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1.
Mar Drugs ; 20(2)2022 Jan 26.
Artigo em Inglês | MEDLINE | ID: mdl-35200632

RESUMO

Marine algae are an excellent source of novel lectins. The isolation of lectins from marine algae expands the diversity in structure and carbohydrate specificities of lectins isolated from other sources. Marine algal lectins have been reported to have antiviral, antitumor, and antibacterial activity. Lectins are typically isolated from marine algae by grinding the algal tissue with liquid nitrogen and extracting with buffer and alcohol. While this method produces higher yields, it may not be sustainable for large-scale production, because a large amount of biomass is required to produce a minute amount of compound, and a significant amount of waste is generated during the extraction process. Therefore, non-destructive extraction using algal culture water could be used to ensure a continuous supply of lectins without exclusively disrupting the marine algae. This review discusses the traditional and recent advancements in algal lectin extraction methods over the last decade, as well as the steps required for large-scale production. The challenges and prospects of various extraction methods (destructive and non-destructive) are also discussed.


Assuntos
Organismos Aquáticos/química , Lectinas/isolamento & purificação , Animais , Clorófitas/química , Humanos , Lectinas/química , Lectinas/farmacologia , Feófitas/química , Rodófitas/química
2.
Molecules ; 27(3)2022 Jan 25.
Artigo em Inglês | MEDLINE | ID: mdl-35164055

RESUMO

Rice weevil, Sitophilus oryzae L. (Coleoptera: Curculionidae), is one of the most destructive stored-product pests that is resistant to a wide range of chemical insecticides. In the present study, we investigated whether a lectin extracted from Polygonum persicaria L. (PPA) can be used as a biorational agent to control such insect pests. Along with the lethal digestive assay, the sub-lethal insecticidal activities of PPA, including the effects on digestive, detoxifying, and antioxidant enzyme activities, were evaluated against S. oryzae adults. The effect of feeding a diet containing PPA and carob extract as a food attractant on the mortality of S. oryzae adults was also investigated. Feeding on the diet containing PPA resulted in a significant mortality of S. oryzae adults with a LC50 (Lethal Concentration to kill 50% of insects) of 3.68% (w/w). The activity of digestive enzymes, including α-amylase, α-glucosidase, TAG-lipase, trypsin, chymotrypsin, elastase, and carboxy- and aminopeptidase, were decreased by the sub-lethal concentration of PPA. Detoxifying and antioxidant enzymes, including esterase, superoxide dismutase, catalase, glutathione-S-transferase, ascorbate peroxidase, glucose 6-phosphate dehydrogenase, and malondialdehyde, were activated in adults affected by PPA. These findings indicated that PPA, in addition to causing digestive disorders, leads to oxidative stress in S. oryzae. The presence of carob extract had no effect on the PPA-induced mortality of the insect. According to the results of the present study, PPA has promising insecticidal efficiency against S. oryzae. In addition, the usage of PPA with a food attractant carob extract in bait traps can be recommended as a new biorational formulation in S. oryzae management.


Assuntos
Inseticidas/farmacologia , Lectinas/farmacologia , Extratos Vegetais/farmacologia , Polygonum/química , Gorgulhos/efeitos dos fármacos , Animais , Ativação Enzimática/efeitos dos fármacos , Inseticidas/isolamento & purificação , Lectinas/isolamento & purificação , Estresse Oxidativo/efeitos dos fármacos
3.
FEMS Microbiol Lett ; 369(1)2022 02 24.
Artigo em Inglês | MEDLINE | ID: mdl-35142828

RESUMO

Nematode-trapping fungi are natural enemies of nematodes in nature. Arthrobotrys oligospora, a typical nematode-trapping fungus with a clear genetic background, can capture and infect nematodes by forming adhesive three-dimensional networks. Lectins, a class of glycoproteins containing glycosyl-specific recognition domains, play an important role in biological recognition. However, the fucose-specific lectins have rarely been studied regarding the process of preying on nematodes. In this study, we characterized the biological role of the fucose-specific lectin-encoding gene AOL_s00054g276 (g276) in A. oligospora. The gene g276 was first deleted based on homologous recombination, then the phenotype and nematocidal activity of the Δg276 mutant was evaluated. The results showed that the deletion of gene g276 delayed trap formation and weakened its nematocidal activity; however, mycelial growth, conidia production, conidial germination rates and adaption to environmental stresses were not affected. Our results suggest that the fucose-specific lectin-encoding gene g276 might be associated with the morphogenesis of this fungus, and its deletion resulted in a significantly low density of three-dimensional traps (P < 0.05) and a significantly low nematode-trapping efficiency (P < 0.001). These findings provide a basis for further elucidating the mechanism of A. oligospora preying on nematodes and lay a foundation for the development and utilization of fungal-derived lectins for nematode control in the future.


