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Journal articles on the topic 'Lectin receptor'

Author: Grafiati

Published: 16 November 2024

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1

Masnikosa, Romana, Anna Nikolic, and Olgica Nedic. "Lectin-induced alterations of the interaction of insulin and insulin-like growth factor 1 receptors with their ligands." Journal of the Serbian Chemical Society 73, no. 8-9 (2008): 793–804. http://dx.doi.org/10.2298/jsc0809793m.

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In order to study whether the carbohydrate moieties of the human placental IGF-I receptor (IGF1R), IGF-II receptor (IGF2R) and insulin receptors (IRs) play a role in ligand binding, solubilised cell membrane preparations were incubated with 125I-labelled IGF-I, IGF-II and insulin in the presence of lectins with different sugar specificities. Three incubation procedures were tested: ligand-first, co-incubation and lectin-first incubation. Wheat germ agglutinin (WGA), concanavalin A (Con A) and phytohaemagglutinin (PHA) altered the binding of IGF-I and insulin to their high-affinity receptors in

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2

Jégouzo, Sabine A. F., Conor Nelson, Thomas Hardwick, et al. "Mammalian lectin arrays for screening host–microbe interactions." Journal of Biological Chemistry 295, no. 14 (2020): 4541–55. http://dx.doi.org/10.1074/jbc.ra120.012783.

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Many members of the C-type lectin family of glycan-binding receptors have been ascribed roles in the recognition of microorganisms and serve as key receptors in the innate immune response to pathogens. Other mammalian receptors have become targets through which pathogens enter target cells. These receptor roles have often been documented with binding studies involving individual pairs of receptors and microorganisms. To provide a systematic overview of interactions between microbes and the large complement of C-type lectins, here we developed a lectin array and suitable protocols for labeling

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Upham, Jacqueline P., Danielle Pickett, Tatsuro Irimura, E. Margot Anders, and Patrick C. Reading. "Macrophage Receptors for Influenza A Virus: Role of the Macrophage Galactose-Type Lectin and Mannose Receptor in Viral Entry." Journal of Virology 84, no. 8 (2010): 3730–37. http://dx.doi.org/10.1128/jvi.02148-09.

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ABSTRACT Although sialic acid has long been recognized as the primary receptor determinant for attachment of influenza virus to host cells, the specific receptor molecules that mediate viral entry are not known for any cell type. For the infection of murine macrophages by influenza virus, our earlier study indicated involvement of a C-type lectin, the macrophage mannose receptor (MMR), in this process. Here, we have used direct binding techniques to confirm and characterize the interaction of influenza virus with the MMR and to seek additional macrophage surface molecules that may have potenti

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4

Baricevic, Ivona, Ljiljana Vicovac-Panic, Vesna Marinovic, and Margita Cuperlovic. "Investigations of asialoglycoprotein receptor glycosylation by lectin affinity methods." Journal of the Serbian Chemical Society 67, no. 5 (2002): 331–38. http://dx.doi.org/10.2298/jsc0205331b.

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The asialoglycoprotein receptor belongs to the family of calcium-dependent (C-type) animal lectins. The purified receptor is a glycoprotein in which 10 % of the dry weight consists of sialic acid, galactose, N-acetylglucosamine and mannose. The carbohydrate content of the asialoglycoprotein receptor was investigated by lectin affinity methods. The usefulness of plant lectin affinity methods in the characterization of the saccharide content of the asialoglycoprotein receptor, as an animal lectin, is demonstrated. RCA I ConA, PHA, SNA I and WGA showed greater affinity toward the asialoglycoprote

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5

Karpova, I. S., I. M. Shuba, V. V. Lylo, and O. Y. Glavatskyi. "Characteristics of lectin receptors on erythrocyte membranes of patients with glioblastoma." Faktori eksperimental'noi evolucii organizmiv 34 (September 25, 2024): 165–69. http://dx.doi.org/10.7124/feeo.v34.1634.

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Aim. This work is devoted to the search the abnormalities of the receptor-lectin reactions associated with glioblastoma for diagnostic purposes. Methods. Red blood cell (RBC) specimens were taken from 22 persons distributed into the two cohorts: donors without an oncological diagnosis; patients with glioblastoma (GB). Panel of 9 commercial lectins (LECTINOTEST, Lviv, Ukraine) was used: ConA, WGA, PHA-P; PHA-E; PHA-L, SNA, VAA, STA, and LABA. Also the original lectin from persimmon sepals (named PSL) was used. It was obtained by isoelectric focusing and ammonium sulfate fractionation. Intensity

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Hébert, Eric. "Endogenous Lectins as Cell Surface Transducers." Bioscience Reports 20, no. 4 (2000): 213–37. http://dx.doi.org/10.1023/a:1026484722248.

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Interactions between cells or between cell and substratum involve specificreceptors and their ligands. Among the various cell surface receptorsidentified during the last decades, the carbohydrate-binding proteins, e.g., lectins are of peculiar interest because glycolipids, glycoproteinsand proteoglycans have been shown to interact with lectins on the surfaceof animal cells. Animal lectins are recognized as molecules playingimportant roles in a variety of biological processes through binding toglycoconjugates and lectin-like receptors such as selectins, sialoadhesins(CD22, CD33), natural killer

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Karpova, I. S. "SPECIFIC INTERACTIONS BETWEEN LECTINS AND RED BLOOD CELLS OF CHORNOBYL CLEANUP WORKERS AS INDICATOR OF SOME LATE RADIATION EFFECTS." Experimental Oncology 38, no. 4 (2016): 261–66. http://dx.doi.org/10.31768/2312-8852.2016.38(4):261-266.

