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[PMID]:28468279
[Au] Autor:Terfrüchte M; Reindl M; Jankowski S; Sarkari P; Feldbrügge M; Schipper K
[Ad] Endereço:Institute for Microbiology, Cluster for Excellence on Plant Sciences, Heinrich Heine University Düsseldorf, 40204 Düsseldorf, Germany. marius.terfruechte@hhu.de.
[Ti] Título:Applying Unconventional Secretion in Ustilago maydis for the Export of Functional Nanobodies.
[So] Source:Int J Mol Sci;18(5), 2017 Apr 29.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Exploiting secretory pathways for production of heterologous proteins is highly advantageous with respect to efficient downstream processing. In eukaryotic systems the vast majority of heterologous proteins for biotechnological application is exported via the canonical endoplasmic reticulum-Golgi pathway. In the endomembrane system target proteins are often glycosylated and may thus be modified with foreign glycan patterns. This can be destructive for their activity or cause immune reactions against therapeutic proteins. Hence, using unconventional secretion for protein expression is an attractive alternative. In the fungal model , chitinase Cts1 is secreted via an unconventional pathway connected to cell separation which can be used to co-export heterologous proteins. Here, we apply this mechanism for the production of nanobodies. First, we achieved expression and unconventional secretion of a functional nanobody directed against green fluorescent protein (Gfp). Second, we found that Cts1 binds to chitin and that this feature can be applied to generate a Gfp-trap. Thus, we demonstrated the dual use of Cts1 serving both as export vehicle and as purification tag. Finally, we established and optimized the production of a nanobody against botulinum toxin A and hence describe the first pharmaceutically relevant target exported by Cts1-mediated unconventional secretion.
[Mh] Termos MeSH primário: Quitinases/metabolismo
Proteínas Fúngicas/metabolismo
Anticorpos de Domínio Único/metabolismo
Ustilago/metabolismo
[Mh] Termos MeSH secundário: Toxinas Botulínicas Tipo A/imunologia
Quitina/metabolismo
Clonagem Molecular
Proteínas de Fluorescência Verde/imunologia
Microbiologia Industrial
Transporte Proteico
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Proteínas Recombinantes/metabolismo
Anticorpos de Domínio Único/genética
Anticorpos de Domínio Único/imunologia
Ustilago/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Recombinant Proteins); 0 (Single-Domain Antibodies); 1398-61-4 (Chitin); 147336-22-9 (Green Fluorescent Proteins); EC 3.2.1.14 (Chitinases); EC 3.4.24.69 (Botulinum Toxins, Type A)
[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:170505
[St] Status:MEDLINE


  2 / 3078 MEDLINE  
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[PMID]:29257362
[Au] Autor:Sharma P; Choudhary B; Nagpure A; Gupta RK
[Ti] Título:Antifungal potential of actinomycete isolate Streptomyces exfoliates MT9 against wood-rotting fungi.
[So] Source:J Environ Biol;37(6):1231-37, 2016 Nov.
[Is] ISSN:0254-8704
[Cp] País de publicação:India
[La] Idioma:eng
[Ab] Resumo:An actinomycete isolate, Streptomyces exfoliatus MT9 was assessed for in vitro antagonism against wood-rotting fungi. Strain MT9 showed strong antagonistic activity (ZOI ? 25 mm) towards various tested wood-rotting fungi. Extracellular production of antifungal metabolite(s) including primary and secondary was monitored up to 10 days of submerged fermentation. Antagonist S. exfoliatus MT9 produces fungal cell-wall lytic enzymes, namely chitinase (3.098 U ml-1), b-1,3 glucanase (2.4 U ml-1) and protease (144.0 U ml-1) and also showed antifungal activity towards tested P. chrysosporium MTCC 787 (12.0 mm) and P. placenta MTCC 144 (16.0 mm). Extracellular culture filtrate (ECF) of S. exfoliatus MT9 also exhibited strong antifungal activity (ZOI ≥ 25 mm) towards tested wood-rotting fungi and n-butanol was found to be the suitable solvent for complete extraction of antifungal metabolite(s) from ECF. Reduced antifungal activity of n-butanol extract against P. chrysosporium MTCC 787 (11.00 mm) and P. placenta MTCC 144 (10.00 mm) on ergosterol agar plate, no activity against bacteria and characteristic UV spectra at 224 nm revealed the polyene nature of antifungal metabolite(s) present in the n-butanol extract. A novel actinomycete isolate, S. exfoliatus MT9 is producing antifungal metabolite(s) that makes it suitable for biotechnological processes and has the potential to be used as a bioactive agent for controlling wood-rotting fungi.