Assuntos
Ascomicetos , Nematoides , Animais , Antinematódeos , Ascomicetos/genética , Lectinas/genética , Lectinas/farmacologia
4.
J Biomol Struct Dyn ; 40(8): 3560-3580, 2022 May.
Artigo em Inglês | MEDLINE | ID: mdl-33200676

RESUMO

A novel lectin was purified from newly cyanobacterium isolate, Oscillatoria acuminate MHM-632 MK014210.1 using affinity chromatography with a molecular weight of 120 kDa under native-PAGE and 30 kDa on reducing-PAGE, represented tetramer nature of this lectin. Oscillatorial lectin showed stability at 60 °C for 30 min, pH-dependent, with the highest activities over the pH range of 6-8, and required zinc ions to express its full activity. Oscillatorial lectin is a glycan-binding protein with a neutral carbohydrate content of 7.0% as evaluated by the phenol-sulfuric acid method. Polyols and α- glycosides polymer of mannose sugar or sugars alcohol were completely inhibited oscillatorial lectin with MIC of 0.195 mM, while ß-glycosides sugars did not show any inhibition effect. The oscillatorial lectin has anti-proliferative activity against Huh-7 and MCF-7 cancer cells and inhibited their proliferation with EC50 values of 106.75 µg/ml and 254.14 µg/ml, respectively. Besides the anticancer effect, oscillatorial lectin also has potent antiviral activity against HSV-1 in a dose-dependent manner via virions neutralization and inhibition of viral replication with IC50 values of 90.95 ng/ml and 131.3 ng/ml, respectively. The unique carbohydrate affinity of oscillatorial lectin provides insight into its use as a promising candidate in many biotechnological applications, like fighting viral infection and combating cancer disease.Communicated by Ramaswamy H. Sarma.


Assuntos
Lectinas , Oscillatoria , Antivirais/farmacologia , Bactérias , Carboidratos/química , Glicosídeos , Humanos , Lectinas/química , Lectinas/farmacologia , Manose/química
5.
Exp Cell Res ; 410(1): 112949, 2022 01 01.
Artigo em Inglês | MEDLINE | ID: mdl-34843714

RESUMO

Glioma stem/initiating cells have been considered a major cause of tumor recurrence and therapeutic resistance. In this study, we have established a new glioma stem-like cell (GSC), named U373-GSC, from the U373 glioma cell line. The cells exhibited stemness properties, e.g., expression of stem cell markers, self-renewal activity, multi-lineage differentiating abilities, and drug resistance. Using U373-GSC and GSC-03A-a GSC clone previously established from patient tissue, we have identified a novel GSC-associated sialic acid-modified glycan commonly expressed in both cell lines. Lectin fluorescence staining showed that Maackia amurensis lectin II (MAL-II)-binding alpha2,3-sialylated glycan (MAL-SG) was highly expressed in GSCs, and drastically decreased during FBS induced differentiation to glioma cells or little in the parental cells. Treatment of GSCs by MAL-II, compared with other lectins, showed that MAL-II significantly suppresses cell viability and sphere formation via induction of cell cycle arrest and apoptosis of the GSCs. Similar effects were observed when the cells were treated with a sialyltransferase inhibitor or sialidase. Taken together, we demonstrate for the first time that MAL-SGs/alpha-2,3 sialylations are upregulated and control survival/maintenances of GSCs, and their functional inhibitions lead to apoptosis of GSCs. MAL-SG could be a potential marker and therapeutic target of GSCs; its inhibitors, such as MAL-II, may be useful for glioma treatment in the future.


Assuntos
Glioma/tratamento farmacológico , Lectinas/farmacologia , Maackia/química , Células-Tronco Neoplásicas/efeitos dos fármacos , Apoptose/efeitos dos fármacos , Linhagem Celular Tumoral , Proliferação de Células/efeitos dos fármacos , Regulação Neoplásica da Expressão Gênica , Humanos , Lectinas/química , Polissacarídeos/antagonistas & inibidores , Polissacarídeos/química , Sialiltransferases/química
6.
Int J Med Mushrooms ; 23(11): 45-57, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-34936308

