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55 results for “lectins”
Dataset related to article "Complement activation promoted by the lectin pathway mediates C3aR-dependent sarcoma progression and immunosuppression"
<p>This record contains raw data related to article “Complement activation promoted by the lectin pathway mediates C3aR-dependent sarcoma progression and immunosuppression"</p> <p>Complement has emerged as a component of tumor promoting inflammation. We conducted a systematic assessment of the role of complement activation and effector pathways in sarcomas. <em>C3</em> <sup>-/-</sup>, <em>MBL1/2</em> <sup>-/-</sup> and <em>C4</em> <sup>-/-</sup> mice showed reduced susceptibility to 3-methylcholanthrene sarcomagenesis and transplanted sarcomas, whereas C1q and factor B deficiency had marginal effects. Complement 3a receptor (C3aR), but not C5aR1 and C5aR2, deficiency mirrored the phenotype of <em>C3</em> <sup>-/-</sup> mice. C3 and C3aR deficiency were associated with reduced accumulation and functional skewing of tumor-associated macrophages, increased T cell activation and response to anti-PD-1 therapy. Transcriptional profiling of sarcoma infiltrating macrophages and monocytes revealed the enrichment of MHC II-dependent antigen presentation pathway in C3-deficient cells. In patients, C3aR expression correlated with a macrophage population signature and C3 deficiency-associated signatures predicted better clinical outcome. These results suggest that the lectin pathway and C3a/C3aR axis are key components of complement and macrophage-mediated sarcoma promotion and immunosuppression.</p>
Рис. 2. Варианты преΑсказанной Αоменной структуры патогенраспознающих моΛекуΛ гемоцитов моΛΛюсков Planorbarius corneus. a — фибриногенпоΑобные беΛки, b — гаΛектины, c — F-Λектины. УсΛовные обозначения и сокращения, зΑесь и ΑаΛее: горизонтаΛьные красные поΛоски — сигнаΛьный пептиΑ, горизонтаΛьные розовые — обΛасть низкой сΛожности, вертикаΛьные синие поΛоски — трансмембранная обΛасть, FBG — фибриногеновый Αомен, FTP — Αомен фукоΛектина, EGF — Αомен эпиΑермаΛьного фактора роста, EGF_CA — каΛьцийсвязывающий EGF-поΑобный Αомен, PAN_AP — APPLE-поΑобный Αомен, SCAN — обΛасть, богатая Λейцином, GLECT — гаΛактозосвязывающий Λектин, CLECT — Λектин C-типа, Gal-bind — гаΛактозиΑ–связывающий Λектин, ML — MD-2- поΑробный Αомен распознавания ΛипиΑов Fig. 2. Variants of the predicted domain structure of pattern recognition molecules from hemocytes of Planorbarius corneus molluscs. a — fibrinogen-related proteins, b — galectins, c — F-lectins. Symbols and abbreviations (here and further): horizontal red stripes — signal peptide, horizontal pink stripes — a low complexity region, vertical blue stripes — transmembrane region, FBG — fibrinogen-related domain, FTP — fucolectin domain, EGF — epidermal growth factor-like domain, EGF_CA — calcium-binding EGF-like domain, PAN_AP — APPLE-like domain, SCAN — leucine rich region, Apple — APPLE domain, GLECT — galactose-binding lectin, CLECT — C-type lectin, Gal-bind — galactoside-binding lectin, ML — MD-2-related lipid-recognition domain in Pathogen recognition molecules from hemocytes of Planorbarius corneus molluscs (Planorbidae, Pulmonata)
Рис. 2. Варианты преΑсказанной Αоменной структуры патогенраспознающих моΛекуΛ гемоцитов моΛΛюсков Planorbarius corneus. a — фибриногенпоΑобные беΛки, b — гаΛектины, c — F-Λектины. УсΛовные обозначения и сокращения, зΑесь и ΑаΛее: горизонтаΛьные красные поΛоски — сигнаΛьный пептиΑ, горизонтаΛьные розовые — обΛасть низкой сΛожности, вертикаΛьные синие поΛоски — трансмембранная обΛасть, FBG — фибриногеновый Αомен, FTP — Αомен фукоΛектина, EGF — Αомен эпиΑермаΛьного фактора роста, EGF_CA — каΛьцийсвязывающий EGF-поΑобный Αомен, PAN_AP — APPLE-поΑобный Αомен, SCAN — обΛасть, богатая Λейцином, GLECT — гаΛактозосвязывающий Λектин, CLECT — Λектин C-типа, Gal-bind — гаΛактозиΑ–связывающий Λектин, ML — MD-2- поΑробный Αомен распознавания ΛипиΑов Fig. 2. Variants of the predicted domain structure of pattern recognition molecules from hemocytes of Planorbarius corneus molluscs. a — fibrinogen-related proteins, b — galectins, c — F-lectins. Symbols and abbreviations (here and further): horizontal red stripes — signal peptide, horizontal pink stripes — a low complexity region, vertical blue stripes — transmembrane region, FBG — fibrinogen-related domain, FTP — fucolectin domain, EGF — epidermal growth factor-like domain, EGF_CA — calcium-binding EGF-like domain, PAN_AP — APPLE-like domain, SCAN — leucine rich region, Apple — APPLE domain, GLECT — galactose-binding lectin, CLECT — C-type lectin, Gal-bind — galactoside-binding lectin, ML — MD-2-related lipid-recognition domain
Low Plasma Mannose Binding Lectin (p-MBL) Level is a Risk Factor for Recurrent Pregnancy Loss (RPL)
ClinicalTrials.gov study NCT04017754. IPD Sharing: UNDECIDED. Countries: 1. Publications: 1.