[Mh] Termos MeSH primário: Proteínas de Bactérias/farmacologia
Quitinases/metabolismo
Quitinases/farmacologia
Fungos/fisiologia
Streptomyces/enzimologia
Madeira/microbiologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Parede Celular/efeitos dos fármacos
Regulação Bacteriana da Expressão Gênica
Regulação Enzimológica da Expressão Gênica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 3.2.1.14 (Chitinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE


  3 / 3078 MEDLINE  
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[PMID]:29236932
[Au] Autor:Ortigão-Farias JR; Di-Blasi T; Telleria EL; Andorinho AC; Lemos-Silva T; Ramalho-Ortigão M; Tempone AJ; Traub-Csekö YM
[Ad] Endereço:Laboratório de Biologia Molecular de Parasitos e Vetores, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz-Fiocruz, Rio de Janeiro, RJ, Brasil.
[Ti] Título:Alternative splicing originates different domain structure organization of Lutzomyia longipalpis chitinases.
[So] Source:Mem Inst Oswaldo Cruz;113(2):96-101, 2018 Feb.
[Is] ISSN:1678-8060
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:BACKGROUND The insect chitinase gene family is composed by more than 10 paralogs, which can codify proteins with different domain structures. In Lutzomyia longipalpis, the main vector of visceral leishmaniasis in Brazil, a chitinase cDNA from adult female insects was previously characterized. The predicted protein contains one catalytic domain and one chitin-binding domain (CBD). The expression of this gene coincided with the end of blood digestion indicating a putative role in peritrophic matrix degradation. OBJECTIVES To determine the occurrence of alternative splicing in chitinases of L. longipalpis. METHODS We sequenced the LlChit1 gene from a genomic clone and the three spliced forms obtained by reverse transcription polymerase chain reaction (RT-PCR) using larvae cDNA. FINDINGS We showed that LlChit1 from L. longipalpis immature forms undergoes alternative splicing. The spliced form corresponding to the adult cDNA was named LlChit1A and the two larvae specific transcripts were named LlChit1B and LlChit1C. The B and C forms possess stop codons interrupting the translation of the CBD. The A form is present in adult females post blood meal, L4 larvae and pre-pupae, while the other two forms are present only in L4 larvae and disappear just before pupation. Two bands of the expected size were identified by Western blot only in L4 larvae. MAIN CONCLUSIONS We show for the first time alternative splicing generating chitinases with different domain structures increasing our understanding on the finely regulated digestion physiology and shedding light on a potential target for controlling L. longipalpis larval development.
[Mh] Termos MeSH primário: Processamento Alternativo/genética
Quitinases/genética
Sistema Digestório/enzimologia
Psychodidae/enzimologia
[Mh] Termos MeSH secundário: Animais
Quitinases/fisiologia
Feminino
Filogenia
Psychodidae/fisiologia
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.14 (Chitinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE


  4 / 3078 MEDLINE  
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[PMID]:27770452
[Au] Autor:Bogus MI; Wlóka E; Wronska A; Kaczmarek A; Kazek M; Zalewska K; Ligeza-Zuber M; Golebiowski M
[Ad] Endereço:Witold Stefanski Institute of Parasitology, Department of Molecular Biology, Polish Academy of Sciences, Warsaw, Poland.
