Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (beta-D-Gal(1----3)D-GalNAc).

Sastry, M V Krishna; Banarjee, P; Patanjali, Sankhavaram R.; Swamy, Musti J.; Swarnalatha, G; Surolia, Avadhesha

doi:10.1016/s0021-9258(18)67304-1

Cited by 197 publications

(22 citation statements)

References 39 publications

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“…The lectin jacalin is a valuable reagent for O-glycosylation assays because of its ability to bind Tn antigen, the basic building block of all O-linked glycans, as well as non-and mono-sialylated core 1 carbohydrates (Jeyaprakash et al, 2002;Sastry et al, 1986;Tachibana et al, 2006;Wu et al, 2003). SIVmac239 gp120, which has been shown unambiguously to be O-glycosylated on V1, was used as positive control (Stansell et al, 2011).…”

Section: A Subset Of Hiv-1 Strains With Long V1 Domains Are O-glycosylatedmentioning

confidence: 99%

Discovery of O-Linked Carbohydrate on HIV-1 Envelope and Its Role in Shielding against One Category of Broadly Neutralizing Antibodies

et al. 2020

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Section: A Subset Of Hiv-1 Strains With Long V1 Domains Are O-glycosylatedmentioning

confidence: 99%

Discovery of O-Linked Carbohydrate on HIV-1 Envelope and Its Role in Shielding against One Category of Broadly Neutralizing Antibodies

et al. 2020

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“…Purified NCTC11168 MOMP showed significant binding to the lectins Jacalin [35] and, to a lesser extent, DSL and LEL (figure 5a). Among the galactose-specific lectins, Jacalin exhibits specificity for human tumour-specific Thomsen-Friedenreich disaccharide (T-antigen; Gal(b1-3)-GalNAca1-Ser/Thr) [36]. To confirm that the Jacalin binding was the result of O-glycosylation of amino acid Thr 268 , MOMPs purified from NCTC11168 and NCTC11168 MOMP 268T/G were probed with monoclonal anti-T-antigen in ELISA assays (figure 5b).…”

Section: O-glycosylation Of Nctc11168 Momp Effects Bgag Bindingmentioning

confidence: 99%

A novelO-linked glycan modulatesCampylobacter jejunimajor outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization

et al. 2014

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Campylobacter jejuni is an important cause of human foodborne gastroenteritis; strategies to prevent infection are hampered by a poor understanding of the complex interactions between host and pathogen. Previous work showed that C. jejuni could bind human histo-blood group antigens (BgAgs) in vitro and that BgAgs could inhibit the binding of C. jejuni to human intestinal mucosa ex vivo. Here, the major flagella subunit protein (FlaA) and the major outer membrane protein (MOMP) were identified as BgAg-binding adhesins in C. jejuni NCTC11168. Significantly, the MOMP was shown to be O-glycosylated at Thr268; previously only flagellin proteins were known to be O-glycosylated in C. jejuni. Substitution of MOMP Thr268 led to significantly reduced binding to BgAgs. The O-glycan moiety was characterized as Gal(β1–3)-GalNAc(β1–4)-GalNAc(β1–4)-GalNAcα1-Thr268; modelling suggested that O-glycosylation has a notable effect on the conformation of MOMP and this modulates BgAg-binding capacity. Glycosylation of MOMP at Thr268 promoted cell-to-cell binding, biofilm formation and adhesion to Caco-2 cells, and was required for the optimal colonization of chickens by C. jejuni, confirming the significance of this O-glycosylation in pathogenesis.

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“…Jacalin was puri ed from jackfruit seeds by a nity chromatography using epichlorohydrin-activated guar gum as the a nity matrix [24]. The activity of the lectin was checked by its ability to agglutinate the red blood cells (RBCs) and the purity was analysed by Sodium dodecyl sulphate-polyacrylamide gel electrophoresis.…”

Section: Puri Cation Of Jacalinmentioning

confidence: 99%

Immunomodulatory Effects of Jacalin, A Dietary Plant Lectin on the Peripheral Blood Mononuclear Cells (PBMCs)

Lavanya¹,

Bommanabonia

Ahmed

et al. 2021

Preprint

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The tumor microenvironment that refers to the tumour’s surroundings is a key modulator of tumor growth and invasion. The tumour derived signals are known to downregulate the anti-tumor effects of the effector cells present in the TME. Thus, the cross talk between the tumor cells with the surrounding immune cells helps in evading the tumor surveillance as well as aiding in tumor growth and proliferation. Hence, knowledge regarding the effects of drugs/compound on the tumor-stromal interactions are gaining importance. In the present study, the effects of jacalin, a dietary lectin on the proliferation and cytokine production of peripheral blood mononuclear cells (PBMCs) are investigated. Jacalin was shown to act as a mitogen of PBMCs, the key cytokine secreting immune cells. Also, jacalin initially induces increased mRNA expression of pro-inflammatory cytokine IFN-γ; however prolonged stimulation of PBMCs resulted in increased expression of anti-inflammatory cytokine, mainly TGF-β. Further, 6 h jacalin prestimulated PBMCs (Jac-PBMCs) were shown to inhibit HeLa cell proliferation while 24 h (Jac-PBMCs) were found to favor tumor growth. Thus, it may be postulated that while jacalin initially polarizes the PBMCs to hinder the tumor growth, after a stipulated time point, interaction of jacalin with PBMCs can lead to an immunosuppressive TME that may probably assist in tumor growth and progression.

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Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (beta-D-Gal(1----3)D-GalNAc).

Cited by 197 publications

References 39 publications

Discovery of O-Linked Carbohydrate on HIV-1 Envelope and Its Role in Shielding against One Category of Broadly Neutralizing Antibodies

Discovery of O-Linked Carbohydrate on HIV-1 Envelope and Its Role in Shielding against One Category of Broadly Neutralizing Antibodies

A novelO-linked glycan modulatesCampylobacter jejunimajor outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization

Immunomodulatory Effects of Jacalin, A Dietary Plant Lectin on the Peripheral Blood Mononuclear Cells (PBMCs)

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