lectin family
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2021 ◽  
Vol 99 (Supplement_3) ◽  
pp. 266-267
Author(s):  
Bharath Kumar Mulakala ◽  
Eluka-Okoludoh Eboghoye ◽  
Kingsley Ekwemalor ◽  
Mulumebet Worku

Abstract The objective of this study was to assess the expression and secretion of Galectins (Gal) in cow milk. Cow milk contains a range of proteins of moderate or low abundance that contribute to host defense. However, host defense proteins in milk were not fully discovered. Galectins belong to the lectin family that recognizes specific carbohydrates on cells and involved in innate immune responses. Holstein Friesian cows (n = 16) from North Carolina A&T diary unit were used for this study. Based on the Dairy Heard farm index, eight cows each were assigned to the high or low SCC group. Total RNA was isolated from somatic cells converted to cDNA, for real-time PCR. Cow-specific Gal primers were designed using the NCBI Primer 3 tool. Housekeeping genes RPLP0, UCHL5, and beta-actin were served as internal controls. Total whey protein concentration was determined using a BCA kit. Secretion of Gal was assessed using a specific ELISA kit. Data were analyzed using the Proc ANOVA procedure in SAS 9.4. Galectin was transcribed and secreted in milk. Transcription of Galectin was different in both HSCC and LSCC groups. Total protein concentration remained the same in both groups. Secretion of galectins was different between the HSCC and LSCC group but not significantly. The observed difference in HSCC and LSCC cows warrants further study using more animals; this will aid in a better definition of the role of Gal in the milk host defense. These may also aid as the diagnostic biomarkers for certain infections.


Marine Drugs ◽  
2021 ◽  
Vol 19 (9) ◽  
pp. 474
Author(s):  
Tatyana O. Mizgina ◽  
Irina V. Chikalovets ◽  
Valentina I. Molchanova ◽  
Rustam H. Ziganshin ◽  
Oleg V. Chernikov

Lectin from the bivalve Glycymeris yessoensis (GYL) was purified by affinity chromatography on porcine stomach mucin–Sepharose. GYL is a dimeric protein with a molecular mass of 36 kDa, as established by SDS-PAGE and MALDI-TOF analysis, consisting of 18 kDa subunits linked by a disulfide bridge. According to circular dichroism data, GYL is a β/α-protein with the predominance of β-structure. GYL preferentially agglutinates enzyme-treated rabbit erythrocytes and recognizes glycoproteins containing O-glycosidically linked glycans, such as porcine stomach mucin (PSM), fetuin, thyroglobulin, and ovalbumin. The amino acid sequences of five segments of GYL were acquired via mass spectrometry. The sequences have no homology with other known lectins. GYL is Ca2+-dependent and stable over a range above a pH of 8 and temperatures up to 20 °C for 30 min. GYL is a pattern recognition receptor, as it binds common pathogen-associated molecular patterns, such as peptidoglycan, LPS, β-1,3-glucan and mannan. GYL possesses a broad microbial-binding spectrum, including Gram-positive (Bacillus subtilis, Staphylococcus aureus) and Gram-negative bacteria (Escherichia coli, Vibrio proteolyticus), but not the fungus Candida albicans. Expression levels of GYL in the hemolymph were significantly upregulated after bacterial challenge by V. proteolyticus plus environmental stress (diesel fuel). Results indicate that GYL is probably a new member of the C-type lectin family, and may be involved in the immune response of G. yessoensis to bacterial attack.


2021 ◽  
Vol 22 (15) ◽  
pp. 8284
Author(s):  
Soran Mohammed ◽  
Natalie Ferry

Sialic acid (Sia) is considered as one of the most important biomolecules of life since its derivatives and terminal orientations on cell membranes and macromolecules play a major role in many biological and pathological processes. To date, there is only a limited number of active molecules that can selectively bind to Sia and this limitation has made the study of this glycan challenging. The lectin superfamily is a well-known family of glycan binding proteins, which encompasses many strong glycan binding peptides with diverse glycan affinities. Mistletoe lectin (ML) is considered one of the most active members of lectin family which was initially classified in early studies as a galactose binding lectin; more recent studies have suggested that the peptide can also actively bind to Sia. However, the details with respect to Sia binding of ML and the domain responsible for this binding are left unanswered because no comprehensive studies have been instigated. In this study, we sought to identify the binding domain responsible for the sialic acid affinity of mistletoe lectin isoform I (MLI) in comparison to the binding activity of elderberry lectin isoform I (SNA), which has long been identified as a potent Sia binding lectin. In order to execute this, we performed computational carbohydrate-protein docking for MLB and SNA with Neu5Ac and β-Galactose. We further analyzed the coding sequence of both lectins and identified their glycan binding domains, which were later cloned upstream and downstream to green fluorescent protein (GFP) and expressed in Escherichia coli (E. coli). Finally, the glycan affinity of the expressed fusion proteins was assessed by using different biochemical and cell-based assays and the Sia binding domains were identified.