[Ti] Título:Cuticle hydrolysis in four medically important fly species by enzymes of the entomopathogenic fungus Conidiobolus coronatus.
[So] Source:Med Vet Entomol;31(1):23-35, 2017 03.
[Is] ISSN:1365-2915
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Entomopathogenic fungi infect insects via penetration through the cuticle, which varies remarkably in chemical composition across species and life stages. Fungal infection involves the production of enzymes that hydrolyse cuticular proteins, chitin and lipids. Host specificity is associated with fungus-cuticle interactions related to substrate utilization and resistance to host-specific inhibitors. The soil fungus Conidiobolus coronatus (Constantin) (Entomophthorales: Ancylistaceae) shows virulence against susceptible species. The larvae and pupae of Calliphora vicina (Robineau-Desvoidy) (Diptera: Calliphoridae), Calliphora vomitoria (Linnaeus), Lucilia sericata (Meigen) (Diptera: Calliphoridae) and Musca domestica (Linnaeus) (Diptera: Muscidae) are resistant, but adults exposed to C. coronatus quickly perish. Fungus was cultivated for 3 weeks in a minimal medium. Cell-free filtrate, for which activity of elastase, N-acetylglucosaminidase, chitobiosidase and lipase was determined, was used for in vitro hydrolysis of the cuticle from larvae, puparia and adults. Amounts of amino acids, N-glucosamine and fatty acids released were measured after 8 h of incubation. The effectiveness of fungal enzymes was correlated with concentrations of compounds detected in the cuticles of tested insects. Positive correlations suggest compounds used by the fungus as nutrients, whereas negative correlations may indicate compounds responsible for insect resistance. Adult deaths result from the ingestion of conidia or fungal excretions.
[Mh] Termos MeSH primário: Exoesqueleto/microbiologia
Conidiobolus/fisiologia
Dípteros/microbiologia
Dípteros/fisiologia
[Mh] Termos MeSH secundário: Animais
Quitinases/metabolismo
Conidiobolus/enzimologia
Dípteros/crescimento & desenvolvimento
Feminino
Proteínas Fúngicas/metabolismo
Moscas Domésticas/crescimento & desenvolvimento
Moscas Domésticas/microbiologia
Moscas Domésticas/fisiologia
Hidrólise
Larva/crescimento & desenvolvimento
Larva/microbiologia
Larva/fisiologia
Lipase/metabolismo
Masculino
Peptídeo Hidrolases/metabolismo
Pupa/crescimento & desenvolvimento
Pupa/microbiologia
Pupa/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fungal Proteins); EC 3.1.1.3 (Lipase); EC 3.2.1.14 (Chitinases); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171220
[Lr] Data última revisão:
171220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE
[do] DOI:10.1111/mve.12202


  5 / 3078 MEDLINE  
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[PMID]:28833103
[Au] Autor:Wakita S; Kobayashi S; Kimura M; Kashimura A; Honda S; Sakaguchi M; Sugahara Y; Kamaya M; Matoska V; Bauer PO; Oyama F
[Ad] Endereço:Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo, Japan.
[Ti] Título:Mouse acidic mammalian chitinase exhibits transglycosylation activity at somatic tissue pH.
[So] Source:FEBS Lett;591(20):3310-3318, 2017 Oct.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mouse acidic mammalian chitinase (AMCase) degrades chitin with highest efficiency at pH 2.0 and is active up to pH 8.0. Here, we report that mouse AMCase also exhibits transglycosylation activity under neutral conditions. We incubated natural and artificial chitin substrates with mouse AMCase at pH 2.0 or 7.0 and analyzed the resulting oligomers using an improved method of fluorescence-assisted carbohydrate electrophoresis. Mouse AMCase produces primarily dimers of N-acetyl-d-glucosamine [(GlcNAc) ] under both pH conditions while generating transglycosylated (GlcNAc) primarily at pH 7.0 and at lower levels at pH 2.0. These results indicate that mouse AMCase catalyzes hydrolysis as well as transglycosylation and suggest that this enzyme can play a novel role under physiological conditions in peripheral tissues, such as the lungs.
