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  1 / 1020 MEDLINE  
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[PMID]:28827815
[Au] Autor:Mamedov T; Cicek K; Gulec B; Ungor R; Hasanova G
[Ad] Endereço:Akdeniz University, Department of Agricultural Biotechnology, Antalya, Turkey.
[Ti] Título:In vivo production of non-glycosylated recombinant proteins in Nicotiana benthamiana plants by co-expression with Endo-ß-N-acetylglucosaminidase H (Endo H) of Streptomyces plicatus.
[So] Source:PLoS One;12(8):e0183589, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A plant transient expression system, with eukaryotic post-translational modification machinery, offers superior efficiency, scalability, safety, and lower cost over other expression systems. However, due to aberrant N-glycosylation, this expression system may not be a suitable expression platform for proteins not carrying N-linked glycans in the native hosts. Therefore, it is crucial to develop a strategy to produce target proteins in a non-glycosylated form while preserving their native sequence, conformation and biological activity. Previously, we developed a strategy for enzymatic deglycosylation of proteins in planta by co-expressing bacterial peptide-N-glycosidase F (PNGase F). Though PNGase F removes oligosaccharides from glycosylated proteins, in so doing it causes an amino acid change due to the deamidation of asparagine to aspartate in the N-X-S/T site. Endo-ß-N-acetylglucosaminidase (EC3.2.1.96, Endo H), another deglycosylating enzyme, catalyzes cleavage between two N-Acetyl-D-glucosamine residues of the chitobiose core of N-linked glycans, leaving a single N-Acetyl-D-glucosamine residue without the concomitant deamidation of asparagine. In this study, a method for in vivo deglycosylation of recombinant proteins in plants by transient co-expression with bacterial Endo H is described for the first time. Endo H was fully active in vivo. and successfully cleaved N-linked glycans from glycoproteins were tested. In addition, unlike the glycosylated form, in vivo Endo H deglycosylated Pfs48/45 was recognized by conformational specific Pfs48/45 monoclonal antibody, in a manner similar to its PNGase F deglycosylated counterpart. Furthermore, the deglycosylated PA83 molecule produced by Endo H showed better stability than a PNGase F deglycosylated counterpart. Thus, an Endo H in vivo deglycosylation approach provides another opportunity to develop vaccine antigens, therapeutic proteins, antibodies, and industrial enzymes.
[Mh] Termos MeSH primário: Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/metabolismo
Proteínas de Plantas/biossíntese
Streptomyces/metabolismo
Tabaco/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Clonagem Molecular
Glicosilação
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/química
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/genética
Proteínas Recombinantes/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Recombinant Proteins); EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183589


  2 / 1020 MEDLINE  
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[PMID]:28614667
[Au] Autor:Lee SM; Booe JM; Gingell JJ; Sjoelund V; Hay DL; Pioszak AA
[Ad] Endereço:Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center , 975 NE 10th Street BRC 462B, Oklahoma City, Oklahoma 73104, United States.
[Ti] Título:N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity.
[So] Source:Biochemistry;56(26):3380-3393, 2017 Jul 05.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The calcitonin receptor (CTR) is a class B G protein-coupled receptor that is activated by the peptide hormones calcitonin and amylin. Calcitonin regulates bone remodeling through CTR, whereas amylin regulates blood glucose and food intake by activating CTR in complex with receptor activity-modifying proteins (RAMPs). These receptors are targeted clinically for the treatment of osteoporosis and diabetes. Here, we define the role of CTR N-glycosylation in hormone binding using purified calcitonin and amylin receptor extracellular domain (ECD) glycoforms and fluorescence polarization/anisotropy and isothermal titration calorimetry peptide-binding assays. N-Glycan-free CTR ECD produced in Escherichia coli exhibited ∼10-fold lower peptide affinity than CTR ECD produced in HEK293T cells, which yield complex N-glycans, or in HEK293S GnTI cells, which yield core N-glycans (Man GlcNAc ). PNGase F-catalyzed removal of N-glycans at N73, N125, and N130 in the CTR ECD decreased peptide affinity ∼10-fold, whereas Endo H-catalyzed trimming of the N-glycans to single GlcNAc residues had no effect on peptide binding. Similar results were observed for an amylin receptor RAMP2-CTR ECD complex. Characterization of peptide-binding affinities of purified N → Q CTR ECD glycan site mutants combined with PNGase F and Endo H treatment strategies and mass spectrometry to define the glycan species indicated that a single GlcNAc residue at CTR N130 was responsible for the peptide affinity enhancement. Molecular modeling suggested that this GlcNAc functions through an allosteric mechanism rather than by directly contacting the peptide. These results reveal an important role for N-linked glycosylation in the peptide hormone binding of a clinically relevant class B GPCR.
