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[PMID]:29232689
[Au] Autor:Wester MJ; Lin J; Neumann AK
[Ad] Endereço:Department of Mathematics and Statistics and Center for Spatiotemporal Modeling of Cell Signaling, University of New Mexico, Albuquerque, New Mexico, United States of America.
[Ti] Título:A computational model for regulation of nanoscale glucan exposure in Candida albicans.
[So] Source:PLoS One;12(12):e0188599, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Candida albicans is a virulent human opportunistic pathogen. It evades innate immune surveillance by masking an immunogenic cell wall polysaccharide, ß-glucan, from recognition by the immunoreceptor Dectin-1. Glucan unmasking by the antifungal drug caspofungin leads to changes in the nanostructure of glucan exposure accessible to Dectin-1. The physical mechanism that regulates glucan exposure is poorly understood, but it controls the nanobiology of fungal pathogen recognition. We created computational models to simulate hypothetical physical processes of unmasking glucan in a biologically realistic distribution of cell wall glucan fibrils. We tested the predicted glucan exposure nanostructural features arising from these models against experimentally measured values. A completely spatially random unmasking process, reflective of random environmental damage to the cell wall, cannot account for experimental observations of glucan unmasking. However, the introduction of partially edge biased unmasking processes, consistent with an unmasking contribution from active, local remodeling at glucan exposure sites, produces markedly more accurate predictions of experimentally observed glucan nanoexposures in untreated and caspofungin-treated yeast. These findings suggest a model of glucan unmasking wherein cell wall remodeling processes in the local nanoscale neighborhood of glucan exposure sites are an important contributor to the physical process of drug-induced glucan unmasking in C. albicans.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Candida albicans/efeitos dos fármacos
Simulação por Computador
beta-Glucanas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (beta-Glucans)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188599


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[PMID]:29329339
[Au] Autor:Granger BL
[Ad] Endereço:Department of Microbiology and Immunology, Montana State University, Bozeman, Montana, United States of America.
[Ti] Título:Accessibility and contribution to glucan masking of natural and genetically tagged versions of yeast wall protein 1 of Candida albicans.
[So] Source:PLoS One;13(1):e0191194, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Yeast wall protein 1 (Ywp1) is an abundant glycoprotein of the cell wall of the yeast form of Candida albicans, the most prevalent fungal pathogen of humans. Antibodies that bind to the polypeptide backbone of isolated Ywp1 show little binding to intact yeast cells, presumably because the Ywp1 epitopes are masked by the polysaccharides of the mannoproteins that form the outer layer of the cell wall. Rare cells do exhibit much greater anti-Ywp1 binding, however, and one of these was isolated and characterized. No differences were seen in its Ywp1, but it exhibited greater adhesiveness, sensitivity to wall perturbing agents, and exposure of its underlying ß-1,3-glucan layer to external antibodies. The molecular basis for this greater epitope accessibility has not been determined, but has facilitated exploration of how these properties change as a function of cell growth and morphology. In addition, previously engineered strains with reduced quantities of Ywp1 in their cell walls were also found to have greater ß-1,3-glucan exposure, indicating that Ywp1 itself contributes to the masking of wall epitopes, which may be important for understanding the anti-adhesive effect of Ywp1. Ectopic production of Ywp1 by hyphae, which reduces the adhesivity of these filamentous forms of C. albicans, was similarly found to reduce exposure of the ß-1,3-glucan in their walls. To monitor Ywp1 in the cell wall irrespective of its accessibility, green fluorescent protein (Gfp) was genetically inserted into wall-anchored Ywp1 using a bifunctional cassette that also allowed production from a single transfection of a soluble, anchor-free version. The wall-anchored Ywp1-Gfp-Ywp1 accumulated