[Mh] Termos MeSH primário: Acetilglucosamina/metabolismo
Quitina/metabolismo
Quitinases/metabolismo
[Mh] Termos MeSH secundário: Animais
Quitinases/genética
Clonagem Molecular
Dimerização
Eletroforese/métodos
Escherichia coli/genética
Escherichia coli/metabolismo
Fluorescência
Expressão Gênica
Glicosilação
Concentração de Íons de Hidrogênio
Hidrólise
Cinética
Pulmão/enzimologia
Camundongos
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Recombinant Proteins); 1398-61-4 (Chitin); EC 3.2.1.14 (AMCase, mouse); EC 3.2.1.14 (Chitinases); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170824
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12798


  6 / 3078 MEDLINE  
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[PMID]:28771547
[Au] Autor:Dutta J; Thakur D
[Ad] Endereço:Microbial Biotechnology Laboratory, Life Sciences Division, Institute of Advanced Study in Science and Technology, Guwahati, Assam, India.
[Ti] Título:Evaluation of multifarious plant growth promoting traits, antagonistic potential and phylogenetic affiliation of rhizobacteria associated with commercial tea plants grown in Darjeeling, India.
[So] Source:PLoS One;12(8):e0182302, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plant growth promoting rhizobacteria (PGPR) are studied in different agricultural crops but the interaction of PGPR of tea crop is not yet studied well. In the present study, the indigenous tea rhizobacteria were isolated from seven tea estates of Darjeeling located in West Bengal, India. A total of 150 rhizobacterial isolates were screened for antagonistic activity against six different fungal pathogens i.e. Nigrospora sphaerica (KJ767520), Pestalotiopsis theae (ITCC 6599), Curvularia eragostidis (ITCC 6429), Glomerella cingulata (MTCC 2033), Rhizoctonia Solani (MTCC 4633) and Fusarium oxysporum (MTCC 284), out of which 48 isolates were antagonist to at least one fungal pathogen used. These 48 isolates exhibited multifarious antifungal properties like the production of siderophore, chitinase, protease and cellulase and also plant growth promoting (PGP) traits like IAA production, phosphate solubilization, ammonia and ACC deaminase production. Amplified ribosomal DNA restriction analysis (ARDRA) and BOX-PCR analysis based genotyping clustered the isolates into different groups. Finally, four isolates were selected for plant growth promotion study in two tea commercial cultivars TV-1 and Teenali-17 in nursery conditions. The plant growth promotion study showed that the inoculation of consortia of these four PGPR isolates significantly increased the growth of tea plant in nursery conditions. Thus this study underlines the commercial potential of these selected PGPR isolates for sustainable tea cultivation.
[Mh] Termos MeSH primário: Alphaproteobacteria/classificação
Alphaproteobacteria/metabolismo
Camellia sinensis/crescimento & desenvolvimento
Camellia sinensis/microbiologia
Filogenia
[Mh] Termos MeSH secundário: Alphaproteobacteria/isolamento & purificação
Amônia/metabolismo
Antifúngicos/metabolismo
Antifúngicos/farmacologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Fosfatos de Cálcio/metabolismo
Carbono-Carbono Liases/metabolismo
Celulase/genética
Celulase/metabolismo
Quitinases/genética
Quitinases/metabolismo
DNA Fúngico/isolamento & purificação
DNA Fúngico/metabolismo
Fungos/efeitos dos fármacos
Genótipo
Glicosídeo Hidrolases/genética
Glicosídeo Hidrolases/metabolismo
Índia
Ácidos Indolacéticos/metabolismo
Raízes de Plantas/crescimento & desenvolvimento
Raízes de Plantas/microbiologia
RNA Ribossômico 16S/classificação
RNA Ribossômico 16S/isolamento & purificação
RNA Ribossômico 16S/metabolismo
Sideróforos/metabolismo
Sideróforos/farmacologia
Microbiologia do Solo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Bacterial Proteins); 0 (Calcium Phosphates); 0 (DNA, Fungal); 0 (Indoleacetic Acids); 0 (RNA, Ribosomal, 16S); 0 (Siderophores); 6U1S09C61L (indoleacetic acid); 7664-41-7 (Ammonia); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.14 (Chitinases); EC 3.2.1.4 (Cellulase); EC 3.5.99.7 (1-aminocyclopropane-1-carboxylate deaminase); EC 4.1.- (Carbon-Carbon Lyases); K4C08XP666 (tricalcium phosphate)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182302


  7 / 3078 MEDLINE  
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[PMID]:28738346
[Au] Autor:Li Y; Huang J; Li L; Liu L
[Ad] Endereço:State Key Laboratory for Diagnosis and Treatment of Infectious Diseases, The First Affiliated Hospital, College of Medicine, Zhejiang University, Hangzhou, China.