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Aim: Growing interest in lectins is based on their diagnostic and pharmacological potential, especially the ability to inhibit proliferation and initiate apoptosis of cancer cells. In our research microplate lectinoassay able to detect carbohydrate containing structures (receptors) on erythrocyte surface have been proposed for Chornobyl cleanup workers (1986) monitoring. It was expected to reveal specific abnormalities associated with pathological condition arising as a result of late radiation effects. Materials and Methods: Red blood cell (RBC) specimens were taken from 171 persons distribut

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Lakhtin, V. M., M. V. Lakhtin, A. Yu Mironov, V. A. Aleshkin, and S. S. Afanasiev. "LECTIN POPULATIONS OF NK CELLS AGAINST VIRUSES-ASSOCIATED TUMORS (REVIEW OF LITERATURE)." Russian Clinical Laboratory Diagnostics 64, no. 5 (2019): 314–20. http://dx.doi.org/10.18821/0869-2084-2019-64-5-314-320.

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Analysis of the human NK (natural killers) cells and their functionally different populations in connection to tumor processes accompanied with viral infections is presented. Receptor lectins (non-immunoglobulin proteins and their complexes recognizing polysaccharides, glycoconjugates and glycopattern-containing molecules) play important role in regulation of innate immunity. Communicative diversity of NK-cell populations (in which lectins cofunction to other receptors) is directed against tumors and viruses. Effectiveness and selectivity of action of NK cell populations can be increased in co

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9

Landi, Alessia, Muriel Mari, Svenja Kleiser, et al. "Pseudomonas aeruginosa lectin LecB impairs keratinocyte fitness by abrogating growth factor signalling." Life Science Alliance 2, no. 6 (2019): e201900422. http://dx.doi.org/10.26508/lsa.201900422.

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Lectins are glycan-binding proteins with no catalytic activity and ubiquitously expressed in nature. Numerous bacteria use lectins to efficiently bind to epithelia, thus facilitating tissue colonisation. Wounded skin is one of the preferred niches for Pseudomonas aeruginosa, which has developed diverse strategies to impair tissue repair processes and promote infection. Here, we analyse the effect of the P. aeruginosa fucose-binding lectin LecB on human keratinocytes and demonstrate that it triggers events in the host, upon binding to fucosylated residues on cell membrane receptors, which exten

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10

Barre, Annick, Els J. M. Van Damme, Mathias Simplicien, et al. "Man-Specific Lectins from Plants, Fungi, Algae and Cyanobacteria, as Potential Blockers for SARS-CoV, MERS-CoV and SARS-CoV-2 (COVID-19) Coronaviruses: Biomedical Perspectives." Cells 10, no. 7 (2021): 1619. http://dx.doi.org/10.3390/cells10071619.

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Betacoronaviruses, responsible for the “Severe Acute Respiratory Syndrome” (SARS) and the “Middle East Respiratory Syndrome” (MERS), use the spikes protruding from the virion envelope to attach and subsequently infect the host cells. The coronavirus spike (S) proteins contain receptor binding domains (RBD), allowing the specific recognition of either the dipeptidyl peptidase CD23 (MERS-CoV) or the angiotensin-converting enzyme ACE2 (SARS-Cov, SARS-CoV-2) host cell receptors. The heavily glycosylated S protein includes both complex and high-mannose type N-glycans that are well exposed at the su

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Salmon, J. E., S. Kapur, and R. P. Kimberly. "Opsonin-independent ligation of Fc gamma receptors. The 3G8-bearing receptors on neutrophils mediate the phagocytosis of concanavalin A-treated erythrocytes and nonopsonized Escherichia coli." Journal of Experimental Medicine 166, no. 6 (1987): 1798–813. http://dx.doi.org/10.1084/jem.166.6.1798.

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We report that phagocytosis by human neutrophils of Con A-treated erythrocytes (E-Con A) and nonopsonized Escherichia coli with mannose-binding adhesions is mediated by the Fc gamma receptor bearing the 3G8 epitope. Modulation of Fc receptors by pretreating with aggregated-IgG or with 3G8 anti-Fc gamma receptor mAb markedly inhibited internalization of E-Con A and E. coli without altering their cell surface attachment. Phagocytosis of these probes was specifically blocked by alpha-methylmannoside and D-mannose and not by other monosaccharides. Thus, recognition of E-Con A and E. coli by the Fc

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12

Abbott, W. M., E. F. Hounsell, and T. Feizi. "Further studies of oligosaccharide recognition by the soluble 13 kDa lectin of bovine heart muscle. Ability to accommodate the blood-group-H and -B-related sequences." Biochemical Journal 252, no. 1 (1988): 283–87. http://dx.doi.org/10.1042/bj2520283.