in the wall of the yeast forms but not hyphae, and appeared to have properties similar to native Ywp1, including its adhesion-inhibiting effect. Some pseudohyphal walls also detectably accumulated this probe. Strains of C. albicans with tandem hemagglutinin (HA) epitopes inserted into wall-anchored Ywp1 were previously created by others, and were further explored here. As above, rare cells with much greater accessibility of the HA epitopes were isolated, and also found to exhibit greater exposure of Ywp1 and ß-1,3-glucan. The placement of the HA cassette inhibited the normal N-glycosylation and propeptide cleavage of Ywp1, but the wall-anchored Ywp1-HA-Ywp1 still accumulated in the cell wall of yeast forms. Bifunctional transformation cassettes were used to additionally tag these molecules with Gfp, generating soluble Ywp1-HA-Gfp and wall-anchored Ywp1-HA-Gfp-Ywp1 molecules. The former revealed unexpected electrophoretic properties caused by the HA insertion, while the latter further highlighted differences between the presence of a tagged Ywp1 molecule (as revealed by Gfp fluorescence) and its accessibility in the cell wall to externally applied antibodies specific for HA, Gfp and Ywp1, with accessibility being greatest in the rapidly expanding walls of budding daughter cells. These strains and results increase our understanding of cell wall properties and how C. albicans masks itself from recognition by the human immune system.
[Mh] Termos MeSH primário: Candida albicans/genética
Candida albicans/metabolismo
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
beta-Glucanas/metabolismo
[Mh] Termos MeSH secundário: Anticorpos Antifúngicos
Antígenos de Fungos/química
Antígenos de Fungos/genética
Antígenos de Fungos/metabolismo
Candida albicans/imunologia
Parede Celular/genética
Parede Celular/imunologia
Parede Celular/metabolismo
Epitopos/química
Epitopos/genética
Epitopos/metabolismo
Proteínas Fúngicas/imunologia
Glicosilação
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/imunologia
Proteínas de Fluorescência Verde/metabolismo
Hemaglutininas/genética
Hemaglutininas/imunologia
Hemaglutininas/metabolismo
Seres Humanos
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/imunologia
Glicoproteínas de Membrana/metabolismo
Engenharia de Proteínas
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/imunologia
Proteínas Recombinantes de Fusão/metabolismo
beta-Glucanas/química
beta-Glucanas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Fungal); 0 (Antigens, Fungal); 0 (Epitopes); 0 (Fungal Proteins); 0 (Hemagglutinins); 0 (Membrane Glycoproteins); 0 (Recombinant Fusion Proteins); 0 (beta-Glucans); 0 (mannoproteins); 147336-22-9 (Green Fluorescent Proteins); 9051-97-2 (beta-1,3-glucan)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191194


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[PMID]:28467361
[Au] Autor:Francioso A; Cossi R; Fanelli S; Mastromarino P; Mosca L
[Ad] Endereço:Department of Biochemical Sciences, "Sapienza" University of Rome, Piazzale Aldo Moro, 5, 00185 Roma, Italy. antonio.francioso@uniroma1.it.
[Ti] Título:Studies on Trans-Resveratrol/Carboxymethylated (1,3/1,6)-ß-d-Glucan Association for Aerosol Pharmaceutical Applications.
[So] Source:Int J Mol Sci;18(5), 2017 May 03.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:A resveratrol/carboxymethylated glucan (CM-glucan) combination is known to inhibit rhinovirus replication and expression of inflammatory mediators in nasal epithelia. The aim of this study was to develop an aerosol formulation containing an association of the two molecules which could reach the lower respiratory tract. Mass median aerodynamic diameter (MMAD) of a resveratrol/CM-glucan combination was lower than that shown by resveratrol or CM-glucan alone (2.83 versus 3.28 and 2.96 µm, respectively). The resveratrol/CM-glucan association results in the finest and most monodispersed particles in comparison to the two single components. The association also evidenced lower values for all particle size distribution parameters, suggesting that the pharmacological synergy observed in previous studies may be accompanied by a pharmaceutical one. Moreover, we showed that the CM-glucan matrix did not exert an inhibitory effect on resveratrol nebulization, demonstrating the good suitability of these two molecules in association for simultaneous aerosol volatilization.