[Ti] Título:Synergistic Activity of Berberine with Azithromycin against Pseudomonas Aeruginosa Isolated from Patients with Cystic Fibrosis of Lung In Vitro and In Vivo.
[So] Source:Cell Physiol Biochem;42(4):1657-1669, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Pseudomonas aeruginosa (PA) is one of the major opportunistic pathogens which can cause chronic lung infection of cystic fibrosis (CF). The formation of PA biofilm promotes CF development and restricts the antimicrobial efficacies of current antibiotics. METHODS: The antimicrobial effects of azithromycin (AZM) and berberine (BER) alone and in combination were evaluated using microdilution method, checkerboard assay, time-kill test, qRT-PCR analysis and absorption method. The treatments of AZM and/or BER were further evaluated in an animal lung infection model via observing survival rate, bacterial burden and histopathology of lung, the levels of pro-/anti-inflammatory cytokines. RESULTS: AZM-BER were demonstrated to be synergistic against ten clinical PA isolates as well as the standard reference PA ATCC27853, in which PA03 was the most susceptible isolate to AZM-BER with FICI of 0.13 and chosen for subsequent experiments. The synergism of AZM-BER was further confirmed against PA03 in time-kill test and scanning electron microscope (SEM) at their concentrations showing synergism. In PA03, we found that AZM-BER could significantly attenuate productions of a series of virulence factors including alginate, LasA protease, LasB protease, pyoverdin, pyocyanin, chitinase as well as extracellular DNA, and remarkably inhibit the levels of quorum sensing (QS) molecules and the expressions of lasI, lasR, rhlI, rhlR at 1/2×MIC, 1×MIC and 2×MIC. In the infection model, the mice survival were increased markedly, the inflammations of infected lungs were improved greatly along with reduced IL-6, IL-8 and ascended IL-10 at 0.8 mg/kg of AZM combined with 3.2 mg/kg of BER. CONCLUSION: BER might be a promising synergist to enhance the antimicrobial activity of AZM in vitro and in vivo.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Azitromicina/farmacologia
Berberina/farmacologia
Biofilmes/efeitos dos fármacos
Infecções por Pseudomonas/tratamento farmacológico
Pseudomonas aeruginosa/efeitos dos fármacos
[Mh] Termos MeSH secundário: Alginatos
Animais
Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Biofilmes/crescimento & desenvolvimento
Quitinases/antagonistas & inibidores
Quitinases/genética
Quitinases/metabolismo
Ciclofosfamida
Fibrose Cística/microbiologia
DNA Bacteriano/antagonistas & inibidores
DNA Bacteriano/biossíntese
Combinação de Medicamentos
Sinergismo Farmacológico
Ácido Glucurônico/antagonistas & inibidores
Ácido Glucurônico/biossíntese
Ácidos Hexurônicos/antagonistas & inibidores
Seres Humanos
Pulmão/efeitos dos fármacos
Pulmão/metabolismo
Pulmão/microbiologia
Metaloendopeptidases/antagonistas & inibidores
Metaloendopeptidases/genética
Metaloendopeptidases/metabolismo
Metaloproteases/antagonistas & inibidores
Metaloproteases/genética
Metaloproteases/metabolismo
Camundongos
Camundongos Endogâmicos BALB C
Testes de Sensibilidade Microbiana
Neutropenia/induzido quimicamente
Neutropenia/tratamento farmacológico
Neutropenia/genética
Neutropenia/patologia
Oligopeptídeos/antagonistas & inibidores
Oligopeptídeos/biossíntese
Infecções por Pseudomonas/induzido quimicamente
Infecções por Pseudomonas/genética
Infecções por Pseudomonas/patologia