2021 ◽  
Vol 22 (13) ◽  
pp. 6661
Author(s):  
Tereza Koukalová ◽  
Petr Kovaříček ◽  
Pavla Bojarová ◽  
Valentino L. P. Guerra ◽  
Vladimír Vrkoslav ◽  
...  

The monolayer character of two-dimensional materials predestines them for application as active layers of sensors. However, their inherent high sensitivity is always accompanied by a low selectivity. Chemical functionalization of two-dimensional materials has emerged as a promising way to overcome the selectivity issues. Here, we demonstrate efficient graphene functionalization with carbohydrate ligands—chitooligomers, which bind proteins of the lectin family with high selectivity. Successful grafting of a chitooligomer library was thoroughly characterized, and glycan binding to wheat germ agglutinin was studied by a series of methods. The results demonstrate that the protein quaternary structure remains intact after binding to the functionalized graphene, and that the lectin can be liberated from the surface by the addition of a binding competitor. The chemoenzymatic assay with a horseradish peroxidase conjugate also confirmed the intact catalytic properties of the enzyme. The present approach thus paves the way towards graphene-based sensors for carbohydrate–lectin binding.


2021 ◽  
Vol 28 (1) ◽  
Author(s):  
Pei-Shan Sung ◽  
Shie-Liang Hsieh

AbstractDysregulated formation of neutrophil extracellular traps (NETs) is observed in acute viral infections. Moreover, NETs contribute to the pathogenesis of acute viral infections, including those caused by the dengue virus (DV) and severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Furthermore, excessive NET formation (NETosis) is associated with disease severity in patients suffering from SARS-CoV-2-induced multiple organ injuries. Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) and other members of C-type lectin family (L-SIGN, LSECtin, CLEC10A) have been reported to interact with viral glycans to facilitate virus spreading and exacerbates inflammatory reactions. Moreover, spleen tyrosine kinase (Syk)-coupled C-type lectin member 5A (CLEC5A) has been shown as the pattern recognition receptor for members of flaviviruses, and is responsible for DV-induced cytokine storm and Japanese encephalomyelitis virus (JEV)-induced neuronal inflammation. Moreover, DV activates platelets via CLEC2 to release extracellular vesicles (EVs), including microvesicles (MVs) and exosomes (EXOs). The DV-activated EXOs (DV-EXOs) and MVs (DV-MVs) stimulate CLEC5A and Toll-like receptor 2 (TLR2), respectively, to enhance NET formation and inflammatory reactions. Thus, EVs from virus-activated platelets (PLT-EVs) are potent endogenous danger signals, and blockade of C-type lectins is a promising strategy to attenuate virus-induced NETosis and intravascular coagulopathy.


2021 ◽  
Vol 5 (5) ◽  
pp. 1305-1309 ◽  
Author(s):  
Shang-Chuen Wu ◽  
Connie M. Arthur ◽  
Jianmei Wang ◽  
Hans Verkerke ◽  
Cassandra D. Josephson ◽  
...  

Key Points The RBD of SARS-CoV-2 shares sequence similarity with an ancient lectin family known to bind blood group antigens. SARS-CoV-2 RBD binds the blood group A expressed on respiratory epithelial cells, directly linking blood group A and SARS-CoV-2.


2021 ◽  
Vol 22 (3) ◽  
pp. 1081
Author(s):  
Tomohisa Ogawa ◽  
Rie Sato ◽  
Takako Naganuma ◽  
Kayeu Liu ◽  
Saho Sato ◽  
...  

Previously, we isolated jacalin-related lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of Pteria penguin (Mabe) pearl shell. They showed the sequence homology with the plant lectin family, jacalin-related β-prism fold lectins (JRLs). While PPL3s and PPL4 shared only 35%–50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these lectins and compared their biomineral functions. It was found that these lectins showed different effects on CaCO3 crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO3 calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO3 crystalization; however, PPL4 regulated the size of crystals collaborated with N-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this lectin family involved in the mollusk shell formation.


Author(s):  
Wenxuan Hong ◽  
Ming Kong ◽  
Mengwen Qi ◽  
Hui Bai ◽  
Zhiwen Fan ◽  
...  