A lectin receptor-like kinase controls self-pollen recognition in Phlox
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Data from: Mannose-binding lectin gene polymorphisms in the East Siberia and Russian Arctic populations
<p><b>Background:</b> Mannose-binding lectin (MBL) encoded by <i>MBL2</i> gene is a protein with the ability to form carbohydrate complexes with microbial wall promoting their subsequent elimination. Genetically determined levels of MBL can modify the risk and clinical characteristics of many infectious diseases. The frequency of <i>MBL2</i> genotypes exhibits significant population differences. The data on the distribution of <i>MBL2</i> genotypes among the aborigines of the Russian Arctic territories have not yet been published.</p> <p><b>Methods:</b> A total of 880 <a name="_Hlk41162363">specimens of </a><a name="_Hlk41162353">dried blood spots </a>of the newborns were genotyped. The newborns represented four populations: <a name="_Hlk28526418">Nenets, Dolgan-Nganasans</a>, Mixed <a name="_Hlk28526407">aboriginal population</a>, and Russians (<a name="_Hlk28526350">Caucasians</a>, Krasnoyarsk). Six polymorphisms of the <i>MBL2</i> gene were studied: rs11003125, rs7096206, rs7095891, rs5030737, rs1800450, and rs1800451.</p> <p><b>Results:</b> The frequency of the combined rare O allele (composed of the coding region variants rs5030737, rs1800450, and rs1800451) in the homozygous state was significantly higher in Russians: 10% vs 2% in Nenets and 1% in Dolgan-Nganosans (p<0.001 for Russians vs other populations). The frequency of the high-producing haplotype (HYPA) was 35.4% in the Russian newborns, in keeping with European populations (27-33%); 64% for Nenets and 56% for Dolgan-Nganasans, similar to the estimates obtained for Eskimos and North Amerinds (64-81%).</p> <p><b>Conclusion: </b>Our study results are in line with the hypothesis that human evolution has been moving in the direction of accumulation of the genotypes associated with low activity of the lectin complement activation pathway because of the prevalence of some intracellular infections such as tuberculosis, whereby low MBL activity may have a protective effect.</p>
9H0Q N terminal domain of BC2L-C lectin in complex with N-(beta-L-Fucopyranosyl)-biphenyl-3-carboxamide
<p>X-ray diffraction images collected on proxima 2 Soleil the 5th of july 2024 at SOLEIL synchrotron, Saint Aubin, France for PDB ID 9H0Q using a DECTRIS EIGER X 9M detector. X-ray dataset and xdsme processing for the structure of the N terminal domain of BC2L-C lectin in complex with N-(beta-L-Fucopyranosyl)-biphenyl-3-carboxamide. Rsolution was dut at 2.55 angstrom</p>
Fig. 1 in Cucurbitaceae phloem exudate lectins: Purification, molecular characterization and carbohydrate binding characteristics
Fig. 1. Multiple sequence alignment of the amino acid sequence of PP2 proteins from Cucurbitaceae species as well as from A. thaliana and A. graveolens. Sequences of A. graveolens (CBC70481.1), A. thaliana (CAB78986.1), Coccinia indica agglutinin CIA17 (P0DSP5.1), Cucumis sativus (KAE8649724.1), Cucumis melo (AAM74924.1), Luffa acutangula (C0HJV2.1), Cucurbita argyrosperma (CBC70491.1), Cucurbita arg. sororia (AAM82558.1), Cucurbita moschata (AAF74345.1), Cucurbita pepo (023518987.1), Cucurbita maxima (AAA33117.1), Cucurbita digitata (AAM82559.1) were taken from NCBI gene bank. Multiple sequence alignment was performed using Clustal Omega (https://www.ebi.ac.uk/Tools/msa/clustalo/). The highly conserved amino acids 100-Leu-Ile-Glu-Val-Ser-Trp-105 and 199-Trp- Lys-200, which are important for chitooligosaccharide binding are shown in boxes. The residue numbers correspond to the primary structure of PPL.