[Mh] Termos MeSH primário: Asparagina/metabolismo
Calcitonina/metabolismo
Polipeptídeo Amiloide das Ilhotas Pancreáticas/metabolismo
Modelos Moleculares
Processamento de Proteína Pós-Traducional
Proteína 2 Modificadora da Atividade de Receptores/metabolismo
Receptores da Calcitonina/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosamina/química
Acetilglucosamina/metabolismo
Substituição de Aminoácidos
Asparagina/química
Sítios de Ligação
Calcitonina/química
Glicosilação
Células HEK293
Seres Humanos
Polipeptídeo Amiloide das Ilhotas Pancreáticas/química
Cinética
Ligantes
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/genética
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/metabolismo
Conformação Molecular
Mutação
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Peptídeo-N4-(N-acetil-beta-glucosaminil) Asparagina Amidase/metabolismo
Domínios e Motivos de Interação entre Proteínas
Proteína 2 Modificadora da Atividade de Receptores/agonistas
Proteína 2 Modificadora da Atividade de Receptores/química
Proteína 2 Modificadora da Atividade de Receptores/genética
Receptores da Calcitonina/agonistas
Receptores da Calcitonina/química
Receptores da Calcitonina/genética
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Islet Amyloid Polypeptide); 0 (Ligands); 0 (Peptide Fragments); 0 (RAMP2 protein, human); 0 (Receptor Activity-Modifying Protein 2); 0 (Receptors, Calcitonin); 0 (Recombinant Fusion Proteins); 7006-34-0 (Asparagine); 9007-12-9 (Calcitonin); EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase); EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170615
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00256


  3 / 1020 MEDLINE  
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[PMID]:28512024
[Au] Autor:Bi Y; Might M; Vankayalapati H; Kuberan B
[Ad] Endereço:Department of Medicinal Chemistry, University of Utah, Salt Lake City, Utah 84112, United States.
[Ti] Título:Repurposing of Proton Pump Inhibitors as first identified small molecule inhibitors of endo-ß-N-acetylglucosaminidase (ENGase) for the treatment of NGLY1 deficiency, a rare genetic disease.
[So] Source:Bioorg Med Chem Lett;27(13):2962-2966, 2017 07 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:N-Glycanase deficiency, or NGLY1 deficiency, is an extremely rare human genetic disease. N-Glycanase, encoded by the gene NGLY1, is an important enzyme involved in protein deglycosylation of misfolded proteins. Deglycosylation of misfolded proteins precedes the endoplasmic reticulum (ER)-associated degradation (ERAD) process. NGLY1 patients produce little or no N-glycanase (Ngly1), and the symptoms include global developmental delay, frequent seizures, complex hyperkinetic movement disorder, difficulty in swallowing/aspiration, liver dysfunction, and a lack of tears. Unfortunately, there has not been any therapeutic option available for this rare disease so far. Recently, a proposed molecular mechanism for NGLY1 deficiency suggested that endo-ß-N-acetylglucosaminidase (ENGase) inhibitors may be promising therapeutics for NGLY1 patients. Herein, we performed structure-based virtual screening utilizing FDA-approved drug database on this ENGase target to enable repurposing of existing drugs. Several Proton Pump Inhibitors (PPIs), a series of substituted 1H-benzo [d] imidazole, and 1H-imidazo [4,5-b] pyridines, among other scaffolds, have been identified as potent ENGase inhibitors. An electrophoretic mobility shift assay was employed to assess the inhibition of ENGase activity by these PPIs. Our efforts led to the discovery of Rabeprazole Sodium as the most promising hit with an IC of 4.47±0.44µM. This is the first report that describes the discovery of small molecule ENGase inhibitors, which can potentially be used for the treatment of human NGLY1 deficiency.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Doenças Genéticas Inatas/tratamento farmacológico
Inibidores da Bomba de Prótons/farmacologia
Bombas de Próton/metabolismo
Rabeprazol/farmacologia
Bibliotecas de Moléculas Pequenas/farmacologia
[Mh] Termos MeSH secundário: Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Doenças Genéticas Inatas/genética
Seres Humanos