Pseudomonas aeruginosa/crescimento & desenvolvimento
Pseudomonas aeruginosa/patogenicidade
Piocianina/antagonistas & inibidores
Piocianina/biossíntese
Fatores de Virulência/antagonistas & inibidores
Fatores de Virulência/genética
Fatores de Virulência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alginates); 0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (Drug Combinations); 0 (Hexuronic Acids); 0 (Oligopeptides); 0 (Virulence Factors); 0I8Y3P32UF (Berberine); 8062-00-8 (pyoverdin); 83905-01-5 (Azithromycin); 8A5D83Q4RW (Glucuronic Acid); 8C3Z4148WZ (alginic acid); 8N3DW7272P (Cyclophosphamide); 9OQM399341 (Pyocyanine); EC 3.2.1.14 (Chitinases); EC 3.4.- (LasA protein, Pseudomonas aeruginosa); EC 3.4.- (Metalloproteases); EC 3.4.24.- (Metalloendopeptidases); EC 3.4.24.26 (pseudolysin, Pseudomonas aeruginosa)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1159/000479411


  8 / 3078 MEDLINE  
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[PMID]:28721730
[Au] Autor:Niu X; Zhou JS; Wang YX; Liu CC; Liu ZH; Yuan S
[Ad] Endereço:Jiangsu Key Laboratory for Microbes and Microbial Functional Genomics, Jiangsu Engineering and Technology Research Center for Industrialization of Microbial Resources, College of Life Science, Nanjing Normal University , Nanjing, PR China 210023.
[Ti] Título:Heterologous Expression and Characterization of a Novel Chitinase (ChiEn1) from Coprinopsis cinerea and its Synergism in the Degradation of Chitin.
[So] Source:J Agric Food Chem;65(32):6943-6956, 2017 Aug 16.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chitinase ChiEn1 did not hydrolyze insoluble chitin but showed hydrolysis and transglycosylation activities toward chitin-oligosaccharides. Interestingly, the addition of ChiEn1 increased the amount of reducing sugars released from chitin powder by endochitinase ChiIII by 105.0%, and among the released reducing sugars the amount of (GlcNAc) was increased by 149.5%, whereas the amount of GlcNAc was decreased by 10.3%. The percentage of GlcNAc in the products of chitin powder with the combined ChiIII and ChiEn1 was close to that in the products of chitin-oligosaccharides with ChiEn1, rather than that with ChiIII. These results indicate that chitin polymers are first degraded into chitin oligosaccharides by ChiIII and the latter are further degraded to monomers and dimers by ChiEn1, and the synergistic action of ChiEn1 and ChiIII is involved in the efficient degradation of chitin in cell walls during pileus autolysis. The structure modeling explores the molecular base of ChiEn1 action.
[Mh] Termos MeSH primário: Agaricales/enzimologia
Quitina/metabolismo
Quitinases/genética
Quitinases/metabolismo
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
[Mh] Termos MeSH secundário: Agaricales/metabolismo
Biocatálise
Quitina/biossíntese
Quitinases/química
Quitinases/isolamento & purificação
Proteínas Fúngicas/química
Proteínas Fúngicas/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 1398-61-4 (Chitin); EC 3.2.1.14 (Chitinases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170720
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b02278


  9 / 3078 MEDLINE  
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[PMID]:28610983
[Au] Autor:Maccari G; Deodato D; Fiorucci D; Orofino F; Truglio GI; Pasero C; Martini R; De Luca F; Docquier JD; Botta M
[Ad] Endereço:Department of Biotechnology, Chemistry and Pharmacy, University of Siena, I-53100 Siena, Italy.