Fig. 6 in Cucurbitaceae phloem exudate lectins: Purification, molecular characterization and carbohydrate binding characteristics
Fig. 6. Interaction of chitohexaose with the carbohydrate binding cleft of PPL, showing the amino acid residues involved in carbohydrate binding. The binding site was divided into three subsites as indicated by arrows: subsite 1 (Leu-100, Glu-102), subsite 2 (Ile-101, Ser-104, Trp-105) and subsite 3 (Trp-199, Lys- 200). Only three GlcNAc residues from the non-reducing end of chitohexaose are seen to interact with the binding cleft. GlcNAc residues at the reducing end interact with another PPL monomer (shown in the circle at the top left corner). Reproduced from Bobbili et al. (2014). Copyright (2014) Elsevier.
Fig. 3. A LigPlot depicting the interactions between CIA17 in Cucurbitaceae phloem exudate lectins: Purification, molecular characterization and carbohydrate binding characteristics
Fig. 3. A LigPlot depicting the interactions between CIA17 and bound chitotetraose. Adapted from the Supporting Information of Bobbili et al. (2019). Copyright (2019) Elsevier.
Fig. 5. A in Cucurbitaceae phloem exudate lectins: Purification, molecular characterization and carbohydrate binding characteristics
Fig. 5. A Complex of chitohexaose with PPL dimer obtained from molecular docking studies and optimized by molecular dynamics simulations. Reproduced from (Narahari et al., 2011b). Copyright (2011) American Chemical Society.
Influence of Periodontal Disease Treatment on Serum Levels of Sirtuin 1 and Mannose-binding Lectin
ClinicalTrials.gov study NCT03753451. IPD Sharing: NO. Countries: 1. Publications: 5.
Genetic Polymorphisms of Mannan-binding Lectin (MBL)and Serum Levels of MBL in Patients With Endometriosis
ClinicalTrials.gov study NCT01738932. IPD Sharing: Not stated. Countries: 1. Publications: 2.
Mistletoe Lectin in Treating Patients With Refractory Advanced Solid Tumors
ClinicalTrials.gov study NCT00006477. IPD Sharing: Not stated. Countries: 2. Publications: 1.
Data from: Mannose-binding lectin gene polymorphisms in the East Siberia and Russian Arctic populations
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Data from: A lectin-mediated resistance of higher fungi against predators and parasites
Fruiting body lectins are ubiquitous in higher fungi and characterized by being synthesized in the cytoplasm and up-regulated during sexual development. The function of these lectins is unclear. A lack of phenotype in sexual development upon inactivation of the respective genes argues against a function in this process. We tested a series of characterized fruiting body lectins from different fungi for toxicity towards the nematode Caenorhabditis elegans, the mosquito Aedes aegypti and the amoeba Acanthamoeba castellanii. Most of the fungal lectins were found to be toxic towards at least one of the three target organisms. By altering either the fungal lectin or the glycans of the target organisms, or by including soluble carbohydrate ligands as competitors, we demonstrate that the observed toxicity is dependent on the interaction between the fungal lectins and specific glycans in the target organisms. The toxicity was found to be dose-dependent such that low levels of lectin were no longer toxic but still led to food avoidance by C. elegans. Finally, we show, in an ecologically more relevant scenario, that challenging the vegetative mycelium of Coprinopsis cinerea with the fungal-feeding nematode Aphelenchus avenae induces the expression of the nematotoxic fruiting body lectins CGL1 and CGL2. Based on these findings, we propose that filamentous fungi possess an inducible resistance against predators and parasites mediated by lectins that are specific for glycans of these antagonists.
Lectine Pathway in Unstable Carotid Plaque
ClinicalTrials.gov study NCT03822195. IPD Sharing: Not stated. Countries: 0. Publications: 8.
Electrochemical Biosensor Based on Lectin-functionalized Nitrogen, Sulfur-doped Graphene Quantum Dot Decorated Gold Nanoparticles for Breast Cancer Diagnosis: From Academic Research to Clinical Transl
ClinicalTrials.gov study NCT07034248. IPD Sharing: Not stated. Countries: 0. Publications: 0.
Data from: A lectin-mediated resistance of higher fungi against predators and parasites
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qPCR array study for cell cycle related genes in Caco-2 cells treated with human lectin ZG16p
GEO Series GSE84321. Homo sapiens. 6 samples. Type: Expression profiling by RT-PCR.
rBC2LCN lectin detects early-stage HER2-positive breast cancer
GEO Series GSE139670. Homo sapiens. 8 samples. Type: Expression profiling by array.
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Allen Brain Atlas
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