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Oligosaccharide recognition by the 13 kDa soluble lectin from bovine heart muscle has been investigated by inhibition of binding of the 125I-labelled lectin to trypsin-treated rabbit erythrocytes. The results indicate that the Type 1 (Gal beta 1-3GlcNAc) and the Type 2 (Gal beta 1-4GlcNAc) backbone structures are the basic recognition units, and that the blood-group-H structure, the blood-group-B structure, the ‘B-like’ structure [afucosyl-(blood group B)] and the alpha 2-3 sialylated analogues of the backbone structures can also be accommodated and hence are candidate receptor structures for

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13

Bardosi, A., T. Dimitri, B. Wosgien, and H. J. Gabius. "Expression of endogenous receptors for neoglycoproteins, especially lectins, that allow fiber typing on formaldehyde-fixed, paraffin-embedded muscle biopsy specimens. A glycohistochemical, immunohistochemical, and glycobiochemical study." Journal of Histochemistry & Cytochemistry 37, no. 7 (1989): 989–98. http://dx.doi.org/10.1177/37.7.2732460.

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A panel of biotinylated (neo)glycoproteins was used for specific detection of endogenous sugar receptors, especially lectins, in formaldehyde-fixed, paraffin-embedded muscle biopsy specimens from human deltoid, quadriceps, and biceps muscles, tibial and quadriceps muscles of rat, and bovine masseter muscle. The glycohistochemical probes used consisted of conjugates of a labeled, histochemically inert carrier protein and various covalently linked, histochemically crucial sugar moieties. Specific binding of alpha-L-fucoside, beta-D-galactoside, beta-D-xyloside, and alpha-D-mannoside to muscle se

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14

Rushton, Emma, Danielle L. Kopke, and Kendal Broadie. "Extracellular heparan sulfate proteoglycans and glycan-binding lectins orchestrate trans-synaptic signaling." Journal of Cell Science 133, no. 15 (2020): jcs244186. http://dx.doi.org/10.1242/jcs.244186.

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ABSTRACTThe exceedingly narrow synaptic cleft (<20 nm) and adjacent perisynaptic extracellular space contain an astonishing array of secreted and membrane-anchored glycoproteins. A number of these extracellular molecules regulate intercellular trans-synaptic signaling by binding to ligands, acting as co-receptors or modulating ligand–receptor interactions. Recent work has greatly expanded our understanding of extracellular proteoglycan and glycan-binding lectin families as key regulators of intercellular signaling at the synapse. These secreted proteins act to regulate the compartmentalizat

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15

Eble, Johannes. "Structurally Robust and Functionally Highly Versatile—C-Type Lectin (-Related) Proteins in Snake Venoms." Toxins 11, no. 3 (2019): 136. http://dx.doi.org/10.3390/toxins11030136.

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Snake venoms contain an astounding variety of different proteins. Among them are numerous C-type lectin family members, which are grouped into classical Ca2+- and sugar-binding lectins and the non-sugar-binding snake venom C-type lectin-related proteins (SV-CLRPs), also called snaclecs. Both groups share the robust C-type lectin domain (CTLD) fold but differ in a long loop, which either contributes to a sugar-binding site or is expanded into a loop-swapping heterodimerization domain between two CLRP subunits. Most C-type lectin (-related) proteins assemble in ordered supramolecular complexes w

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Hoober, J. Kenneth. "ASGR1 and Its Enigmatic Relative, CLEC10A." International Journal of Molecular Sciences 21, no. 14 (2020): 4818. http://dx.doi.org/10.3390/ijms21144818.

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The large family of C-type lectin (CLEC) receptors comprises carbohydrate-binding proteins that require Ca2+ to bind a ligand. The prototypic receptor is the asialoglycoprotein receptor-1 (ASGR1, CLEC4H1) that is expressed primarily by hepatocytes. The early work on ASGR1, which is highly specific for N-acetylgalactosamine (GalNAc), established the foundation for understanding the overall function of CLEC receptors. Cells of the immune system generally express more than one CLEC receptor that serve diverse functions such as pathogen-recognition, initiation of cellular signaling, cellular adhes

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Hart, Derek N. J., Seema Khan, Elisabetta d’Aniello, Kylie J. McDonald, and Masato Kato. "Role of Novel C-Type Lectin Receptor DCL-1 in Phagocytes and Dendritic Cells." Blood 110, no. 11 (2007): 2419. http://dx.doi.org/10.1182/blood.v110.11.2419.2419.

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Abstract Cell surface C-type lectins are implicated in many aspects of immunity. For example, professional phagocytes utilise cell surface C-type lectins in pathogen recognition/binding and phagocytosing the pathogens for destruction and/or antigen processing (e.g. mannose receptor, DC-SIGN, dectin-1). Some C-type lectins are involved in cell-cell adhesion and trafficking of leukocytes (e.g. selectins). DCL-1 is a small type I transmembrane C-type lectin receptor, discovered as a genetic fusion partner of DEC-205. DCL-1 protein was highly conserved amongst the human, mouse and rat orthologs. T

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van Kooyk, Yvette. "C-type lectins on dendritic cells: key modulators for the induction of immune responses." Biochemical Society Transactions 36, no. 6 (2008): 1478–81. http://dx.doi.org/10.1042/bst0361478.

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DCs (dendritic cells) are specialized in the recognition of pathogens and play a pivotal role in the control of immune responses. DCs are also important for homoeostatic control, recognizing self-antigens and tolerizing the tissue environment. The nature of the antigen recognized tilts the balance towards immunity or tolerance. CLRs (C-type lectin receptors) expressed by DC are involved in the recognition and capture of many glycosylated self-antigens and pathogens. It is now becoming clear that these CLRs may not only serve as antigen receptors allowing internalization and antigen presentatio

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Aucoin, Emilyn B., Elizabeth Skapinker, Abdulrahman M. Yaish, et al. "Glycosyl Mobile Radical Structures of Folic Acid Receptors Impact the Internalization of Functionalized Folate Amphiphilic Alternating Copolymer in Cancer Cells." Receptors 3, no. 4 (2024): 457–73. http://dx.doi.org/10.3390/receptors3040023.