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/antagonistas & inibidores
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/metabolismo
Estrutura Molecular
Peptídeo-N4-(N-acetil-beta-glucosaminil) Asparagina Amidase/deficiência
Peptídeo-N4-(N-acetil-beta-glucosaminil) Asparagina Amidase/metabolismo
Inibidores da Bomba de Prótons/síntese química
Inibidores da Bomba de Prótons/química
Rabeprazol/síntese química
Rabeprazol/química
Bibliotecas de Moléculas Pequenas/síntese química
Bibliotecas de Moléculas Pequenas/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Proton Pump Inhibitors); 0 (Proton Pumps); 0 (Small Molecule Libraries); 32828355LL (Rabeprazole); EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase); EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170518
[St] Status:MEDLINE


  4 / 1020 MEDLINE  
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[PMID]:28426790
[Au] Autor:Fujihira H; Masahara-Negishi Y; Tamura M; Huang C; Harada Y; Wakana S; Takakura D; Kawasaki N; Taniguchi N; Kondoh G; Yamashita T; Funakoshi Y; Suzuki T
[Ad] Endereço:Glycometabolome Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, Saitama, Japan.
[Ti] Título:Lethality of mice bearing a knockout of the Ngly1-gene is partially rescued by the additional deletion of the Engase gene.
[So] Source:PLoS Genet;13(4):e1006696, 2017 Apr.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cytoplasmic peptide:N-glycanase (Ngly1 in mammals) is a de-N-glycosylating enzyme that is highly conserved among eukaryotes. It was recently reported that subjects harboring mutations in the NGLY1 gene exhibited severe systemic symptoms (NGLY1-deficiency). While the enzyme obviously has a critical role in mammals, its precise function remains unclear. In this study, we analyzed Ngly1-deficient mice and found that they are embryonic lethal in C57BL/6 background. Surprisingly, the additional deletion of the gene encoding endo-ß-N-acetylglucosaminidase (Engase), which is another de-N-glycosylating enzyme but leaves a single GlcNAc at glycosylated Asn residues, resulted in the partial rescue of the lethality of the Ngly1-deficient mice. Additionally, we also found that a change in the genetic background of C57BL/6 mice, produced by crossing the mice with an outbred mouse strain (ICR) could partially rescue the embryonic lethality of Ngly1-deficient mice. Viable Ngly1-deficient mice in a C57BL/6 and ICR mixed background, however, showed a very severe phenotype reminiscent of the symptoms of NGLY1-deficiency subjects. Again, many of those defects were strongly suppressed by the additional deletion of Engase in the C57BL/6 and ICR mixed background. The defects observed in Ngly1/Engase-deficient mice (C57BL/6 background) and Ngly1-deficient mice (C57BL/6 and ICR mixed background) closely resembled some of the symptoms of patients with an NGLY1-deficiency. These observations strongly suggest that the Ngly1- or Ngly1/Engase-deficient mice could serve as a valuable animal model for studies related to the pathogenesis of the NGLY1-deficiency, and that cytoplasmic ENGase represents one of the potential therapeutic targets for this genetic disorder.
[Mh] Termos MeSH primário: Doenças Genéticas Inatas/genética
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/genética
Peptídeo-N4-(N-acetil-beta-glucosaminil) Asparagina Amidase/deficiência
Peptídeo-N4-(N-acetil-beta-glucosaminil) Asparagina Amidase/genética
[Mh] Termos MeSH secundário: Animais
Citoplasma/enzimologia
Doenças Genéticas Inatas/terapia
Glicosilação
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Modelos Animais
Peptídeo-N4-(N-acetil-beta-glucosaminil) Asparagina Amidase/metabolismo
Deleção de Sequência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase); EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170602
[Lr] Data última revisão:
170602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006696


  5 / 1020 MEDLINE  
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[PMID]:28187141
[Au] Autor:Chang X; Xu B; Bai Y; Luo H; Ma R; Shi P; Yao B
[Ad] Endereço:College of Biological Sciences and Engineering, Jiangxi Agricultural University, Nanchang, People's Republic of China.
