Effective glycoanalysis with Maackia amurensis lectins requires a clear understanding of their binding specificities.
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ABSTRACT:
SUBMITTER: Geisler C
PROVIDER: S-EPMC3130539 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature
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Effective glycoanalysis with Maackia amurensis lectins requires a clear understanding of their binding specificities.
Geisler Christoph C Jarvis Donald L DL
Glycobiology 20110801 8
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Project description:The pathophysiology of autistic spectrum disorder (ASD) is not fully understood and there are no diagnostic or predictive biomarkers. Glycosylation modified as many as 70% of all human proteins can sensitively reflect various pathological changes. However, little is known about the alterations of glycosylation and glycoproteins in ASD. In this study, serum glycopattern and the maackia amurensis lectin-II binding glycoproteins (MBGs) in 65 children with ASD and 65 age-matched typically developing (TD) children were compared by using lectin microarrays and lectin-magnetic particle conjugate-assisted LC-MS/MS analyses. Expression of Siaα2-3 Gal/GalNAc was significantly increased in pooled (fold change = 3.33, p < 0.001) and individual (p = 0.009) serum samples from ASD versus TD children. A total of 194 and 217 MGBs were identified from TD and ASD sera respectively, of which 74 proteins were specially identified or up-regulated in ASD. Bioinformatic analysis revealed abnormal complement cascade and aberrant regulation of response-to-stimulus that might be novel makers or markers for ASD. Moreover, increase of APOD α2-3 sialoglycosylation could sensitively and specifically distinguish ASD samples from TD samples (AUC is 0.88). In conclusion, alteration of MBGs expression and their sialoglycosylation may serve as potential biomarkers for diagnosis of ASD, and provide useful information for investigations into the pathogenesis of ASD.
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Project description:In this study, we isolated a new isoflavanostilbene maackiapicevestitol (1) as a mixture of two stable conformers 1a and 1b as well as five previously known dimeric and monomeric stilbens: piceatannol (2), maackin (3), scirpusin A (4), maackiasine (5), and maackolin (6) from M. amurensis heartwood, using column chromatography on polyamide, silicagel, and C-18. The structures of these compounds were elucidated by NMR, HR-MS, and CD techniques. Maksar® obtained from M. amurensis heartwood and polyphenolics 1-6 possessed moderate anti-HSV-1 activity in cytopathic effect (CPE) inhibition and RT-PCR assays. A model of PQ-induced neurotoxicity was used to study the neuroprotective potential of polyphenolic compounds from M. amurensis. Maksar® showed the highest neuroprotective activity and increased cell viability by 18% at a concentration of 10 μg/mL. Maackolin (6) also effectively increased the viability of PQ-treated Neuro-2a cells and the value of mitochondrial membrane potential at concentrations up to 10 μΜ. Maksar® and compounds 1-6 possessed higher FRAP and DPPH-scavenging effects than quercetin. However, only compounds 1 and 4 at concentrations of 10 μM as well as Maksar® (10 μg/mL) statistically significantly reduced the level of intracellular ROS in PQ-treated Neuro-2a cells.
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Project description:BackgroundLectins are carbohydrate-binding molecules that can bind specifically to the sugar residues of glycoconjugates and are found in almost all organisms. Plant lectins subjected to many studies reported exhibiting anti-cancer activity. This study aimed to investigate the possible molecular mechanisms of Maackia amurensis leukoagglutinin II (MAL-II) treated ATCCs.Methods and resultsWe tested the effects of MAL-II, which is isolated from Amur seeds, on cancerous features of 8505C human anaplastic thyroid cancer cells (ATCCs) on a large scale using RNA-Seq. Transcriptome analysis was performed using Illumina next-generation sequencing technology by using cDNA libraries obtained from total RNA isolates of ATCCs treated with 0.25 µM MAL-II for 24 h. Gene ontology and pathway enrichment analysis were performed for the systematic analysis of gene functions. Moreover, we validated RNA-Seq findings using qPCR. Our results showed that many cancer-related genes such as TENM4, STIM2, SYT12, PIEZO2, ABCG1, SPNS2, ARRB1, and IRX5 were downregulated and many anticancer genes such as HSPA6, G0S2, TNFAIP3, GEM, GADD45G, RND1, SERPINB2, and IL24 were upregulated. Also, pathway enrichment analysis showed that differentially expressed genes were found to be associated with Ras, p53, and apoptosis signaling pathways, which are some important signal transduction pathways in development, proliferation, stem cell control, and carcinogenesis.ConclusionCollectively, our results show that MAL-II treatment reveals significant antitumor activity by changing the expression of many cancer-related genes and implies that MAL-II treatment might be a potential candidate molecule to inhibit the malignancy of human anaplastic thyroid cancer.
