Recognition factors of Ricinus communis agglutinin 1 (RCA1)

Wu, Albert M.; Wu, June H.; Singh, T. N.; Lai, Li-Ju; Yang, Zhangung; Herp, Anthony

doi:10.1016/j.molimm.2005.09.008

Cited by 37 publications

(36 citation statements)

References 49 publications

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“…The binding probability increases exponentially with surface delay time (c). This time dependency is consistent with the concept that binding of RCA 120 and Gal is slow kinetics process, [30,31] thus the binding probability of RCA 120 and Gal on the HeLa cell surface increases with prolonged interaction time. From these data, we found the interaction time needed for half-maximal probability of binding, t 0.5 = 0.3 s. This allowed us to estimate the association rate constant, k on = t 0.5…”

supporting

confidence: 90%

Molecular Recognition Force Spectroscopy Study of the Specific Lectin and Carbohydrate Interaction in a Living Cell

Wang

Xing

et al. 2011

ChemPhysChem

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supporting

confidence: 90%

Molecular Recognition Force Spectroscopy Study of the Specific Lectin and Carbohydrate Interaction in a Living Cell

Wang

Xing

et al. 2011

ChemPhysChem

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“…2. I/II, Galβ1→3/4GlcNAcβ1→-Ricinus communis (RCA 1 ) [19], Datura stramonium (Thorn apple), Wheat germ (WGA) [20], Erythrina cristagalli [21], Erythrina corallodendron [22] and ricin [17]. 3.…”

Section: Grouping Lectins Based On Recognition Of Monosaccharides Andmentioning

confidence: 99%

“…The biotin/avidin-based plate assay facilitated the study of fine specificity of multiple plant and bacterial lectins, where interaction of each lectin with several tens of highand low-molecular mass glycoforms was examined [12,18,19,21,28,68]. Similar studies were performed on galectins, rat galectin-4 (G4-N) and galectin-5, and chicken liver galectin CG-16 [40,41,63,69,70].…”

Section: Biotin/avidin Based Microtiter Plate Enzyme-linked Lectinosomentioning

confidence: 99%

Lectins as tools in glycoconjugate research

et al. 2008

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Lectins are ubiquitous proteins of nonimmune origin, present in plants, microorganisms, animals and humans which specifically bind defined monosugars or oligosaccharide structures. Great progress has been made in recent years in understanding crucial roles played by lectins in many biological processes. Elucidation of carbohydrate specificity of human and animal lectins is of great importance for better understanding of these processes. Long before the role of carbohydrate-protein interactions had been explored, many lectins, mostly of plant origin, were identified, characterized and applied as useful tools in studying glycoconjugates. This review focuses on the specificity-based lectin classification and the methods of measuring lectin-carbohydrate interactions, which are used for determination of lectin specificity or for identification and characterization of glycoconjugates with lectins of known specificity. The most frequently used quantitative methods are shortly reviewed and the methods elaborated and used in our laboratories, based on biotinylated lectins, are described. These include the microtiter plate enzyme-linked lectinosorbent assay, lectinoblotting and lectin-glycosphingolipid interaction on thin-layer plates. Some chemical modifications of lectin ligands on the microtiter plates and blots (desialylation, Smith degradation, beta-elimination), which extend the applicability of these methods, are also described.

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“…Conversely, studies carried out using ELISA reported very low, if any, binding of sialylated lactosides to RCA 120 . 52 Fluorescence glycan array data from the Consortium for Functional Glycomics 53 using polyacrylamide-based glycoconjugates 54 show high RCA 120 binding to non-reducing terminal Gal, Galb1-4Glc and Galb1-4GlcNAc. Interestingly, some but not all oligosaccharides terminating in the Neu5Aca2-6Galb1-4GlcNAc sequence were also strongly recognised on these arrays (see SI, Fig.…”

Section: Binding Of 6-modified Galactosides To Rca 120 In Other Intermentioning

confidence: 99%

Surface plasmon resonance imaging of glycoarrays identifies novel and unnatural carbohydrate-based ligands for potential ricin sensor development

et al. 2011

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Carbohydrate microarrays provide access to high through-put analysis of protein-carbohydrate interactions. Herein we demonstrate the use of SPR imaging (SPRi) of glycoarrays to assess the ligand specificity of the reputedly galactose-specific plant lectin RCA 120 (Ricinus communis agglutinin 120), a surrogate for the bioterrorism agent ricin. Glycoarray studies identified RCA 120 ligands based on galactose substituted at the 6-position with sialic acid. These observations, which were confirmed by saturation transfer difference (STD) NMR spectroscopy studies, inspired the synthesis of non-natural 6-substituted galactose derivatives, which were shown to have $3-4 fold enhanced binding to RCA 120 with respect to the unsubstituted compound. These novel unnatural galactosides, which are chemically and biologically more robust than their natural glycan counterparts, represent new potential ligands for the development of carbohydrate-based ricin sensors.

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Recognition factors of Ricinus communis agglutinin 1 (RCA1)

Cited by 37 publications

References 49 publications

Molecular Recognition Force Spectroscopy Study of the Specific Lectin and Carbohydrate Interaction in a Living Cell

Molecular Recognition Force Spectroscopy Study of the Specific Lectin and Carbohydrate Interaction in a Living Cell

Lectins as tools in glycoconjugate research

Surface plasmon resonance imaging of glycoarrays identifies novel and unnatural carbohydrate-based ligands for potential ricin sensor development

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