[Ti] Título:Role of N-linked glycosylation in the enzymatic properties of a thermophilic GH 10 xylanase from Aspergillus fumigatus expressed in Pichia pastoris.
[So] Source:PLoS One;12(2):e0171111, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-Glycosylation is a posttranslational modification commonly occurred in fungi and plays roles in a variety of enzyme functions. In this study, a xylanase (Af-XYNA) of glycoside hydrolase (GH) family 10 from Aspergillus fumigatus harboring three potential N-glycosylation sites (N87, N124 and N335) was heterologously produced in Pichia pastoris. The N-glycosylated Af-XYNA (WT) exhibited favorable temperature and pH optima (75°C and pH 5.0) and good thermostability (maintaining stable at 60°C). To reveal the role of N-glycosylation on Af-XYNA, the enzyme was deglycosylated by endo-ß-N-acetylglucosaminidase H (DE) or modified by site-directed mutagenesis at N124 (N124T). The deglycosylated DE and mutant N124T showed narrower pH adaptation range, lower specific activity, and worse pH and thermal stability. Further thermodynamic analysis revealed that the enzyme with higher N-glycosylation degree was more thermostable. This study demonstrated that the effects of glycosylation at different degrees and sites were diverse, in which the glycan linked to N124 played a key role in pH and thermal stability of Af-XYNA.
[Mh] Termos MeSH primário: Aspergillus fumigatus/enzimologia
Proteínas Fúngicas/metabolismo
Pichia/enzimologia
Processamento de Proteína Pós-Traducional
Xilosidases/metabolismo
[Mh] Termos MeSH secundário: Aspergillus fumigatus/genética
Estabilidade Enzimática
Proteínas Fúngicas/química
Proteínas Fúngicas/genética
Glicosilação
Temperatura Alta
Concentração de Íons de Hidrogênio
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/metabolismo
Mutação de Sentido Incorreto
Pichia/genética
Polissacarídeos/metabolismo
Xilosidases/química
Xilosidases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Polysaccharides); EC 3.2.1.- (Xylosidases); EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170211
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0171111


  6 / 1020 MEDLINE  
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[PMID]:27714557
[Au] Autor:Higuchi Y; Eshima Y; Huang Y; Kinoshita T; Sumiyoshi W; Nakakita SI; Takegawa K
[Ad] Endereço:Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Fukuoka, 812-8581, Japan.
[Ti] Título:Highly efficient transglycosylation of sialo-complex-type oligosaccharide using Coprinopsis cinerea endoglycosidase and sugar oxazoline.
[So] Source:Biotechnol Lett;39(1):157-162, 2017 Jan.
[Is] ISSN:1573-6776
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: To establish an efficient method of chemoenzymatic modification for making N-linked oligosaccharide chains of glycoproteins structurally homogeneous, which crucially affects their bioactivities. RESULTS: Deglycosylated-RNase B (GlcNAc-RNase B; acceptor), sialylglyco (SG)-oxazoline (donor) and an N180H mutant of Coprinopsis cinerea endo-ß-N-acetylglucosaminidase (Endo-CC ) were employed. pH 7.5 was ideal for both SG-oxazoline's stability and Endo-CC's transglycosylation reaction. The most efficient reaction conditions for producing glycosylated-RNase B, virtually modified completely with sialo-biantennary-type complex oligosaccharide, were: 80 µg GlcNAc-RNase B, 200 µg SG-oxazoline and 3 µg Endo-CC in 20 µl 20 mM Tris/HCl pH 7.5 at 30 °C for 30-60 min. CONCLUSIONS: This transglycosylation method using SG-oxazoline and Endo-CC is beneficial for producing pharmaceutical glycoproteins modified with homogenous biantennary-complex-type oligosaccharides.
[Mh] Termos MeSH primário: Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/metabolismo
Oligossacarídeos/metabolismo
[Mh] Termos MeSH secundário: Glicosilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligosaccharides); EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170308
[Lr] Data última revisão:
170308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161008
[St] Status:MEDLINE
[do] DOI:10.1007/s10529-016-2230-0


  7 / 1020 MEDLINE  
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[PMID]:27131291
[Au] Autor:Yamanoi T; Oda Y; Katsuraya K; Inazu T; Yamamoto K
[Ad] Endereço:Faculty of Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado, Saitama 350-0295, Japan. Electronic address: yamanoi1119@gmail.com.