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Project description:There is a high desire for novel targets/biomarkers to diagnose and treat colorectal cancer (CRC). Here, an approach starting from a polyacrylamide hydrogel-based lectin microarray is presented to screen the high expression of glycans on the CRC cell surface and to identify new lectin biomarkers for CRC. Three common CRC cell lines (SW480, SW620, and HCT116) and one normal colon cell line (NCM460) are profiled on the microarray with 27 lectins. The experimental results reveal that CRC cells highly express the glycans with d-galactose, d-glucose, and/or sialic acid residues, and Uelx Europaeus Agglutinin-I (UEA-I) exhibits reasonable specificity with SW480 cells. After conjugation of UEA-I with silica-coated NaGdF4:Yb3+, Er3+@NaGdF4 upconversion nanoparticles, the follow-up in vitro and in vivo experiments provide further evidence on that UEA-I can serve as tumor-targeting molecule to diagnose SW480 tumor by multimodal imaging including upconversion luminescence imaging, T1-weighted magnetic resonance imaging, and X-ray computed tomography imaging.
| S-EPMC6010763 | biostudies-literature
Project description:PurposeOral cancer causes over 120,000 deaths annually and affects the quality of life for survivors. Over 90% of oral cancers are derived from oral squamous cell carcinoma cells (OSCCs) which are generally resistant to standard cytotoxic chemotherapy agents. OSCC cells often exhibit increased TGFβ and PDPN receptor activity compared to nontransformed oral epithelial cells. Maackia amurensis seed lectin (MASL) can target the PDPN receptor and has been identified as a novel agent that can be used to treat oral cancer. However, mechanisms by which MASL inhibits OSCC progression are not yet clearly defined.MethodsHere, we performed cell migration and cytotoxicity assays to assess the effects of MASL on OSCC motility and viability at physiologically relevant concentrations. We then performed comprehensive transcriptome analysis combined with transcription factor reporter assays to investigate the how MASL affects OSCC gene expression at these concentration. Key data were then confirmed by western blotting to evaluate the effects of MASL on gene expression and kinase signaling activity at the protein level.ResultsMASL significantly affected the expression of about 27% of approximately 15,000 genes found to be expressed by HSC-2 cells used to model OSCC cells in this study. These genes affected by MASL include members of the TGFβ-SMAD, JAK-STAT, and Wnt-βCTN signaling pathways. In particular, MASL decreased expression of PDPN, SOX2, and SMAD5 at the RNA and protein levels. MASL also inhibited SMAD and MAPK activity, and exhibited potential for combination therapy with doxorubicin and 5-fluorouracil.ConclusionsTaken together, results from this study indicate that MASL decreases activity of JAK-STAT, TGFβ-SMAD, and Wnt-βCTN signaling pathways to inhibit OSCC growth and motility. These data suggest that further studies should be undertaken to determine how MASL may also be used alone and in combination with other agents to treat oral cancer.
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Project description:Carbohydrate-lectin interactions dictate a range of signalling and recognition processes in biological systems. The exploitation of these, particularly for diagnostic applications, is complicated by the inherent promiscuity of lectins along with their low affinity for individual glycans which themselves are challenging to access (bio)synthetically. Inspired by how a 'tongue' can discriminate between hundreds of flavours using a minimal set of multiplexed sensors and a training algorithm, here individual lectins are 'profiled' based on their unique binding profile (barcode) to a range of monosaccharides. By comparing the relative binding of a panel of 5 lectins to 3 monosaccharide-coated surfaces, it was possible to generate a training algorithm that enables correct identification of lectins, even those with similar glycan preferences. This is demonstrated to be useful for discrimination between the cholera and ricin toxin lectins showing the potential of this minimalist approach for exploiting glycan complexity.