[Mh] Termos MeSH primário: Anti-Inflamatórios não Esteroides/química
Anti-Inflamatórios não Esteroides/farmacologia
Antivirais/química
Antivirais/farmacologia
Estilbenos/química
Estilbenos/farmacologia
beta-Glucanas/química
[Mh] Termos MeSH secundário: Aerossóis
Sobrevivência Celular/efeitos dos fármacos
Células HeLa
Seres Humanos
Mucosa Nasal
Nebulizadores e Vaporizadores
Tamanho da Partícula
Rhinovirus/efeitos dos fármacos
Volatilização
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aerosols); 0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (Antiviral Agents); 0 (Stilbenes); 0 (beta-Glucans); 9051-97-2 (beta-1,3-glucan); Q369O8926L (resveratrol)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


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[PMID]:29293326
[Au] Autor:Ide M; Okumura M; Koizumi K; Kumagai M; Yoshida I; Yoshida M; Mishima T; Nakamura M
[Ad] Endereço:Japan Food Research Laboratories , Osaka 567-0085, Japan.
[Ti] Título:Novel Method to Quantify ß-Glucan in Processed Foods: Sodium Hypochlorite Extracting and Enzymatic Digesting (SEED) Assay.
[So] Source:J Agric Food Chem;66(4):1033-1038, 2018 Jan 31.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Some ß-glucans have attracted attention due to their functionality as an immunostimulant and have been used in processed foods. However, accurately measuring the ß-glucan content of processed foods using existing methods is difficult. We demonstrate a new method, the Sodium hypochlorite Extracting and Enzymatic Digesting (SEED) assay, in which ß-glucan is extracted using sodium hypochlorite, dimethyl sulfoxide, and 5 mol/L sodium hydroxide and then digested into ß-glucan fragments using Westase which is an enzyme having ß-1,6- and ß-1,3 glucanase activity. The ß-glucan fragments are further digested into glucose using exo-1,3-ß-d-glucanase and ß-glucosidase. We measured ß-glucan comprising ß-1,3-, -1,6-, and -1,(3),4- bonds in various polysaccharide reagents and processed foods using our novel method. The SEED assay was able to quantify ß-glucan with good reproducibility, and the recovery rate was >90% for food containing ß-glucan. Therefore, the SEED assay is capable of accurately measuring the ß-glucan content of processed foods.
[Mh] Termos MeSH primário: Análise de Alimentos/métodos
Hipoclorito de Sódio
beta-Glucanas/análise
[Mh] Termos MeSH secundário: Manipulação de Alimentos
Glucana 1,3-beta-Glucosidase/metabolismo
Glucanos/química
Hordeum/química
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucans); 0 (beta-Glucans); 9008-22-4 (laminaran); DY38VHM5OD (Sodium Hypochlorite); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase); EC 3.2.1.58 (beta-1,3-exoglucanase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05044


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[PMID]:29285925
[Au] Autor:Cao Y; Sun Y; Zou S; Duan B; Sun M; Xu X
[Ad] Endereço:College of Chemistry and Molecular Sciences, Wuhan University , Wuhan 430072, China.
[Ti] Título:Yeast ß-Glucan Suppresses the Chronic Inflammation and Improves the Microenvironment in Adipose Tissues of ob/ob Mice.