[Ti] Título:Complete NMR assignment of a bisecting hybrid-type oligosaccharide transferred by Mucor hiemalis endo-ß-N-acetylglucosaminidase.
[So] Source:Carbohydr Res;427:60-5, 2016 Jun 02.
[Is] ISSN:1873-426X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:This study describes the complete nuclear magnetic resonance (NMR) spectral assignment of a bisecting hybrid-type oligosaccharide 1, transferred by Mucor hiemalis endo-ß-N-acetylglucosaminidase (Endo-M). Through (1)H- and (13)C-NMR, DQF-COSY, HSQC, HMBC, TOCSY, and NOESY experiments, we determine the structure of the glycoside linkage formed by the Endo-M transglycosylation, i.e., the connection between GlcNAc and GlcNAc in oligosaccharide 1.
[Mh] Termos MeSH primário: Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/metabolismo
Mucor/enzimologia
Oligossacarídeos/química
[Mh] Termos MeSH secundário: Sequência de Carboidratos
Glicosilação
Espectroscopia de Ressonância Magnética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligosaccharides); EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170203
[Lr] Data última revisão:
170203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160501
[St] Status:MEDLINE


  8 / 1020 MEDLINE  
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[PMID]:27101370
[Au] Autor:Mamedov T; Chichester JA; Jones RM; Ghosh A; Coffin MV; Herschbach K; Prokhnevsky AI; Streatfield SJ; Yusibov V
[Ad] Endereço:Fraunhofer USA Center for Molecular Biotechnology, Newark, Delaware, United States of America.
[Ti] Título:Production of Functionally Active and Immunogenic Non-Glycosylated Protective Antigen from Bacillus anthracis in Nicotiana benthamiana by Co-Expression with Peptide-N-Glycosidase F (PNGase F) of Flavobacterium meningosepticum.
[So] Source:PLoS One;11(4):e0153956, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacillus anthracis has long been considered a potential biological warfare agent, and therefore, there is a need for a safe, low-cost and highly efficient anthrax vaccine with demonstrated long-term stability for mass vaccination in case of an emergency. Many efforts have been made towards developing an anthrax vaccine based on recombinant protective antigen (rPA) of B. anthracis, a key component of the anthrax toxin, produced using different expression systems. Plants represent a promising recombinant protein production platform due to their relatively low cost, rapid scalability and favorable safety profile. Previous studies have shown that full-length rPA produced in Nicotiana benthamiana (pp-PA83) is immunogenic and can provide full protection against lethal spore challenge; however, further improvement in the potency and stability of the vaccine candidate is necessary. PA of B. anthracis is not a glycoprotein in its native host; however, this protein contains potential N-linked glycosylation sites, which can be aberrantly glycosylated during expression in eukaryotic systems including plants. This glycosylation could affect the availability of certain key epitopes either due to masking or misfolding of the protein. Therefore, a non-glycosylated form of pp-PA83 was engineered and produced in N. benthamiana using an in vivo deglycosylation approach based on co-expression of peptide-N-glycosidase F (PNGase F) from Flavobacterium meningosepticum. For comparison, versions of pp-PA83 containing point mutations in six potential N-glycosylation sites were also engineered and expressed in N. benthamiana. The in vivo deglycosylated pp-PA83 (pp-dPA83) was shown to have in vitro activity, in contrast to glycosylated pp-PA83, and to induce significantly higher levels of toxin-neutralizing antibody responses in mice compared with glycosylated pp-PA83, in vitro deglycosylated pp-PA83 or the mutated versions of pp-PA83. These results suggest that pp-dPA83 may offer advantages in terms of dose sparing and enhanced immunogenicity as a promising candidate for a safe, effective and low-cost subunit vaccine against anthrax.
