Enzyme-linked lectin assay (ELLA)

McCoy, J. Philip; Varani, James; Goldstein, Irwin J.

doi:10.1016/0014-4827(84)90359-8

Cited by 33 publications

(9 citation statements)

References 13 publications

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“…Lastly, L. amazonensis and L. infantum lysates were plated and incubated either with biotinylated MOA or purified anti-α-Gal antibody in an ELISA-type assay ( Figure 1 E). 27 As before, the presence of α-Gal was confirmed for both species, but to a greater degree for L. amazonensis . Preincubation with an α-galactosidase enzyme reduced binding by more than 90% ( Figure 1 F), showing that the terminal galactose residue is critical.…”

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confidence: 67%

Virus-like Particle Display of the α-Gal Carbohydrate for Vaccination against Leishmania Infection

et al. 2017

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Secreted and surface-displayed carbohydrates are essential for virulence and viability of many parasites, including for immune system evasion. We have identified the α-Gal trisaccharide epitope on the surface of the protozoan parasites Leishmania infantum and Leishmania amazonensis, the etiological agents of visceral and cutaneous leishmaniasis, respectively, with the latter bearing larger amounts of α-Gal than the former. A polyvalent α-Gal conjugate on the immunogenic Qβ virus-like particle was tested as a vaccine against Leishmania infection in a C57BL/6 α-galactosyltransferase knockout mouse model, which mimics human hosts in producing high titers of anti-α-Gal antibodies. As expected, α-Gal-T knockout mice infected with promastigotes of both Leishmania species showed significantly lower parasite load in the liver and slightly decreased levels in the spleen, compared with wild-type mice. Vaccination with Qβ–α-Gal nanoparticles protected the knockout mice against Leishmania challenge, eliminating the infection and proliferation of parasites in the liver and spleen as probed by qPCR. The α-Gal epitope may therefore be considered as a vaccine candidate to block human cutaneous and visceral leishmaniasis.

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confidence: 67%

Virus-like Particle Display of the α-Gal Carbohydrate for Vaccination against Leishmania Infection

et al. 2017

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“…In contrast to these results with the highly malignant cells, the same treatments were, taken together, much less effective with the low malignant cells. These cells contain far fewer surface a-D-galactopyranosyl residues than the highly malignant cells [14]. This suggests that mechanisms which are, at least in part, independent of a-D-g&iCtOpyranOSyl end groups play a greater role in the attachment of the low malignant cells than of the highly malignant cells.…”

Section: Discussionmentioning

confidence: 96%

Contribution of α-d-galactopyranosyl end groups to attachment of highly and low metastatic murine fibrosarcoma cells to various substrates

Grimstad

Varani

McCoy

1984

Experimental Cell Research

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There are much greater numbers of cell surface terminal, non-reducing alpha-D-galactorpyranosyl groups in highly malignant (metastatic) cells than are found in low malignant cells derived from the same murine fibrosarcoma. We have examined the contribution of these residues to attachment of the cells to various collagens and to plastic. Removal of these carbohydrate groups with alpha-galactosidase or blocking them with lectins from Griffonia simplicifolia seeds or with anti-blood group B antiserum all dramatically inhibited the attachment of both the highly malignant and the low malignant cells. Following removal with the enzyme, the alpha-D-galactopyranosyl end groups were rapidly resynthesized. This resynthesis was inhibited by tunicamycin, an inhibitor of de novo glycoprotein synthesis. This antibiotic also impaired cell attachment and, when used in addition to treatment with alpha-galactosidase, it inhibited cell attachment more than did treatment with the enzyme alone. The effects of all treatments on cell attachment were greater for the highly malignant than for the low malignant cells. With the latter cells, inhibition by lectin was seen only in the absence of serum, whereas the adhesion of highly malignant cells was affected in both the presence and the absence of serum. On their surface membrane the highly malignant cells express much more than do the low malignant cells of a glycoprotein that cross-reacts immunologically with laminin. The basement membrane glycoprotein laminin promotes cell attachment to collagen, and both glycoproteins contain terminal, non-reducing alpha-D-galactopyranosyl groups. Attachment of cells is a requirement for the formation of a metastasis, and thus the laminin-like molecule and the alpha-D-galactopyranosyl end groups (whether on the laminin-related moiety or on other cell surface molecules) may both be important for expression of the most malignant phenotype.

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“…Two-site ELLA experiments were employed to test the crosslinking ability of the multilactosides, first with peanut agglutinin. In this case, the relative potency per lactoside ranged from 2.1 to 3.2 (McCoy et al, 1984 ). However, the crosslinking ability was not reproduced for galectins, for which the affinity increased in proportion to the lactose content.…”

Section: Multivalent Presentation Strategiesmentioning

confidence: 99%

Targeting Galectins With Glycomimetics

et al. 2020

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Among glycan-binding proteins, galectins, β-galactoside-binding lectins, exhibit relevant biological roles and are implicated in many diseases, such as cancer and inflammation. Their involvement in crucial pathologies makes them interesting targets for drug discovery. In this review, we gather the last approaches toward the specific design of glycomimetics as potential drugs against galectins. Different approaches, either using specific glycomimetic molecules decorated with key functional groups or employing multivalent presentations of lactose and N-acetyl lactosamine analogs, have provided promising results for binding and modulating different galectins. The review highlights the results obtained with these approximations, from the employment of S-glycosyl compounds to peptidomimetics and multivalent glycopolymers, mostly employed to recognize and/or detect h Gal-1 and h Gal-3.

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Enzyme-linked lectin assay (ELLA)

Cited by 33 publications

References 13 publications

Virus-like Particle Display of the α-Gal Carbohydrate for Vaccination against Leishmania Infection

Virus-like Particle Display of the α-Gal Carbohydrate for Vaccination against Leishmania Infection

Contribution of α-d-galactopyranosyl end groups to attachment of highly and low metastatic murine fibrosarcoma cells to various substrates

Targeting Galectins With Glycomimetics

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