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Folate receptor alpha (FRα) is a glycosylphosphatidylinositol (GPI) membrane-anchored protein containing three N-glycosylated residues at the N47, N139, and N179 termini. These glycosylation sites have been reported to be crucial for the receptor’s structural integrity and its ability to bind and internalize FA. Here, we investigated the role of FRα glycosylation in the binding and internalization efficacy of FA–DABA–SMA in pancreatic PANC-1 cancer cells. There is a strong association of the FA copolymer with FRα with a Pearson coefficient R-value of 0.7179. PANC-1 cancer cells were pretreated

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Rohlenová, Anna, Miroslav Ledvina, David Šaman, and Karel Bezouška. "Synthesis of Linear and Branched Regioisomeric Chitooligosaccharides as Potential Mimetics of Natural Oligosaccharide Ligands of Natural Killer Cells NKR-P1 and CD69 Lectin Receptors." Collection of Czechoslovak Chemical Communications 69, no. 9 (2004): 1781–804. http://dx.doi.org/10.1135/cccc20041781.

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Regioisomer of chitobiose 13 with β(1→3) glycosidic bond and branched analog of chitotriose 25 having β(1→4) and β(1→3) glycosidic bonds, were prepared and tested as potential mimetics of natural oligosaccharide ligands for activating lectin receptors NKR-P1A and CD69 of natural killer (NK) cells. The structural requirements of NKR-P1 lectin receptor on effective mimetics of its natural ligands has been discussed. A significant binding activity of the branched trisaccharide 25 to the receptor CD69 was observed.

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Lakhtin, M. V., V. M. Lakhtin, V. A. Aleshkin, M. S. Afanasiev, and S. S. Afanasiev. "LECTINS IN ANTI-CANCER STRATEGIES." Acta Biomedica Scientifica 3, no. 4 (2018): 69–77. http://dx.doi.org/10.29413/abs.2018-3.4.11.

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The published during last few years data concerning communicative role of lectins (proteins and their complexes which recognize carbohydrates, glycoconjugates and their patterns) in on-duty supporting and increasing anticancer status of human immunity are analyzed. Examples of lectin-(glycoconjugate pattern) strategies, approaches and tactic variants in study and development of anticancer treatments, principle variants of therapy, possible vaccines in 35 cases of blood connected tumors (leukemia, lymphomas, others), solid tumors (carcinomas, sarcoma, cancers of vaginal biotopes, prostate, blad

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Gabius, H. J., B. Kohnke-Godt, M. Leichsenring, and A. Bardosi. "Heparin binding lectin of human placenta as a tool for histochemical ligand localization and isolation." Journal of Histochemistry & Cytochemistry 39, no. 9 (1991): 1249–56. http://dx.doi.org/10.1177/39.9.1918943.

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Biotinylated heparin has been used to detect the presence of specific binding sites in sections of human placenta, which has prompted demonstration of expression of lectin activity for this proteoglycan. Purification of this lectin from full-term placenta facilitates the synthesis of its biotinylated derivative, using biotin-amidocaproyl hydrazide, without affecting its activity. It also enables immunization to obtain antibodies. The labeled lectin is shown to bind specifically to nuclear and cytoplasmic locations in various cell types of human placenta, nuclear expression of lectin binding si

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Aglyamova, Aliya, Natalia Petrova, Oleg Gorshkov, Liudmila Kozlova, and Tatyana Gorshkova. "Growing Maize Root: Lectins Involved in Consecutive Stages of Cell Development." Plants 11, no. 14 (2022): 1799. http://dx.doi.org/10.3390/plants11141799.

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Proteins that carry specific carbohydrate-binding lectin domains have a great variety and are ubiquitous across the plant kingdom. In turn, the plant cell wall has a complex carbohydrate composition, which is subjected to constant changes in the course of plant development. In this regard, proteins with lectin domains are of great interest in the context of studying their contribution to the tuning and monitoring of the cell wall during its modifications in the course of plant organ development. We performed a genome-wide screening of lectin motifs in the Zea mays genome and analyzed the trans

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Barre, Annick, Christine Hervé, Bernard Lescure, and Pierre Rougé. "Lectin Receptor Kinases in Plants." Critical Reviews in Plant Sciences 21, no. 4 (2002): 379–99. http://dx.doi.org/10.1080/0735-260291044287.

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Hlaing, May Thinzar, Yoshiya Horimoto, Kaori Denda-Nagai, et al. "Tamoxifen-resistant breast cancer cells exhibit reactivity with Wisteria floribunda agglutinin." PLOS ONE 17, no. 8 (2022): e0273513. http://dx.doi.org/10.1371/journal.pone.0273513.

