of the protein chains (the B chain) is a lectin that interacts and binds terminal galactose (Gal) on the surface of eukaryotic cells with multivalent interactions to facilitate entry of the other peptide chain (the A chain) into the cell to cause cellular death via the catalytic... 

Pilohello KT, Slawek DE, Mahal LK. A ratiometric lectin mi- 107. croarray approach to analysis of the dynamic mammalian gly-... 

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