RESUMO

Mushroom lectins have important biological and biomedical applications. Most lectins purified from these organisms exhibit high toxicity in animal cells and toward microbial agents. They are able to induce cell growth inhibition and metabolism by their ability to interact with glyconjugate components (glycoproteins receptors, glycolipids) present in their membrane. After lectins bind to these membrane receptors, they induce cellular signalization chains in which gene expression is regulated and cell death programming (apoptosis) is activated. In this work, a new multimeric lectin was characterized from the rare saprobic edible mushroom, Laetiporus sulphureus strain TMES43, grown in the Algerian forest. Lectin was isolated with ammonium sulfate precipitation followed by affinity chromatography on a Sepharose 4B column, with specific activity of 1204.7 units of hemagglutination activity/mg and 35.55% yield. The protein has a tetrameric structure with a molecular weight of 36 kDa for each subunit, with a total molecular weight of approximately 140 kDa. In addition, a Mascot peptide fingerprint study on a matrix-assisted laser desorption ionization-time of flight tandem fragment showed identity with autophagy-related protein 16 from Meyerozyma guilliermondii (strain ATCC 6260/CBS 566/DSM 6381/JCM 1539/NBRC 10279/NRRL Y-324; Expasy ID: ATG16_PICGU) and no sequence similarity to known mushroom lectins. L. sulphureus hemagglutination activity was reduced by 5 mM of lactose and 10 mM of EDTA incubation and was recovered by metallic cations such as CaCl2, MgCl2, and ZnCl2. L. sulphureus purified lectin had no human ABO group specificity and showed low temperature and alkaline pH stabilities. The MTT preliminary assay showed that L. sulphureus purified lectin induced high cytotoxicity for tumor cells and normal cells.


Assuntos
Lactose , Lectinas , Argélia , Animais , Cromatografia de Afinidade , Lectinas/farmacologia , Polyporales , Enxofre
7.
Mar Drugs ; 19(12)2021 Dec 01.
Artigo em Inglês | MEDLINE | ID: mdl-34940686

RESUMO

Lectins are proteins with a remarkably high affinity and specificity for carbohydrates. Many organisms naturally produce them, including animals, plants, fungi, protists, bacteria, archaea, and viruses. The present report focuses on lectins produced by marine or freshwater organisms, in particular algae and cyanobacteria. We explore their structure, function, classification, and antimicrobial properties. Furthermore, we look at the expression of lectins in heterologous systems and the current research on the preclinical and clinical evaluation of these fascinating molecules. The further development of these molecules might positively impact human health, particularly the prevention or treatment of diseases caused by pathogens such as human immunodeficiency virus, influenza, and severe acute respiratory coronaviruses, among others.


Assuntos
Antibacterianos/farmacologia , Cianobactérias , Lectinas/farmacologia , Microalgas , Extratos Vegetais/farmacologia , Animais , Antibacterianos/química , Organismos Aquáticos , Lectinas/química , Extratos Vegetais/química , Relação Estrutura-Atividade
8.
Anal Biochem ; 635: 114450, 2021 12 15.
Artigo em Inglês | MEDLINE | ID: mdl-34767809

RESUMO

Lectin is a carbohydrate-binding protein, which exhibits a plethora of biological properties such as antimicrobial, antifungal, and anticancer activities. In the present study, lectin, with an antibacterial and antioxidant potential, was purified from the oyster mushroom Pleurotus flabellatus. The P. flabellatus Lectin (PFL-L) was purified by using a DEAE - cellulose anion exchange chromatography followed by gel-filtration chromatography. The PFL-L was characterized by CD, HPLC, and MALDI-TOF/MS. The purity of PFL-L increased to 62.40% with the recovery of hemagglutinating activity (HA) by 12.12%. On SDS - PAGE, the PFL-L gave a single band of 18 kDa. PFL-L, consisting of d-galactose, exhibits a strong hemagglutinating activity. It was stable at pH (6.0-7.5) and temperature (10-20 °C) in addition to having extensive hemagglutinating activity. PFL-L enhanced the HA with the use of different metal ions namely Mg2+, Ca2+, and Fe2+. The study of bacterial growth inhibition led to the inference that the PFL-L was more potent against gram-negative bacteria. PFL-L showed the highest radical scavenging activity for the DPPH assay at 100 µg/mL (89.9 ± 2.53%). The highest antioxidant activities with IC50 values (for DPPH assay) of 53.96 µg/mL were determined for PFL-L and the present study shows that lectin from P. flabellatus manifested distinctive character and potentially exploitable activities.


Assuntos
Antibacterianos/farmacologia , Antioxidantes/farmacologia , Bactérias Gram-Negativas/efeitos dos fármacos , Bactérias Gram-Positivas/efeitos dos fármacos , Lectinas/farmacologia , Pleurotus/química , Animais , Antibacterianos/química , Antibacterianos/isolamento & purificação , Antioxidantes/química , Antioxidantes/isolamento & purificação , Compostos de Bifenilo/antagonistas & inibidores , Lectinas/química , Lectinas/isolamento & purificação , Testes de Sensibilidade Microbiana , Picratos/antagonistas & inibidores , Ovinos
9.
Glycoconj J ; 38(6): 669-688, 2021 12.
Artigo em Inglês | MEDLINE | ID: mdl-34748163