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Glycosylation is one of the most important post-translational modifications of cell surface proteins involved in the proliferation, metastasis and treatment resistance of cancer cells. However, little is known about the role of glycosylation as the mechanism of breast cancer cell resistance to endocrine therapy. Herein, we aimed to identify the glycan profiles of tamoxifen-resistant human breast cancer cells, and their potential as predictive biomarkers for endocrine therapy. We established tamoxifen-resistant cells from estrogen receptor-positive human breast cancer cell lines, and their memb

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Takebayashi, Kohzo, Tatsuhiko Suzuki, Mototaka Yamauchi, et al. "Association of circulating soluble lectin-like oxidized low-density lipoprotein receptor-1 with inflammatory markers and urinary albumin excretion in patients with type 2 diabetes." SAGE Open Medicine 9 (January 2021): 205031212110644. http://dx.doi.org/10.1177/20503121211064468.

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Objectives: The main purpose of the study was to study the association between circulating soluble lectin-like oxidized low-density lipoprotein receptor-1 levels and various markers, including inflammatory markers such as high-sensitivity C-reactive protein and fibrinogen, serum lipids, and renal function, in patients with poorly controlled type 2 diabetes. Methods: The subjects were 70 patients (men 45, women 25) who were hospitalized for treatment of poor glycemic control. Plasma soluble lectin-like oxidized low-density lipoprotein receptor-1 levels were assayed using a sandwich chemilumines

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Thorkelsson, T., G. M. Ciraolo, G. F. Ross, J. A. Whitsett, and R. E. Morris. "Lectin activity of the major surfactant protein (SP-A) may participate in, but is not required for, binding to rat type II cells." Journal of Histochemistry & Cytochemistry 40, no. 5 (1992): 643–49. http://dx.doi.org/10.1177/40.5.1573247.

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Pulmonary surfactant is a complex mixture of lipids and proteins, of which surfactant protein A (SP-A) is the most abundant glycoprotein. The SP-A molecule has several distinct structural features that include a lectin-like domain, sharing structural features with other mammalian lectins. We have tested the hypothesis that lectin activity of the SP-A molecule is required for the binding to its receptor on the surface of alveolar Type II cells. By using colloidal gold immunocytochemistry in conjunction with electron microscopy, we evaluated the ability of mannosylated proteins to inhibit canine

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Valle Argos, Beatriz, Giorgia Chiodin, Francesco Forconi, et al. "Lymphoma-Specific Subversion of B-Cell Receptor Signaling By Macrophage Lectins." Blood 132, Supplement 1 (2018): 2865. http://dx.doi.org/10.1182/blood-2018-99-110954.

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Abstract The clue that surface Ig (sIg) is implicated in the pathogenesis of follicular lymphoma (FL) is that in FL the vast majority of the sIg variable regions are structurally modified by insertion of mannose residues into the antigen-binding sites. This is tumor-specific and reflects positive selection of sequence motifs for glycan addition introduced during somatic hypermutation. The termination at high mannoses is very unusual in cell surface molecules and it confers an ability to interact with local lectins expressed by macrophages. In this respect, the mannose cloaking of the sIg recep

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ZANETTA, Jean-Pierre, Catherine ALONSO, and Jean-Claude MICHALSKI. "Interleukin 2 is a lectin that associates its receptor with the T-cell receptor complex." Biochemical Journal 318, no. 1 (1996): 49–53. http://dx.doi.org/10.1042/bj3180049.

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To determine the nature of the mechanism by which the binding of interleukin-2 (IL-2) to its receptor (IL-2Rβ) induces IL-2Rβ phosphorylation by the tyrosine kinase p56lck associated with the T-cell receptor (TCR) complex, we investigated the possibility that this mechanism was due to the putative lectin activity of IL-2 ([Sherblom, Sathyamoorthy, Decker and Muchmore (1989) J. Immunol. 143, 939–944]. Here we demonstrate that IL-2 is a calcium-independent lectin specific for oligomannosidic N-glycans with five and six mannose residues. This lectin activity is preserved after binding of IL-2 to

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Alsolami, Ahmed, Amina I. Dirar, Emadeldin Hassan E. Konozy, et al. "Genome-Wide Mining of Selaginella moellendorffii for Hevein-like Lectins and Their Potential Molecular Mimicry with SARS-CoV-2 Spike Glycoprotein." Current Issues in Molecular Biology 45, no. 7 (2023): 5879–901. http://dx.doi.org/10.3390/cimb45070372.

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Multidisciplinary research efforts on potential COVID-19 vaccine and therapeutic candidates have increased since the pandemic outbreak of SARS-CoV-2 in 2019. This search has become imperative due to the increasing emergences and limited widely available medicines. The presence of bioactive anti-SARS-CoV-2 molecules was examined from various plant sources. Among them is a group of proteins called lectins that can bind carbohydrate moieties. In this article, we present ten novel, chitin-specific Hevein-like lectins that were derived from Selaginella moellendorffii v1.0’s genome. The capacity of

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Sawyer, J. T., and R. A. Akeson. "Differential redistribution of lectin receptor classes on clonal rat myotubes and myoblasts." Journal of Cell Science 83, no. 1 (1986): 181–96. http://dx.doi.org/10.1242/jcs.83.1.181.