[So] Source:J Agric Food Chem;66(3):621-629, 2018 Jan 24.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inflammation in visceral adipose tissues (VATs) contributes to the pathology of diabetes. This study focused on the inflammatory regulation in VATs by a yeast ß-1,3-glucan (BYG) orally administered to ob/ob mice. BYG decreased pro-inflammatory modulators of TNF-α, IL-6, IL-1ß, CCL2, and SAA3, and increased anti-inflammatory factors of Azgp1 (2.53 ± 0.02-fold change) at protein and/or mRNA levels (p < 0.05). Remarkably, BYG decreased the degree of adipose tissue macrophages (ATMs) infiltration to 82.5 ± 8.3%, especially the newly recruited ATMs. Interestingly, BYG increased the protective Th2 cell regulator GATA3 (7.72 ± 0.04-fold change) and decreased immunosuppressors IL-10 and IL-1ra, suggesting that BYG elicited inflammation inhibition via stimulating immune responses. Additionally, BYG increased the gut microbiota proportion of Akkermansia from 0.07% to 4.85% and improved the microenvironment of VATs through decreasing fibrosis and angiogenesis. These findings suggest that BYG has anti-inflammatory effect in diabetic mice, which can be used as a food component and/or therapeutic agent for diabetes.
[Mh] Termos MeSH primário: Tecido Adiposo/efeitos dos fármacos
Diabetes Mellitus Tipo 2/tratamento farmacológico
Diabetes Mellitus Tipo 2/imunologia
Saccharomyces cerevisiae/química
beta-Glucanas/administração & dosagem
[Mh] Termos MeSH secundário: Tecido Adiposo/imunologia
Animais
Bactérias/classificação
Bactérias/genética
Bactérias/isolamento & purificação
Diabetes Mellitus Tipo 2/genética
Diabetes Mellitus Tipo 2/microbiologia
Microbioma Gastrointestinal/efeitos dos fármacos
Seres Humanos
Interleucina-10/genética
Interleucina-10/imunologia
Interleucina-6/genética
Interleucina-6/imunologia
Intestinos/imunologia
Intestinos/microbiologia
Macrófagos/efeitos dos fármacos
Macrófagos/imunologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Obesos
Saccharomyces cerevisiae/metabolismo
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/imunologia
beta-Glucanas/química
beta-Glucanas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interleukin-6); 0 (Tumor Necrosis Factor-alpha); 0 (beta-Glucans); 130068-27-8 (Interleukin-10)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171230
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04921


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[PMID]:28461332
[Au] Autor:Temple MJ; Cuskin F; Baslé A; Hickey N; Speciale G; Williams SJ; Gilbert HJ; Lowe EC
[Ad] Endereço:From the Institute of Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE4 2HH, United Kingdom and.
[Ti] Título:A Bacteroidetes locus dedicated to fungal 1,6-ß-glucan degradation: Unique substrate conformation drives specificity of the key endo-1,6-ß-glucanase.
[So] Source:J Biol Chem;292(25):10639-10650, 2017 06 23.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycans are major nutrients available to the human gut microbiota. The are generalist glycan degraders, and this function is mediated largely by polysaccharide utilization loci (PULs). The genomes of several species contain a PUL, PUL , that was predicted to target mixed linked plant 1,3;1,4-ß-glucans. To test this hypothesis we characterized the proteins encoded by this locus in , a member of the human gut microbiota. We show here that PUL does not orchestrate the degradation of a plant polysaccharide but targets a fungal cell wall glycan, 1,6-ß-glucan, which is a growth substrate for the bacterium. The locus is up-regulated by 1,6-ß-glucan and encodes two enzymes, a surface endo-1,6-ß-glucanase, BT3312, and a periplasmic ß-glucosidase that targets primarily 1,6-ß-glucans. The non-catalytic proteins encoded by PUL target 1,6-ß-glucans and comprise a surface glycan-binding protein and a SusD homologue that delivers glycans to the outer membrane transporter. We identified the central