Fulminant hepatitis (FH) is a major cause of acute liver failure. Concanavalin A (ConA) belongs to the lectin family and is frequently used as an inducer of FH in animal models. ConA induced FH is characterized by massive accumulation of T lymphocytes in the liver. A host of chemoattractive substances are known to promote T cell homing to the liver during acute hepatitis. Here we investigated the involvement of Brahma-related gene 1 (BRG1), a chromatin remodeling protein, in FH. BRG1-flox mice were crossed to Alb-Cre mice to generate hepatocyte conditional BRG1 knockout (LKO) mice. The mice were peritoneally injected with a single dose of ConA to induce FH. BRG1 deficiency mitigated ConA-induced FH in mice. Consistently, there were fewer T lymphocyte infiltrates in the LKO livers compared to the wild type (WT) livers paralleling downregulation of T cell specific cytokines. Further analysis revealed that BRG1 deficiency repressed the expression of several chemokines critical for T cell homing including nephronectin (Npnt). BRG1 knockdown blocked the induction of Npnt in hepatocytes and attenuated T lymphocyte migration in vitro, which was reversed by the addition of recombinant nephronectin. Mechanistically, BRG1 interacted with β-catenin to directly bind to the Npnt promoter and activate Npnt transcription. Importantly, a positive correlation between infiltration of CD3+ T lymphocyes and nephronectin expression was detected in human acute hepatitis biopsy specimens. In conclusion, our data identify a novel role for BRG1 as a promoter of T lymphocyte trafficking by activating Npnt transcription in hepatocytes. Targeting the BRG1-Npnt axis may yield novel therapeutic solutions for FH.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Mehul B. Ganatra ◽  
Vladimir Potapov ◽  
Saulius Vainauskas ◽  
Anthony Z. Francis ◽  
Colleen M. McClung ◽  
...  

AbstractThe BLL lectin from the edible Japanese “Kurokawa” mushroom (Boletopsis leucomelaena) was previously reported to bind to N-glycans harboring terminal N-acetylglucosamine (GlcNAc) and to induce apoptosis in a leukemia cell line. However, its gene has not been reported. In this study, we used a transcriptomics-based workflow to identify a full-length transcript of a BLL functional ortholog (termed BGL) from Boletopsis grisea, a close North American relative of B. leucomelaena. The deduced amino acid sequence of BGL was an obvious member of fungal fruit body lectin family (Pfam PF07367), a highly conserved group of mushroom lectins with a preference for binding O-glycans harboring the Thomsen–Friedenreich antigen (TF-antigen; Galβ1,3GalNAc-α-) and having two ligand binding sites. Functional characterization of recombinant BGL using glycan microarray analysis and surface plasmon resonance confirmed its ability to bind both the TF-antigen and β-GlcNAc-terminated N-glycans. Structure-guided mutagenesis of BGL’s two ligand binding clefts showed that one site is responsible for binding TF-antigen structures associated with O-glycans, whereas the second site specifically recognizes N-glycans with terminal β-GlcNAc. Additionally, the two sites show no evidence of allosteric communication. Finally, mutant BGL proteins having single functional bindings site were used to enrich GlcNAc-capped N-glycans or mucin type O-glycopeptides from complex samples in glycomics and glycoproteomics analytical workflows.


2020 ◽  
Vol 17 (4) ◽  
pp. 729-737
Author(s):  
Le Dinh Hung ◽  
Dinh Thanh Trung

A lectin from the marine sponge Stylissa flexibilis, designated as SFL, was purified by cold ethanol precipitation followed by ion exchange chromatography on DEAE Sepharose column and Sephacryl S-200 gel filtration. SFL is a dimeric glycoprotein of 32 kDa subunits linked by a disulfide bridge with a molecular mass of 64 kDa by SDS-PAGE and 65 kDa by Sephacryl S-200 gel filtration chromatography. The lectin preferentially agglutinated enzyme treated human A erythrocytes, whereas it did not agglutinate any type of rabbit, human B and O erythrocytes, irrespective of treatment with enzymes. The hemagglutination activity of lectin was strongly inhibited by monosaccharide, D-galactose and glycoproteins, asialo-porcine stomach mucin and asialo-fetuin, indicating that lectin is specific for O-glycans. Activity of SFL was stable over a range of pH from 5 to 8, up to 60 °C for 30 min and its activity was Ca2+ dependent, indicating that SFL was belonged to the C-type lectin family and requires metal for biological activity. SFL caused agglutination of Vibrio alginolyticus and V. parahaemolyticus in a dose dependent manner and inhibited the growth rate of these bacterial strains, suggesting that the lectin caused the agglutination through binding to the target receptor(s) on the surface of Vibrios. Thus, SFL can be considered as a good source of lectin(s) being useful as carbohydrate probe and antibacterial reagent.


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