RESUMO

A N-glycan specific lectin from Rhizoctonia bataticola [RBL] was shown to induce growth inhibitory and apoptotic effect in human ovarian, colon and leukemic cells but mitogenic effect on normal PBMCs as reported earlier, revealing its clinical potential. RBL has unique specificity for high mannose tri and tetra antennary N-glycans, expressed in ovarian cancer and also recognizes glycans which are part of CA 125 antigen, a well known ovarian cancer marker. Hence, in the present study diagnostic and therapeutic potential of RBL was investigated using human ovarian epithelial cancer SKOV3 and OVCAR3 cells known for differentially expressing CA 125. RBL binds differentially to human ovarian normal, cyst and cancer tissues. Flow cytometry, western blot analysis of membrane proteins showed the competitive binding of RBL and CA 125 antibody for the same binding sites on SKOV3 and OVCAR3 cells. RBL has strong binding to both SKOV3 and OVCAR3 cells with MFI of 173 and 155 respectively. RBL shows dose and time dependent growth inhibitory effect with IC50 of 2.5 and 8 µg/mL respectively for SKOV3 and OVCAR3 cells. RBL induces reproductive cell death, morphological changes, nuclear degradation and increased release of ROS in SKOV3 and OVCAR3 cells leading to cell death. This is also supported by increase in hypodiploid population, altered MMP leading to apoptosis possibly involving intrinsic pathway. Adhesion, wound healing, invasion and migration assays demonstrated anti-metastasis effect of RBL apart from its growth inhibitory effect. These results show the promising potential of RBL both as a diagnostic and therapeutic agent.


Assuntos
Antígeno Ca-125 , Neoplasias Ovarianas , Apoptose , Ascomicetos , Antígeno Ca-125/farmacologia , Carcinoma Epitelial do Ovário , Linhagem Celular Tumoral , Movimento Celular , Proliferação de Células , Feminino , Humanos , Lectinas/metabolismo , Lectinas/farmacologia , Neoplasias Ovarianas/tratamento farmacológico , Neoplasias Ovarianas/metabolismo , Neoplasias Ovarianas/patologia
10.
Mar Drugs ; 19(10)2021 Sep 23.
Artigo em Inglês | MEDLINE | ID: mdl-34677432

RESUMO

Aphrocallistes vastus lectin (AVL) is a C-type marine lectin produced by sponges. Our previous study demonstrated that genes encoding AVL enhanced the cytotoxic effect of oncolytic vaccinia virus (oncoVV) in a variety of cancer cells. In this study, the inhibitory effect of oncoVV-AVL on Hela S3 cervical cancer cells, a cell line with spheroidizing ability, was explored. The results showed that oncoVV-AVL could inhibit Hela S3 cells growth both in vivo and in vitro. Further investigation revealed that AVL increased the virus replication, promote the expression of OASL protein and stimulated the activation of Raf in Hela S3 cells. This study may provide insight into a novel way for the utilization of lection AVL.


Assuntos
Adenina/análogos & derivados , Antineoplásicos/farmacologia , Lectinas/farmacologia , Vírus Oncolíticos/patogenicidade , Poríferos , Tiramina/análogos & derivados , Vírus Vaccinia/patogenicidade , Adenina/química , Adenina/farmacologia , Adenina/uso terapêutico , Animais , Antineoplásicos/química , Antineoplásicos/uso terapêutico , Organismos Aquáticos , Proliferação de Células/efeitos dos fármacos , Feminino , Células HeLa/efeitos dos fármacos , Humanos , Lectinas/química , Lectinas/uso terapêutico , Tiramina/química , Tiramina/farmacologia , Tiramina/uso terapêutico , Neoplasias do Colo do Útero/tratamento farmacológico
11.
IET Nanobiotechnol ; 15(3): 318-328, 2021 May.
Artigo em Inglês | MEDLINE | ID: mdl-34694672

RESUMO

Pseudomonas aeruginosa lectin is purified and nanoparticle-conjugated in an attempt to inhibit biofilm formation. Thirteen (23.6%) P. aeruginosa isolates are obtained from chicken meat samples, of which 30.8% are biofilm producers and 69.2% are lectin producers. Lectin is purified 36.8-fold to final specific activity of 506.9 U/mg. Four nanoparticle types are prepared via laser ablation: platinum (Pt), gold (Au), silica oxide (SiO2 ), and tin oxide (SnO2 ). The four types are characterised, and pulse feeding is used to conjugate the lectin and nanoparticles. Pt, Au, SiO2, and SnO2 nanoparticles inhibit biofilm formation, especially SiO2 nanoparticles, which have higher effectiveness when conjugated with purified lectin. SiO2 -conjugated lectin significantly (p < 0.05) inhibits biofilm formation more effectively than control and other nanoparticle-conjugated lectins. Au-, Pt nanoparticle-, and SnO2 -conjugated lectins inhibit biofilm significantly compared with control (p < 0.05), and rhlR gene expression is decreased in the presence of SiO2 -conjugated lectin. Furthermore, lectin and Pt, Au, SiO2 and SnO2 nanoparticles separately, and their conjugated lectins, are effective biofilm inhibitors. Of these, SiO2 -conjugated lectin was most significant as an anti-biofilm. Moreover, virulence factors regulon and RhlR were reduced by SiO2 -conjugated lectin, indicating that this conjugation may also decrease the virulence of P. aeruginosa.