role of the endo-1,6-ß-glucanase in 1,6-ß-glucan depolymerization by deleting , which prevented the growth of on 1,6-ß-glucan. The crystal structure of BT3312 in complex with ß-glucosyl-1,6-deoxynojirimycin revealed a TIM barrel catalytic domain that contains a deep substrate-binding cleft tailored to accommodate the hook-like structure adopted by 1,6-ß-glucan. Specificity is driven by the complementarity of the enzyme active site cleft and the conformation of the substrate. We also noted that PUL is syntenic to many PULs from other Bacteroidetes, suggesting that utilization of yeast and fungal cell wall 1,6-ß-glucans is a widespread adaptation within the human microbiota.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Bacteroidetes/enzimologia
Polissacarídeos Fúngicos/química
Glicosídeo Hidrolases/química
beta-Glucanas/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Bacteroidetes/genética
Configuração de Carboidratos
Cristalografia por Raios X
Loci Gênicos
Glicosídeo Hidrolases/genética
Seres Humanos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fungal Polysaccharides); 0 (beta-Glucans); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.75 (endo-1,6-beta-glucanase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.787606


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[PMID]:29190812
[Au] Autor:Son HJ; Sung H; Park SY; Kim T; Lee HJ; Kim SM; Chong YP; Lee SO; Choi SH; Kim YS; Woo JH; Kim SH
[Ad] Endereço:Departments of Infectious Diseases, Asan Medical Center, University of Ulsan College of Medicine, Seoul, Republic of Korea.
[Ti] Título:Diagnostic performance of the (1-3)-ß-D-glucan assay in patients with Pneumocystis jirovecii compared with those with candidiasis, aspergillosis, mucormycosis, and tuberculosis, and healthy volunteers.
[So] Source:PLoS One;12(11):e0188860, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Diagnosis of pneumocystis pneumonia (PCP) relies on microscopic visualization of P. jirovecii, or detection of Pneumocystis DNA in respiratory specimens, which involves invasive procedures such as bronchoalveolar lavage. The (1-3)-ß-D-glucan (BG) assay has been proposed as a less invasive and less expensive diagnostic test to rule out PCP. We therefore compared blood levels of BG in patients with PCP with those of patients with candidemia, chronic disseminated candidiasis (CDC), invasive aspergillosis, mucormycosis, and tuberculosis and those of healthy volunteers. METHODS: Adult patients who were diagnosed with PCP, candidemia, CDC, invasive aspergillosis, mucormycosis, and tuberculosis whose blood samples were available, and healthy volunteers were enrolled in a tertiary hospital in Seoul, South Korea, during a 21-month period. The blood samples were assayed with the Goldstream Fungus (1-3)-ß-D-glucan test (Gold Mountain River Tech Development, Beijing, China). RESULTS: A total of 136 individuals including 50 patients P. jirovecii,15 candidemia, 6 CDC, 15 invasive aspergillosis, 10 mucormycosis, and 40 controls (20 TB and 20 healthy volunteers) were included. The mean±SD of the concentration of 1-3-ß-D-glucan in the patients with PCP (290.08 pg/mL±199.98) were similar to those of patients with candidemia (314.14 pg/mL±205.60, p = 0.90 at an α = 0.005) and CDC (129.74 pg/mL±182.79, p = 0.03 at an α = 0.005), but higher than those of patients with invasive aspergillosis (131.62 pg/mL±161.67, p = 0.002 at an α = 0.005), mucormycosis (95.08 pg/mL±146.80, p<0.001 at an α = 0.005), and tuberculosis (103.31 pg/mL±140.81, p<0.001 at an α = 0.005) as well as healthy volunteers (101.18 pg/mL±197.52, p<0.001 at an α = 0.005). At a cut-off value > 31.25 pg/mL, which is highly sensitive for PCP versus tuberculosis plus healthy volunteers at the expense of specificity, the BG assay had a sensitivity of 92% (95% CI 81%-98%) and a specificity of 55% (95% CI 39%-71%). CONCLUSIONS: The BG assay appears to be a useful adjunct test for PCP.