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Project description:Mammalian Quaking (QKI) protein, a member of STAR family of proteins is a mRNA-binding protein, which post-transcriptionally modulates the target RNA. QKI protein possesses a maxi-KH domain composed of single heterogeneous nuclear ribonucleoprotein K homology (KH) domain and C-terminal QUA2 domain, that binds a sequence-specific QKI RNA recognition element (QRE), CUAAC. To understand the binding specificities for different mRNA sequences of the KH-QUA2 domain of QKI protein, we introduced point mutations at different positions in the QRE resulting in twelve different mRNA sequences with single nucleotide change. We carried out long unbiased molecular dynamics simulations using two different sets of recently updated forcefield parameters: AMBERff14SB+RNAχOL3 and CHARMM36 (with CMAP correction). We analyzed the changes in intermolecular dynamics as a result of mutation. Our results show that AMBER forcefields performed better to model the interactions between mRNA and protein. We also calculated the binding affinities of different mRNA sequences and found that the relative order correlates to the reported experimental studies. Our study shows that the favorable binding with the formation of stable complex will occur when there is an increase of the total intermolecular contacts between mRNA and protein, but without the loss of native contacts within the KH-QUA domain.
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Project description:Pathogenic enveloped viruses are covered with a glycan shield that provides a dual function: the glycan structures contribute to virus protection as well as host cell recognition. The three classical types of N-glycans, in particular complex glycans, high-mannose glycans, and hybrid glycans, together with some O-glycans, participate in the glycan shield of the Ebola virus, influenza virus, human cytomegalovirus, herpes virus, human immunodeficiency virus, Lassa virus, and MERS-CoV, SARS-CoV, and SARS-CoV-2, which are responsible for respiratory syndromes. The glycans are linked to glycoproteins that occur as metastable prefusion glycoproteins on the surface of infectious virions such as gp120 of HIV, hemagglutinin of influenza, or spike proteins of beta-coronaviruses. Plant lectins with different carbohydrate-binding specificities and, especially, mannose-specific lectins from the Vicieae tribe, such as pea lectin and lentil lectin, can be used as glycan probes for targeting the glycan shield because of their specific interaction with the α1,6-fucosylated core Man3GlcNAc2, which predominantly occurs in complex and hybrid glycans. Other plant lectins with Neu5Ac specificity or GalNAc/T/Tn specificity can also serve as potential glycan probes for the often sialylated complex glycans and truncated O-glycans, respectively, which are abundantly distributed in the glycan shield of enveloped viruses. The biomedical and therapeutical potential of plant lectins as antiviral drugs is discussed.
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Project description:COVID-19 was declared an international public health emergency in January, and a pandemic in March of 2020. There are over 23 million confirmed COVID-19 cases that have cause over 800 thousand deaths worldwide as of August 19th, 2020. COVID-19 is caused by the SARS-CoV-2 virus. SARS-CoV-2 presents a surface "spike" protein that binds to the ACE2 receptor to infect host cells. In addition to the respiratory tract, SARS-Cov-2 can also infect cells of the oral mucosa, which also express the ACE2 receptor. The spike and ACE2 proteins are highly glycosylated with sialic acid modifications that direct viral-host interactions and infection. Maackia amurensis seed lectin (MASL) has a strong affinity for sialic acid modified proteins and can be used as an antiviral agent. Here, we report that MASL targets the ACE2 receptor, decreases ACE2 expression and glycosylation, suppresses binding of the SARS-CoV-2 spike protein, and decreases expression of inflammatory mediators by oral epithelial cells that cause ARDS in COVID-19 patients. This work identifies MASL as an agent with potential to inhibit SARS-CoV-2 infection and COVID-19 related inflammatory syndromes.
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