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To evaluate the relative mobilities of cell surface glycoconjugates during myogenesis we have studied the redistribution of fluorescein-conjugated plant lectins on L6 rat myogenic cells. Previous experiments had demonstrated that the receptors for the lectins soybean agglutinin (SBA), wheat germ agglutinin, concanavalin A and Lens culinaris agglutinin all were relatively uniformly distributed on both myoblasts and myotubes, and that SBA receptors were capable of rapid redistribution on myotubes but not myoblasts at 4 degrees C (Sawyer & Akeson, 1983). Here we show that when SBA-labelled my

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Itin, C., A. C. Roche, M. Monsigny, and H. P. Hauri. "ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins." Molecular Biology of the Cell 7, no. 3 (1996): 483–93. http://dx.doi.org/10.1091/mbc.7.3.483.

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Based on sequence homologies with leguminous lectins, the intermediate compartment marker ERGIC-53 was proposed to be a member of a putative new class of animal lectins associated with the secretory pathway. Independent, 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 ERGIC-53 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 associa

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Chen, Yanan, Harindra Vedala, Gregg P. Kotchey, et al. "Detection of Lectins using Glyco-Functionalized Nanosensors." MRS Proceedings 1451 (2012): 191–96. http://dx.doi.org/10.1557/opl.2012.1291.

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ABSTRACTWe have used single-walled carbon nanotube field-effect transistor (SWNT-FET) and chemically converted graphene field-effect transistor (CCG-FET) devices to probe the interactions between carbohydrates and their recognition lectins. Porphyrin- and pyrene-based glycoconjugates were used as receptor molecules and the target lectins were two bacterial lectins that present different carbohydrate preference, namely PA-IL, PA-IIL from Pseudomonas aeruginosa and a plant lectin Concanavalin A. The specific binding between lectin and carbohydrate can be transduced to the change in FET device co

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Reed, J. C., W. Tadmori, M. Kamoun, G. Koretzky, and P. C. Nowell. "Suppression of interleukin 2 receptor acquisition by monoclonal antibodies recognizing the 50 KD protein associated with the sheep erythrocyte receptor on human T lymphocytes." Journal of Immunology 134, no. 3 (1985): 1631–39. http://dx.doi.org/10.4049/jimmunol.134.3.1631.

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Abstract Monoclonal antibodies OKT11A, 9.6, and 35.1 recognize epitopes on a 50000 dalton surface molecule (p50) identical to or closely associated with the sheep erythrocyte receptor (E receptor) on human T lymphocytes. These three antibodies were investigated for ability to inhibit T cell proliferation and interleukin 2 (IL 2) receptor acquisition (determined with anti-Tac antibody in an immunofluorescence assay) induced by the lectin mitogen phytohemagglutinin (PHA) or by the phorbol ester 12-O-tetradecanoyl-phorbol-13 acetate (TPA). OKT11A, 9.6, and 35.1 were found to suppress [3H]thymidin

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Sheikh, H., H. Yarwood, A. Ashworth, and C. M. Isacke. "Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor." Journal of Cell Science 113, no. 6 (2000): 1021–32. http://dx.doi.org/10.1242/jcs.113.6.1021.

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Endo180 was previously characterized as a novel, cell type specific, recycling transmembrane glycoprotein. This manuscript describes the isolation of a full length human Endo180 cDNA clone which was shown to encode a fourth member of a family of proteins comprising the macrophage mannose receptor, the phospholipase A(2) receptor and the DEC-205/MR6 receptor. This receptor family is unusual in that they contain 8–10 C-type lectin carbohydrate recognition domains in a single polypeptide backbone, however, only the macrophage mannose receptor had been shown to function as a lectin. Sequence analy

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Watson, S. R., Y. Imai, C. Fennie, et al. "The complement binding-like domains of the murine homing receptor facilitate lectin activity." Journal of Cell Biology 115, no. 1 (1991): 235–43. http://dx.doi.org/10.1083/jcb.115.1.235.

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The leukocyte homing receptor (HR), the endothelial leukocyte adhesion molecule, and gmp140/platelet activation-dependent granule membrane protein are members of a family of adhesion molecules, termed the lectin cell adhesion molecules (LEC-CAMS) which are unified by a multi-domain structure containing a lectin motif, an epidermal growth factor-like (egf) motif, and variable numbers of a complement binding-like (CB) motif. Previous data have indicated a predominant role for the lectin motif in cell adhesion directed by the LEC-CAMS, although the egf-like domain of the HR may also play a potent

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Richards, M. L., and D. H. Katz. "The binding of IgE to murine Fc epsilon RII is calcium-dependent but not inhibited by carbohydrate." Journal of Immunology 144, no. 7 (1990): 2638–46. http://dx.doi.org/10.4049/jimmunol.144.7.2638.

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Abstract Despite extensive study, little is known about the functions of the moderate affinity IgE receptors (Fc epsilon RII) on B cells. Recent cDNA and genomic cloning studies have demonstrated that, in contrast to other FcR, Fc epsilon RII is not a member of the Ig gene superfamily. Moreover, it uniquely expresses a region that is highly homologous with a membrane-associated, calcium-dependent binding lectin, the asialoglycoprotein receptor. We now report that the interaction between IgE and the Fc epsilon RII of murine B cells and macrophages requires calcium. Furthermore, as might be expe

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Basu, Prabnab S., Pradip K. Datta, and Tapash K. Datta. "Possible mechanism for the inhibition of lectin-erythrocyte interaction in presence of endogenous lectin receptor." Bioscience Reports 16, no. 6 (1996): 453–58. http://dx.doi.org/10.1007/bf01198460.