Assuntos
Nanopartículas , Pseudomonas aeruginosa , Antibacterianos/farmacologia , Biofilmes , Lectinas/farmacologia , Óxidos , Dióxido de Silício , Virulência
12.
Mar Drugs ; 19(9)2021 Aug 24.
Artigo em Inglês | MEDLINE | ID: mdl-34564136

RESUMO

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 ß/α-protein with the predominance of ß-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, ß-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.


Assuntos
Lectinas/química , Lectinas/farmacologia , Animais , Bactérias , Bivalves , Meio Ambiente , Eritrócitos/efeitos dos fármacos , Eritrócitos/metabolismo , Hemaglutininas/metabolismo , Hemolinfa/química , Estresse Fisiológico
13.
Exp Oncol ; 43(3): 197-203, 2021 09.
Artigo em Inglês | MEDLINE | ID: mdl-34591426

RESUMO

BACKGROUND: Recent studies have shown the potential of using different approaches for immunotherapy in cancer treatment. Macrophages (Mph) are one of the promising targets for immunotherapy. AIM: To investigate changes in the functional activity of Mph in mice with Ehrlich carcinoma by nitric oxide (NO)/arginase (Arg), IRF4/IRF5 and STAT1/STAT6 ratios caused by administration of lectin from B. subtilis IMV-7724. MATERIALS AND METHODS: From the 2nd day after Ehrlich carcinoma inoculation into female Balb/c mice, lectin from B. subtilis IMV B-7724 (0.02 mg/mouse) was administered for 10 days. The peritoneal Mph were isolated on days 14, 21, and 28 after tumor transplantation and their functional state (NO production, Arg activity and cytotoxic activity) was examined. The levels of mRNA expression of transcription factors STAT-1, STAT-6, IRF5, IRF4 were evaluated. RESULTS: In lectin-treated animals with Ehrlich carcinoma, the functional state of Mph (NO/Arg ratio, index of cytotoxic activity) was maintained at the level of intact mice exceeding the values in untreated animals with Ehrlich carcinoma at late terms of tumor growth (21, 28 days). Analysis of mRNA expression levels of transcription factors in these animals showed a significant increase (p < 0.05) in the ratio of STAT1/STAT6 on the day 21 and IRF5/IRF4 on day 28 of tumor growth compared to that in untreated mice. CONCLUSIONS: Administration of lectin from B. subtilis IMV B-7724 to mice with Ehrlich carcinoma led to the prevalence of Mph exhibiting the functional properties of M1 type at late-term tumor growth. The transcription factors of the STAT and IRF signaling pathways are involved in the process of Mph polarization induced by lectin from B. subtilis IMV B-7724.


Assuntos
Arginase/metabolismo , Bacillus subtilis/metabolismo , Carcinoma de Ehrlich/tratamento farmacológico , Regulação da Expressão Gênica/efeitos dos fármacos , Lectinas/farmacologia , Ativação de Macrófagos/imunologia , Óxido Nítrico/metabolismo , Animais , Carcinoma de Ehrlich/imunologia , Carcinoma de Ehrlich/metabolismo , Carcinoma de Ehrlich/patologia , Fatores Reguladores de Interferon/genética , Fatores Reguladores de Interferon/metabolismo , Masculino , Camundongos , Camundongos Endogâmicos BALB C , Fator de Transcrição STAT1/genética , Fator de Transcrição STAT1/metabolismo , Fator de Transcrição STAT6/genética , Fator de Transcrição STAT6/metabolismo
14.
Int J Biol Macromol ; 191: 746-752, 2021 Nov 30.
Artigo em Inglês | MEDLINE | ID: mdl-34592219