[Mh] Termos MeSH primário: Aspergilose/diagnóstico
Candidíase/diagnóstico
Mucormicose/diagnóstico
Pneumocystis carinii/isolamento & purificação
Pneumonia por Pneumocystis/diagnóstico
Tuberculose Pulmonar/diagnóstico
beta-Glucanas/análise
[Mh] Termos MeSH secundário: Adulto
Idoso
Estudos de Casos e Controles
Diagnóstico Diferencial
Feminino
Voluntários Saudáveis
Seres Humanos
Masculino
Meia-Idade
Pneumonia por Pneumocystis/microbiologia
República da Coreia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (beta-Glucans); 9051-97-2 (beta-1,3-glucan)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188860


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[PMID]:28946308
[Au] Autor:Yan J; Han Z; Qu Y; Yao C; Shen D; Tai G; Cheng H; Zhou Y
[Ad] Endereço:Jilin Province Key Laboratory on Chemistry and Biology of Changbai Mountain Natural Drugs, School of Life Sciences, Northeast Normal University, Changchun 130024, PR China.
[Ti] Título:Structure elucidation and immunomodulatory activity of a ß-glucan derived from the fruiting bodies of Amillariella mellea.
[So] Source:Food Chem;240:534-543, 2018 Feb 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A novel polysaccharide AAMP-A70 (5.6kDa) has been purified from the fruiting bodies of Amillariella mellea. Compositional analysis and 1H and 13C NMR spectra indicate that AAMP-A70 is a branched ß-glucan with a main chain that consists of ß-d-(1→6) linked Glcρ residues substituted at O-3 by ß-Glcρ or α-d-(1→6)-linked Galρ side chains. AAMP-A70 increases macrophage phagocytosis and secretion of NO, ROS, TNF-α, IL-6 and IL-1ß. Mechanistically, AAMP-A70 promotes degradation of IκB-α and nuclear translocation of the NF-κB p65 subunit, and enhances phosphorylation of MAPKs. In particular, the function blocking antibody to TLR2 substantially suppresses TNF-α and IL-6 production. Our data demonstrate that AAMP-A70 activates macrophages via NF-κB/MAPK signaling pathways and the TLR2 receptor. Overall, AAMP-A70 may serve as a good food supplement to enhance immunity.
[Mh] Termos MeSH primário: Agaricales
[Mh] Termos MeSH secundário: Carpóforos
Glucanos
NF-kappa B
Transdução de Sinais
beta-Glucanas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucans); 0 (NF-kappa B); 0 (beta-Glucans)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE


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[PMID]:28873599
[Au] Autor:Zhang B; Wang J; Ning S; Yuan Q; Chen X; Zhang Y; Fan J
[Ad] Endereço:Department of Food Science and Engineering, College of Biological Sciences and Technology, Beijing Key Laboratory of Forest Food Processing and Safety, Beijing Forestry University, Beijing 100083, China.
[Ti] Título:Peptides derived from tryptic hydrolysate of Bacillus subtilis culture suppress fungal spoilage of table grapes.
[So] Source:Food Chem;239:520-528, 2018 Jan 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:This study confirmed the anti-fungal effect of trypsin-treated Bacillus subtilis culture (BC) (tryptic hydrolysate, TH) on mold growth on Kyoho grapes. We examined the anti-fungal activity of TH by identifying TH peptides and performing a computational docking analysis. TH was more potent than untreated BC in suppressing fungal growth on grapes. Specifically, TH maintained grape freshness by inhibiting respiration and rachis browning, maintaining firmness, and preventing weight loss. Thirty-six inhibitory peptides against ß-1,3-glucan synthase (GS) were screened from 126 TH peptides identified through proteomic analysis. Among them, 13 peptides bound tightly to GS active pockets with lower binding energies than that of GppNHp. The most potent peptides, LFEIDEELNEK and FATSDLNDLYR, were synthesized, and further experiments showed that these peptides had a highly suppressive effect on GS activity and Aspergillus niger and Penicillium chrysogenum growth. Our results confirm that tryptic treatment is effective for improving the anti-fungal activity of BC.