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The presence of hydrophobic sites in the lectin-I molecule was indicated by hydrophobic probes like 1-anilinonapthalene-8-sulfonic acid (ANS), 2-p-toluidinyl napthalene-6-sulfonic acid (TNS), N-phenyl-1-napthylamine (NA) and rose bengal (RB). This was further confirmed by amino acid modifications in the hydrophobic region of the lectin-I molecule. The binding of ANS, TNS, NA and RB to lectin-I was affected in the presence of NaCl. The involvement of hydrophobic interactions in rice-bean lectin-I-endogenous lectin receptor (ELR) complex were indicated by alterations in the circular dichroism an

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Pérez-Hernández, Jesus, Clarisa Retana-González, Espiridión Ramos-Martínez, et al. "Entamoeba histolytica Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic Lectin." Life 11, no. 9 (2021): 923. http://dx.doi.org/10.3390/life11090923.

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Amoebiasis in humans is caused by the protozoan parasite Entamoeba histolytica, which cytotoxic activity has been demonstrated on a wide variety of target cells. The process involves the adherence of the parasite to the cell, and such adherence is mediated by an amoebic surface lectin, known as Gal/GalNAc lectin. It is composed of heavy, intermediate, and light subunits. The carbohydrate recognition domain (CRD) has been identified within a cysteine-rich region in the lectin heavy subunit and has an amino acid sequence identity to the receptor-binding domain of hepatocyte growth factor (HGF).

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Abbott, W. Mark, and Philip G. Strange. "Partial purification of dopamine D2 receptors using lectin affinity columns." Bioscience Reports 5, no. 4 (1985): 303–8. http://dx.doi.org/10.1007/bf01116901.

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Dopamine D2 receptors, detected by [3H]spiperone Dopamine D2 receptors, detected by [3H]spiperone binding, were solubilized from bovine caudate nucleus by cholate/sodium chloride and were found to bind to wheat germ agglutinin immobilized on agarose. Specific elution could be achieved with N-acetylglucosamine whereas other sugars tested were inactive in this regard. The eluted preparation was enriched in solubilized receptors about sevenfold. The pharmaco-logical properties of the preparation were essentially unchanged by the lectin affinity purification procedure. The D2 dopamine receptor is

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Latham, Virginia H., Jeanette L. Ducut, Karolin Rostamiani, et al. "A rapid lectin receptor binding assay: comparative evaluation of sea urchin embryo cell surface lectin receptors." Acta Histochemica 97, no. 1 (1995): 89–97. http://dx.doi.org/10.1016/s0065-1281(11)80209-6.

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MCABEE, Douglas D., Xin JIANG, and Kevin B. WALSH. "Lactoferrin binding to the rat asialoglycoprotein receptor requires the receptor's lectin properties." Biochemical Journal 348, no. 1 (2000): 113–17. http://dx.doi.org/10.1042/bj3480113.

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Lactoferrin binds to rat hepatic lectin 1 (RHL1), the major subunit of the asialoglycoprotein (ASGP) receptor, with high affinity, by a galactose-independent mechanism. To better understand the molecular basis of this novel interaction, we compared the binding of lactoferrin and asialo-orosomucoid (ASOR) to isolated rat hepatocytes and to purified ASGP receptors as a function of pH, Ca2+ and receptor acylation. Binding of 125I-lactoferrin and 125I-ASOR to isolated rat hepatocytes at 4 °C decreased sharply at pH < 6, following similar titration curves. Binding of 125I-lactoferrin and 125I-AS

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Dupuis, Gilles, and Marc Letellier. "Functional incorporation and preferred orientation of phytohemagglutinin receptor glycoproteins in phospholipid vesicles." Biochemistry and Cell Biology 65, no. 2 (1987): 120–29. http://dx.doi.org/10.1139/o87-017.

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Porcine lymphocyte Phaseolus vulgaris phytohemagglutinin (PHA) receptor glycoproteins purified by affinity chromatography have been reassembled into vesicles made of phosphatidylcholine and phosphatidylserine by detergent (dodecyltrimethylammonium bromide) dialysis. The receptor glycoproteins were incorporated into the lipid vesicles in a nonselective manner with a yield of 65–70%. Vesicles containing the glycoproteins were sealed as evidenced by their impermeability to calcium ions, using quin 2 trapped inside the vesicles. The vesicles were agglutinated by PHA, suggesting that the saccharidi

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Ramos, Márcio Viana, Liezelotte Rezende Bomfim, Bandeira, and Henri Debray. "Evidence of an endogenous lectin receptor in seeds of the legume Cratylia floribunda." Brazilian Journal of Plant Physiology 14, no. 3 (2002): 195–202. http://dx.doi.org/10.1590/s1677-04202002000300003.

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Cratylia floribunda seeds were ground and the clean crude saline extract was fractionated into albumin, globulin, prolamin, acidic and basic glutelin protein fractions. These protein fractions were examined for the presence of an endogenous lectin receptor by SDS-polyacrylamide gel electrophoresis, western blot, affinity chromatography on a Sepharose 4B-Cratylia floribunda (CFL) lectin column and kinetic analysis in real time by surface plasmon resonance (SPR). Prolamin was the richest protein fraction although very poor in haemagglutinating activity. Basic glutelin was far the less interestin

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Argayosa, A. M., F. F. Natividad, R. R. Matias, and G. L. Enriquez. "Detection of Concannavalin a Receptors in Trophozoites and Cysts of Acanthamoeba sp. (W4) Philippine Isolate." Microscopy and Microanalysis 3, S2 (1997): 119–20. http://dx.doi.org/10.1017/s1431927600007480.