RESUMO

The carbohydrate recognition domain (CRD) is the key component of C-type lectins (CTLs) with the capacity to recognize and eliminate invading pathogens. Herein, the recombinant proteins of four CRDs identified from the kuruma shrimp, Marsupenaeus japonicus, were produced and purified by an Escherichia coli expression system and affinity chromatography. Bacterial binding and antibacterial assays showed that the four CRDs displayed various bacterial binding and antibacterial activities against different bacteria. Among the four recombinant CRDs, His-CRD2-3 exhibited the broadest spectrum of bacterial binding and antibacterial activities against gram-negative bacteria (Vibrio parahaemolyticus, V. alginolyticus and V. harveyi) and gram-positive bacteria (Staphylococcus aureus and Micrococcus lysodeikticus). Moreover, the four recombinant CRDs showed different capacities to regulate the expression of several immune effector genes (MjCTL3, MjCTL4, MjCTL, Mjily and Mjsty), among which His-CRD2-3 displayed broader and stronger inductive effects on these immune effector genes. This study indicated that the four CRDs participated in immune defense by binding and killing bacteria and regulating the transcription of other immune effector genes. In addition, our results suggested that His-CRD2-3 might be a promising agent for the prevention and treatment of bacteriosis.


Assuntos
Antibacterianos/química , Lectinas/química , Penaeidae/química , Animais , Antibacterianos/farmacologia , Clonagem Molecular , Lectinas/genética , Lectinas/farmacologia , Micrococcus/efeitos dos fármacos , Penaeidae/metabolismo , Domínios Proteicos , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/farmacologia , Staphylococcus aureus/efeitos dos fármacos , Vibrio/efeitos dos fármacos
15.
Mar Drugs ; 19(7)2021 Jul 14.
Artigo em Inglês | MEDLINE | ID: mdl-34356819

RESUMO

In recent years, there has been considerable interest in lectins from marine invertebrates. In this study, the biological activities of a lectin protein isolated from the eggs of Sea hare (Aplysia kurodai) were evaluated. The 40 kDa Aplysia kurodai egg lectin (or AKL-40) binds to D-galacturonic acid and D-galactose sugars similar to previously purified isotypes with various molecular weights (32/30 and 16 kDa). The N-terminal sequence of AKL-40 was similar to other sea hare egg lectins. The lectin was shown to be moderately toxic to brine shrimp nauplii, with an LC50 value of 63.63 µg/mL. It agglutinated Ehrlich ascites carcinoma cells and reduced their growth, up to 58.3% in vivo when injected into Swiss albino mice at a rate of 2 mg/kg/day. The morphology of these cells apparently changed due to AKL-40, while the expression of apoptosis-related genes (p53, Bax, and Bcl-XL) suggested a possible apoptotic pathway of cell death. AKL-40 also inhibited the growth of human erythroleukemia cells, probably via activating the MAPK/ERK pathway, but did not affect human B-lymphoma cells (Raji) or rat basophilic leukemia cells (RBL-1). In vitro, lectin suppressed the growth of Ehrlich ascites carcinoma and U937 cells by 37.9% and 31.8%, respectively. Along with strong antifungal activity against Talaromyces verruculosus, AKL showed antibacterial activity against Staphylococcus aureus, Shigella sonnei, and Bacillus cereus whereas the growth of Escherichia coli was not affected by the lectin. This study explores the antiproliferative and antimicrobial potentials of AKL as well as its involvement in embryo defense of sea hare.


Assuntos
Antibacterianos/farmacologia , Aplysia , Lectinas/farmacologia , Animais , Organismos Aquáticos , Ovos , Escherichia coli/efeitos dos fármacos , Staphylococcus aureus/efeitos dos fármacos
16.
Cells ; 10(7)2021 06 28.
Artigo em Inglês | MEDLINE | ID: mdl-34203435

RESUMO

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 surface of the spikes. A detailed analysis of the carbohydrate-binding specificity of mannose-binding lectins from plants, algae, fungi, and bacteria, revealed that, depending on their origin, they preferentially recognize either complex type N-glycans, or high-mannose type N-glycans. Since both complex and high-mannose glycans substantially decorate the S proteins, mannose-specific lectins are potentially useful glycan probes for targeting the SARS-CoV, MERS-CoV, and SARS-CoV-2 virions. Mannose-binding legume lectins, like pea lectin, and monocot mannose-binding lectins, like snowdrop lectin or the algal lectin griffithsin, which specifically recognize complex N-glycans and high-mannose glycans, respectively, are particularly adapted for targeting coronaviruses. The biomedical prospects of targeting coronaviruses with mannose-specific lectins are wide-ranging including detection, immobilization, prevention, and control of coronavirus infection.