[Mh] Termos MeSH primário: Bacillus subtilis
[Mh] Termos MeSH secundário: Peptídeos
Proteômica
Vitis
beta-Glucanas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (beta-Glucans); 9051-97-2 (beta-1,3-glucan)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE


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[PMID]:28910320
[Au] Autor:Muire PJ; Hanson LA; Wills R; Petrie-Hanson L
[Ad] Endereço:Department of Basic Sciences, College of Veterinary Medicine, Mississippi State University, Mississippi State, Mississippi, United States of America.
[Ti] Título:Differential gene expression following TLR stimulation in rag1-/- mutant zebrafish tissues and morphological descriptions of lymphocyte-like cell populations.
[So] Source:PLoS One;12(9):e0184077, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the absence of lymphocytes, rag1-/- mutant zebrafish develop protective immunity to bacteria. In mammals, induction of protection by innate immunity can be mediated by macrophages or natural killer (NK) cells. To elucidate potential responsive cell populations, we morphologically characterized lymphocyte-like cells (LLCs) from liver, spleen and kidney hematopoietic tissues. In fish, these cells include NK cells and Non-specific cytotoxic cells (NCCs). We also evaluated the transcriptional expression response of select genes that are important indicators of NK and macrophage activation after exposure to specific TLR ligands. The LLC cell populations could be discriminated by size and further discriminated by the presence of cytoplasmic granules. Expression levels of mx, tnfα, ifnγ, t-bet and nitr9 demonstrated dynamic changes in response to intra-coelomically administered ß glucan (a TLR2/6 ligand), Poly I:C (a TLR3 ligand) and resiquimod (R848) (a TLR7/8 ligand). Following TLR 2/6 stimulation, there was a greater than 100 fold increase in ifnγ in liver, kidney and spleen and moderate increases in tnfα in liver and kidney. TLR3 stimulation caused broad up regulation of mx, down-regulation of tnfα in kidney and spleen tissues and up regulation of nitr9 in the kidney. Following TLR 7/8 stimulation, there was a greater than 100 fold increase in ifnγ in liver and kidney and t-bet in liver. Our gene expression findings suggest that LLCs and macrophages are stimulated following ß glucan exposure. Poly I:C causes type I interferon response and mild induction of LLC in the kidney and R-848 exposure causes the strongest LLC stimulation. Overall, the strongest NK like gene expression occurred in the liver. These differential effects of TLR ligands in rag1-/- mutant zebrafish shows strong NK cell-like gene expression responses, especially in the liver, and provides tools to evaluate the basis for protective immunity mediated by the innate immune cells of fish.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica/imunologia
Proteínas de Homeodomínio/imunologia
Linfócitos/imunologia
Receptores Toll-Like/imunologia
Proteínas de Peixe-Zebra/imunologia
Peixe-Zebra/imunologia
[Mh] Termos MeSH secundário: Animais
Regulação da Expressão Gênica/efeitos dos fármacos
Regulação da Expressão Gênica/genética
Proteínas de Homeodomínio/genética
Imidazóis/farmacologia
Imunidade Inata/efeitos dos fármacos
Imunidade Inata/genética
Macrófagos/imunologia
Especificidade de Órgãos/efeitos dos fármacos
Especificidade de Órgãos/genética
Especificidade de Órgãos/imunologia
Poli I-C/farmacologia
Receptores Toll-Like/agonistas
Peixe-Zebra/genética
Proteínas de Peixe-Zebra/genética
beta-Glucanas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Homeodomain Proteins); 0 (Imidazoles); 0 (Toll-Like Receptors); 0 (Zebrafish Proteins); 0 (beta-Glucans); 128559-51-3 (RAG-1 protein); O84C90HH2L (Poly I-C); V3DMU7PVXF (resiquimod)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170915
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184077



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