Legume lectins — a large family of homologous proteins

Sharon, Nathan; Lis, Halina

doi:10.1096/fasebj.4.14.2227211

Cited by 419 publications

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“…To test the potential relationship of ERGIC-53 to leguminous lectins we generated two mutants in ERGIC-53 myc/6xHis: N156 with N156 changed to A, and AD120/121 was changed to VA (for simplicity called D121 in this study). Figure 1 shows a sequence alignment of the putative carbohydrate binding site of ERGIC-53 with that of two leguminous lectins: Lathyrus ochrus isolectin I (LOL I) and Erythrina corallodendron lectin (ECoRL) (Sharon and Lis, 1990; three-dimensional structures with their ligands have been determined, LOL I with mannose, and ECoRL with galactose (Bourne et al, 1990;Shaanan et al, 1991). The location of the conserved residues D121 and N156 of ERGIC-53 are indicated in Figure 1 with a diamond symbol.…”

Section: Ergic-53 Mutants Containing An N-terminalmentioning

confidence: 99%

“…These findings provide the first direct experimental evidence for a lectin function of ERGIC-53. To test the hypothesis that ERGIC-53 may be a functional homologue of leguminous lectins , we substituted N156 of ERGIC-53, which is conserved and essential in the carbohydrate binding site of leguminous lectins (Sharon and Lis, 1990;van Eijsden et al, 1992;Mirkov and Chrispeels, 1993). A second mutation that also should affect the binding site was generated to confirm the first mutation.…”

Section: Introductionmentioning

confidence: 99%

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ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

Itin

Roche

Monsigny

et al. 1996

MBoC

166

148

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Based on sequence homologies with leguminous lectins, the intermediate compartment marker proposed to be a member of a putative new class of animal lectins associated with the secretory pathway. Independently, a promyelocytic protein, MR60, was purified by mannose-column chromatography, and a cDNA was isolated that matched MR60 peptide sequences. This cDNA was identical to that of and homologies with the animal lectin family of the galectins were noticed. Not all peptide sequences of MR60, however, were found in ERGIC-53, raising the possibility that another protein associated with ERGIC-53 may possess the lectin activity. Here, we provide the first direct evidence for a lectin function of ERGIC-53. Overexpressed ERGIC-53 binds to a mannose column in a calcium-dependent manner and also co-stains with mannosylated neoglycoprotein in a morphological binding assay. By using a sequential elution protocol we show that ERGIC-53 has selectivity for mannose and low affinity for glucose and GlcNAc, but no affinity for galactose. To experimentally address the putative homology of ERGIC-53 to leguminous lectins, a highly conserved protein family with an invariant asparagine essential for carbohydrate binding, we substituted the corresponding asparagine in ERGIC-53. This mutation, as well as a mutation affecting a second site in the putative carbohydrate recognition domain, abolished mannosecolumn binding and co-staining with mannosylated neoglycoprotein. These findings establish ERGIC-53 as a lectin and provide functional evidence for its relationship to leguminous lectins. Based on its monosaccharide specificity, domain organization, and recycling properties, we propose ERGIC-53 to function as a sorting receptor for glycoproteins in the early secretory pathway.

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Section: Ergic-53 Mutants Containing An N-terminalmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

Itin

Roche

Monsigny

et al. 1996

MBoC

166

148

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“…Several legume species are also known to contain two or more lectins. However, in all cases the different lectins clearly belong to the family of legume lectins [16]. Similarly, the different lectins found in elderberry (Sambucus sp.)…”

Section: Discussionmentioning

confidence: 66%

Isolation and partial characterization of a small chitin‐binding lectin from mistletoe (Viscum album)

et al. 1996

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In this report we present evidence that mistletoe contains besides the three above-mentioned type 2 RIP/lectins also a small agglutinin, which on the basis of its structure and specificity can be classified in the group of chitin-binding plant lectins composed of hevein domains [9]. The discovery of the novel agglutinin not only demonstrates that mistletoe contains two groups of totally different lectins, but also raises the question of whether this new lectin possibly contributes either positively or negatively to the therapeutic effects of mistletoe preparations. Since a similar chitin-binding lectin from the rhizomes of stinging nettle (Urtica dioica) is a potent superantigen in mice [10], the latter question is certainly relevant.

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“…4) and were essentially the same as those reported for the previously described ECorL mutants (Adar & Sharon, 1996) as well as for other legume lectins, e.g., Con A (Nicolau et al, 1969;Reed & Cohn, 1970), demonstrating that, in the above three mutants, Mn2+ is in the usual octahedral environment. The importance of the metal ions for both activity and stabilization of the legume lectins has been well established (Sharon & Lis, 1990;Emmerich et al, 1994;Bouckaert et al, 1995). The fact that these mutants have a normal metal content and normal Mn2+ ESR spectra may thus be taken as evidence that the overall topology of the metal sites is unchanged.…”

Section: Metal Ion Analvsesmentioning

confidence: 99%

“…The best-characterized lectins are those of the legumes (Sharon recognition in a variety of biological systems and are widely em-& Lis, 1990;Jordan & Goldstein, 1994;Konami et al, 1995). They ployed in biomedical research as carbohydrate-specific reagents.…”

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confidence: 99%

Structural features of the combining site region of Erythrina corallodendron lectin: Role of tryptophan 135

et al. 1998

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The role of Trp 135 and Tyr 108 in the combining site of Erythrina corallodendron lectin (ECorL) was investigated by physicochemical characterization of mutants obtained by site‐directed mutagenesis, hemagglutination‐inhibition studies, and molecular modeling, including dynamics simulations. The findings demonstrate that Trp 135 in ECorL: (1) is required for the tight binding of Ca2+ and Mn2+ to the lectin because mutation of this residue into alanine results in loss of these ions upon dialysis and concomitant reversible inactivation of the mutant; (2) contributes to the high affinity of methyl α‐N‐dansylgalactosaminide (MeαGalNDns) to the lectin; and (3) is solely responsible for the fluorescence energy transfer between the aromatic residues of the lectin and the dansyl group in the ECorL‐MeαGalNDns complex. Docking of MeαGalNDns into the combining site of the lectin reveals that the dansyl moiety is parallel with the indole of Trp 135, as required for efficient fluorescence energy transfer, in one of the two possible conformations that this ligand assumes in the bound state. In the W135A mutant, which still binds MeαGalNDns strongly, the dansyl group may partially insert itself into the place formerly occupied by Trp 135, a process that from dynamics simulations does not appear to be energetically favored unless the loop containing this residue assumes an open conformation. However, a small fraction of the W135A molecules must be able to bind MeαGalNDns in order to explain the relatively high affinity, as compared to galactose, still remaining for this ligand. A model for the molecular events leading to inactivation of the W135A mutant upon demetallization is also presented in which the cis‐trans isomerization of the Ala 88‐Asp 89 peptide bond, observed in high‐temperature dynamics simulations, appears not to be a required step.

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Legume lectins — a large family of homologous proteins

Cited by 419 publications

References 0 publications

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

Isolation and partial characterization of a small chitin‐binding lectin from mistletoe (Viscum album)

Structural features of the combining site region of Erythrina corallodendron lectin: Role of tryptophan 135

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