Assuntos
Lectinas/farmacologia , Coronavírus da Síndrome Respiratória do Oriente Médio/metabolismo , Vírus da SARS/metabolismo , SARS-CoV-2/metabolismo , Glicoproteína da Espícula de Coronavírus/metabolismo , COVID-19/tratamento farmacológico , COVID-19/virologia , Cianobactérias/química , Sistemas de Liberação de Medicamentos/métodos , Fungos/química , Humanos , Lectinas/isolamento & purificação , Lectinas/uso terapêutico , Coronavírus da Síndrome Respiratória do Oriente Médio/fisiologia , Plantas/química , Ligação Proteica , Vírus da SARS/fisiologia , SARS-CoV-2/fisiologia , Especificidade da Espécie , Internalização do Vírus/efeitos dos fármacos
17.
Mar Drugs ; 19(6)2021 May 21.
Artigo em Inglês | MEDLINE | ID: mdl-34064193

RESUMO

Oncolytic vaccina virus (oncoVV) used for cancer therapy has progressed in recent years. Here, a gene encoding white-spotted charr lectin (WCL) was inserted into an oncoVV vector to form an oncoVV-WCL recombinant virus. OncoVV-WCL induced higher levels of apoptosis and cytotoxicity, and replicated faster than control virus in cancer cells. OncoVV-WCL promoted IRF-3 transcriptional activity to induce higher levels of type I interferons (IFNs) and blocked the IFN-induced antiviral response by inhibiting the activity of IFN-stimulated responsive element (ISRE) and the expression of interferon-stimulated genes (ISGs). The higher levels of viral replication and antitumor activity of oncoVV-WCL were further demonstrated in a mouse xenograft tumor model. Therefore, the engineered oncoVV expressing WCL might provide a new avenue for anticancer gene therapy.


Assuntos
Antineoplásicos/farmacologia , Lectinas/genética , Lectinas/farmacologia , Vírus Oncolíticos/genética , Truta/genética , Vírus Vaccinia/genética , Animais , Antineoplásicos/uso terapêutico , Antivirais/farmacologia , Apoptose/genética , Linhagem Celular Tumoral , Sobrevivência Celular/genética , Feminino , Humanos , Fator Regulador 3 de Interferon/genética , Interferon Tipo I/genética , Interferon Tipo I/metabolismo , Neoplasias Hepáticas/tratamento farmacológico , Neoplasias Pulmonares/tratamento farmacológico , Camundongos Endogâmicos BALB C , Camundongos Nus , Terapia Viral Oncolítica , Vírus Oncolíticos/crescimento & desenvolvimento , Neoplasias do Colo do Útero/tratamento farmacológico , Vírus Vaccinia/crescimento & desenvolvimento , Replicação Viral/genética , Ensaios Antitumorais Modelo de Xenoenxerto
18.
Protein Pept Lett ; 28(10): 1108-1114, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-34137358

RESUMO

BACKGROUND: Altered expression of N-glycans such as polylactosamine is observed in colon cancer. AHL, a polylactosamine specific lectin from Adenia hondala from a medicinal plant from the Passifloraceae family has been reported earlier. OBJECTIVE: The aim of the present study is to study the interaction of AHL with human colon cancer epithelial HT-29 cells and colon cancer tissues. METHODS: Cell viability was determined by MTT [3-[4, 5- dimethylthiazol-2-yl]-2, 5-diphenyltetrazolium bromide] assay, while cell surface binding, apoptosis by Annexin-V-PI assay and ROS production using DCFDA [2',7' - dichlorofluorescindiacetate] kit method were analysed by flowcytometry, immunohistochemistry was performed using biotinylated AHL, protein purification by affinity chromatography using asialofetuin-coupled Sepharose -4B column. RESULTS: AHL strongly binds to HT-29 cells with a Mean Fluorescence Intensity of 12.4, which could be blocked by competing glycoprotein asialofetuin. AHL inhibits HT-29 cell growth in a dose and time-dependent manner with IC50 of 2.5 µg/mL and differentially binds to human normal and cancerous tissues. AHL induces apoptosis and slight necrosis in HT-29 cells with an increase in the early apoptotic population of 25.1 and 36% for 24 h and 48 h respectively and necrotic population of 1.5 and 4.6% at 24 h and 48 h respectively as revealed by Annexin-V-PI assay. AHL induces the release of Reactive Oxygen Species in HT-29 cells in a dose-dependent manner. CONCLUSION: To the best of knowledge, this is the first report on lectin from Adenia hondala which is not a RIP with apoptotic and necrotic effects. These findings support the promising potential of AHL in cancer research.