[Ti] Título:Design and synthesis of a novel inhibitor of T. Viride chitinase through an in silico target fishing protocol.
[So] Source:Bioorg Med Chem Lett;27(15):3332-3336, 2017 08 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In the last ten years, we identified and developed a new therapeutic class of antifungal agents, the macrocyclic amidinoureas. These compounds are active against several Candida species, including clinical isolates resistant to currently available antifungal drugs. The mode of action of these molecules is still unknown. In this work, we developed an in-silico target fishing procedure to identify a possible target for this class of compounds based on shape similarity, inverse docking procedure and consensus score rank-by-rank. Chitinase enzyme emerged as possible target. To confirm this hypothesis a novel macrocyclic derivative has been produced, specifically designed to increase the inhibition of the chitinase. Biological evaluation highlights a stronger enzymatic inhibition for the new derivative, while its antifungal activity drops probably because of pharmacokinetic issues. Collectively, our data suggest that chitinase represent at least one of the main target of macrocyclic amidinoureas.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Quitinases/antagonistas & inibidores
Desenho de Drogas
Inibidores Enzimáticos/farmacologia
Trichoderma/efeitos dos fármacos
[Mh] Termos MeSH secundário: Antifúngicos/síntese química
Antifúngicos/química
Quitinases/metabolismo
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Testes de Sensibilidade Microbiana
Modelos Moleculares
Estrutura Molecular
Relação Estrutura-Atividade
Trichoderma/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Enzyme Inhibitors); EC 3.2.1.14 (Chitinases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171125
[Lr] Data última revisão:
171125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170615
[St] Status:MEDLINE


  10 / 3078 MEDLINE  
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[PMID]:28526403
[Au] Autor:Kintsu H; Okumura T; Negishi L; Ifuku S; Kogure T; Sakuda S; Suzuki M
[Ad] Endereço:Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, 113-8657, Japan.
[Ti] Título:Crystal defects induced by chitin and chitinolytic enzymes in the prismatic layer of Pinctada fucata.
[So] Source:Biochem Biophys Res Commun;489(2):89-95, 2017 Jul 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biomineralization, in which organisms create biogenic hard tissues, with hardness or flexibility enhanced by organic-inorganic interaction is an interesting and attractive focus for application of biomimetic functional materials. Calcites in the prismatic layer of Pinctada fucata are tougher than abiotic calcites due to small crystal defects. However, the molecular mechanism of the defect formation remains unclear. Here, chitin and two chitinolytic enzymes, chitinase and chitobiase, were identified as organic matrices related to for the formation of small crystal defects in the prismatic layer. Experiments with a chitinase inhibitor in vivo showed chitinase is necessary to form the prismatic layer. Analysis of calcite crystals, which were synthesized in a chitin hydrogel treated with chitinolytic enzymes, by electron microscopy and X-ray diffraction showed that crystal defects became larger as chitin was more degraded. These results suggest that interactions between chitin and calcium carbonate increase as chitin is thinner.
[Mh] Termos MeSH primário: Acetilglucosaminidase/química
Quitina/química
Quitinases/química
Pinctada/química
[Mh] Termos MeSH secundário: Acetilglucosaminidase/metabolismo
Acetilglucosaminidase/ultraestrutura
Animais
Quitina/metabolismo
Quitina/ultraestrutura
Quitinases/metabolismo
Quitinases/ultraestrutura
Microscopia Eletrônica
Tamanho da Partícula
Pinctada/metabolismo
Pinctada/ultraestrutura
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
1398-61-4 (Chitin); EC 3.2.1.14 (Chitinases); EC 3.2.1.52 (Acetylglucosaminidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170521
[St] Status:MEDLINE



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