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Distribution of glucose and mannose moieties of Acanthamoeba sp. (W4) Philippine isolate was detected using fluorescem isothiocyanate (FITC)- labeled Concannavalin A (Con A) lectin. Green fluorescent patches around the plasma membrane of agglutinated trophozoites (Fig.1) were observed. Isolated Acanthamoeba cyst exhibited strong fluorescence on the cyst wall Brighter fluorescence was detected on the site of adherence between the Acanthamoeba (W4) cysts and trophozoites (Fig. 1,3). These lectin receptors were concentrated at the uroidal region of the trophozoite. The fluorescence, however, was

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Szczykutowicz, Justyna. "Ligand Recognition by the Macrophage Galactose-Type C-Type Lectin: Self or Non-Self?—A Way to Trick the Host’s Immune System." International Journal of Molecular Sciences 24, no. 23 (2023): 17078. http://dx.doi.org/10.3390/ijms242317078.

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The cells and numerous macromolecules of living organisms carry an array of simple and complex carbohydrates on their surface, which may be recognized by many types of proteins, including lectins. Human macrophage galactose-type lectin (MGL, also known as hMGL/CLEC10A/CD301) is a C-type lectin receptor expressed on professional antigen-presenting cells (APCs) specific to glycans containing terminal GalNAc residue, such as Tn antigen or LacdiNAc but also sialylated Tn antigens. Macrophage galactose-type lectin (MGL) exhibits immunosuppressive properties, thus facilitating the maintenance of imm

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Gregorio-Jauregui, Karla M., Susana A. Carrizales-Alvarez, Jorge E. Rivera-Salinas та ін. "Immobilization of SA-α-2,6-Gal Receptors Related to Influenza on Magnetic Nanoparticles Coated with Chitosan". Advanced Materials Research 976 (червень 2014): 19–24. http://dx.doi.org/10.4028/www.scientific.net/amr.976.19.

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Influenza infection is carried out due to the virus hemagglutinin recognizes host cell surface with terminal sialic acid (SA) linked receptors SA-α-2,6-Gal for human strain. Sambucus nigra lectin has structural similarity to the viral hemagglutinin. Magnetic nanoparticles (MNP) coated with chitosan can be used as support for the study of these receptors. The goal of this study was to extract the SA-α-2,6-Gal receptors of porcine trachea for their immobilization on magnetic nanoparticles coated with chitosan. The extraction was carried out based on affinity of Sambucus nigra lectin to SA-α-2,6-

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Geoffroy, J. S., and S. D. Rosen. "Demonstration that a lectin-like receptor (gp90MEL) directly mediates adhesion of lymphocytes to high endothelial venules of lymph nodes." Journal of Cell Biology 109, no. 5 (1989): 2463–69. http://dx.doi.org/10.1083/jcb.109.5.2463.

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Lymphocyte migration from the blood into most secondary lymphoid organs is initiated by a highly selective adhesive interaction with the endothelium of specialized blood vessels known as high endothelial venules (HEV). The propensity of lymphocytes to migrate to particular lymphoid organs is known as lymphocyte homing, and the receptors on lymphocytes that dictate interactions with HEV at particular anatomical sites are designated "homing receptors". Based upon antibody blockade experiments and cell-type distribution studies, a prominent candidate for the peripheral lymph node homing receptor

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Jordinson, M., P. H. Deprez, R. J. Playford, et al. "Soybean lectin stimulates pancreatic exocrine secretion via CCK-A receptors in rats." American Journal of Physiology-Gastrointestinal and Liver Physiology 270, no. 4 (1996): G653—G659. http://dx.doi.org/10.1152/ajpgi.1996.270.4.g653.

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Rats fed raw soy flour (RSF) show pancreatic growth due to excessive cholecystokinin (CCK) release. Soybean trypsin inhibitors are implicated, but rats fed soybean lectin also showed pancreatic growth. Therefore, we studied the effect of soybean lectin on pancreatic protein secretion in anesthetized rats. Intraduodenal administration of 30 mg of RSF stimulated a 1-h integrated rise in pancreatic protein output of 2.2 +/- 1.1 mg/h (mean +/- SE) in rats with bile pancreatic (BP) juice returned to the duodenum. Selective removal of the lectin by affinity to N-acetyl-D-galactosamineagarose abolish

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Sagar, Divya, Catherine Foss, Zafar Khan, Martin Pomper, and Pooja Jain. "Lectin-targeted dendritic cell immunotherapies against experimental autoimmune encephalitis/multiple sclerosis (CAM5P.242)." Journal of Immunology 192, no. 1_Supplement (2014): 180.13. http://dx.doi.org/10.4049/jimmunol.192.supp.180.13.

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Abstract The molecular mechanisms of how circulating dendritic cells (DCs) access the CNS across the blood-brain barrier (BBB) remains to be investigated. During neuroinflammation, DCs transmigrate across the BBB in the presence of chemoattractants, particularly CCL2, and initiate immune response. We showed through near-infrared imaging that DC accumulation into lesions within the CNS correlated with severity of inflammation during experimental autoimmune encephalitis (EAE). Actin polymerization on DCs upon CCL2 exposure indicated a migratory phenotype. Transmigration of DCs was paracellular a

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