Assuntos
Amino Açúcares/química , Neoplasias do Colo/tratamento farmacológico , Lectinas/química , Necrose/tratamento farmacológico , Passifloraceae/química , Extratos Vegetais/química , Polissacarídeos/química , Apoptose/efeitos dos fármacos , Proliferação de Células/efeitos dos fármacos , Sobrevivência Celular/efeitos dos fármacos , Células HT29 , Humanos , Lectinas/farmacologia , Extratos Vegetais/farmacologia , Espécies Reativas de Oxigênio
19.
Int J Biol Macromol ; 184: 636-647, 2021 Aug 01.
Artigo em Inglês | MEDLINE | ID: mdl-34174302

RESUMO

The second most predominant cancer in the world and the first among women is breast cancer. We aimed to study the protein abundance profiles induced by lectin purified from the Agaricus bisporus mushroom (ABL) and conjugated with CaCO3NPs in the MCF-7 breast cancer cell line. Two-dimensional electrophoresis (2-DE) and orbitrap mass spectrometry techniques were used to reveal the protein abundance pattern induced by lectin. Flow cytometric analysis showed the accumulation of ABL-CaCO3NPs treated cells in the G1 phase than the positive control. Thirteen proteins were found different in their abundance in breast cancer cells after 24 h exposure to lectin conjugated with CaCO3NPs. Most of the identified proteins were showing a low abundance in ABL-CaCO3NPs treated cells in comparison to the positive and negative controls, including V-set and immunoglobulin domain, serum albumin, actin cytoplasmic 1, triosephosphate isomerase, tropomyosin alpha-4 chain, and endoplasmic reticulum chaperone BiP. Hornerin, tropomyosin alpha-1 chain, annexin A2, and protein disulfide-isomerase were up-regulated in comparison to the positive. Bioinformatic analyses revealed the regulation changes of these proteins mainly affected the pathways of 'Bcl-2-associated athanogene 2 signalling pathway', 'Unfolded protein response', 'Caveolar-mediated endocytosis signalling', 'Clathrin-mediated endocytosis signalling', 'Calcium signalling' and 'Sucrose degradation V', which are associated with breast cancer. We concluded that lectin altered the abundance in molecular chaperones/heat shock proteins, cytoskeletal, and metabolic proteins. Additionally, lectin induced a low abundance of MCF-7 cancer cell proteins in comparison to the positive and negative controls, including; V-set and immunoglobulin domain, serum albumin, actin cytoplasmic 1, triosephosphate isomerase, tropomyosin alpha-4 chain, and endoplasmic reticulum chaperone BiP.


Assuntos
Agaricus/química , Neoplasias da Mama/metabolismo , Carbonato de Cálcio/química , Redes Reguladoras de Genes/efeitos dos fármacos , Lectinas/farmacologia , Proteômica/métodos , Neoplasias da Mama/tratamento farmacológico , Ciclo Celular/efeitos dos fármacos , Proliferação de Células/efeitos dos fármacos , Sobrevivência Celular/efeitos dos fármacos , Feminino , Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos , Humanos , Lectinas/química , Células MCF-7 , Nanopartículas
20.
Basic Clin Pharmacol Toxicol ; 129(2): 130-138, 2021 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-33993648

RESUMO

Lectins are proteins that recognize specific carbohydrates, and the vasorelaxant effect of legume lectins has been previously reported, for example the Dioclea rostrata lectin (DRL). This study evaluated major pathways of DRL-induced relaxation in different artery segments and the possible molecular interactions involved. Rat thoracic aorta, coronary and mesenteric resistance arteries were tested "in vitro" with concentration-response curves to DRL (0.01-100 µg/mL). L-NAME, indomethacin and high KCl were used to evaluate nitric oxide, cyclooxygenase and hyperpolarization-dependent effects. DRL promoted relaxation of all vessels throughout different mechanisms. L-NAME blunted DRL-induced effects only in the aorta and mesenteric resistance artery. By the use of depolarizing KCl solution, vasodilation was reduced in all arteries, while incubation with indomethacin indicated a role of cyclooxygenase-derived factors for DRL effects in mesenteric and coronary arteries, but not in the aorta. Molecular docking results suggested interactions between DRL and heparan sulphate, CD31 and other glycans present on the membrane surface. These data indicate that the mechanisms involved in DRL-mediated vasodilation vary between conductance and resistance arteries of different origins, and these effects may be related to the capacity of DRL to bind a diversity of glycans, especially heparan sulphate, a proposed mechanoreceptor for nitric oxide synthase and cyclooxygenase activation.


Assuntos
Artérias/efeitos dos fármacos , Dioclea , Lectinas/metabolismo , Lectinas/farmacologia , Vasodilatação/efeitos dos fármacos , Vasodilatadores/farmacologia , Animais , Aorta Torácica/efeitos dos fármacos , Aorta Torácica/fisiologia , Artérias/fisiologia , Vasos Coronários/efeitos dos fármacos , Vasos Coronários/fisiologia , Masculino , Artérias Mesentéricas/efeitos dos fármacos , Artérias Mesentéricas/fisiologia , Simulação de Acoplamento Molecular , NG-Nitroarginina Metil Éster/farmacologia , Óxido Nítrico/metabolismo , Prostaglandina-Endoperóxido Sintases/metabolismo , Ratos , Ratos Wistar
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