[Mh] Termos MeSH primário: Vacinas contra Antraz/genética
Antígenos de Bactérias/genética
Bacillus anthracis/genética
Toxinas Bacterianas/genética
Flavobacterium/enzimologia
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/metabolismo
Tabaco/genética
[Mh] Termos MeSH secundário: Animais
Antraz/imunologia
Antraz/prevenção & controle
Vacinas contra Antraz/imunologia
Vacinas contra Antraz/metabolismo
Antígenos de Bactérias/imunologia
Antígenos de Bactérias/metabolismo
Toxinas Bacterianas/imunologia
Toxinas Bacterianas/metabolismo
Clonagem Molecular
Flavobacterium/genética
Glicosilação
Imunidade
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/genética
Camundongos Endogâmicos BALB C
Plantas Geneticamente Modificadas/genética
Engenharia de Proteínas
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anthrax Vaccines); 0 (Antigens, Bacterial); 0 (Bacterial Toxins); 0 (Recombinant Proteins); 0 (anthrax toxin); EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160422
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0153956


  9 / 1020 MEDLINE  
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[PMID]:27084007
[Au] Autor:Karav S; Le Parc A; Leite Nobrega de Moura Bell JM; Frese SA; Kirmiz N; Block DE; Barile D; Mills DA
[Ad] Endereço:Department of Food Science and Technology, University of California, Davis, California, USA.
[Ti] Título:Oligosaccharides Released from Milk Glycoproteins Are Selective Growth Substrates for Infant-Associated Bifidobacteria.
[So] Source:Appl Environ Microbiol;82(12):3622-30, 2016 Jun 15.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Milk, in addition to nourishing the neonate, provides a range of complex glycans whose construction ensures a specific enrichment of key members of the gut microbiota in the nursing infant, a consortium known as the milk-oriented microbiome. Milk glycoproteins are thought to function similarly, as specific growth substrates for bifidobacteria common to the breast-fed infant gut. Recently, a cell wall-associated endo-ß-N-acetylglucosaminidase (EndoBI-1) found in various infant-borne bifidobacteria was shown to remove a range of intact N-linked glycans. We hypothesized that these released oligosaccharide structures can serve as a sole source for the selective growth of bifidobacteria. We demonstrated that EndoBI-1 released N-glycans from concentrated bovine colostrum at the pilot scale. EndoBI-1-released N-glycans supported the rapid growth of Bifidobacterium longum subsp. infantis (B. infantis), a species that grows well on human milk oligosaccharides, but did not support growth of Bifidobacterium animalis subsp. lactis (B. lactis), a species which does not. Conversely, B. infantis ATCC 15697 did not grow on the deglycosylated milk protein fraction, clearly demonstrating that the glycan portion of milk glycoproteins provided the key substrate for growth. Mass spectrometry-based profiling revealed that B. infantis consumed 73% of neutral and 92% of sialylated N-glycans, while B. lactis degraded only 11% of neutral and virtually no (<1%) sialylated N-glycans. These results provide mechanistic support that N-linked glycoproteins from milk serve as selective substrates for the enrichment of infant-associated bifidobacteria capable of carrying out the initial deglycosylation. Moreover, released N-glycans were better growth substrates than the intact milk glycoproteins, suggesting that EndoBI-1 cleavage is a key initial step in consumption of glycoproteins. Finally, the variety of N-glycans released from bovine milk glycoproteins suggests that they may serve as novel prebiotic substrates with selective properties similar to those of human milk oligosaccharides. IMPORTANCE: It has been previously shown that glycoproteins serve as growth substrates for bifidobacteria. However, which part of a glycoprotein (glycans or polypeptides) is responsible for this function was not known. In this study, we used a novel enzyme to cleave conjugated N-glycans from milk glycoproteins and tested their consumption by various bifidobacteria. The results showed that the glycans selectively stimulated the growth of B. infantis, which is a key infant gut microbe. The selectivity of consumption of individual N-glycans was determined using advanced mass spectrometry (nano-liquid chromatography chip-quadrupole time of flight mass spectrometry [nano-LC-Chip-Q-TOF MS]) to reveal that B. infantis can consume the range of glycan structures released from whey protein concentrate.
[Mh] Termos MeSH primário: Bifidobacterium/enzimologia
Bifidobacterium/metabolismo
Glicoproteínas/metabolismo
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/metabolismo
Leite/metabolismo
Oligossacarídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Bifidobacterium/crescimento & desenvolvimento
Seres Humanos
Lactente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Oligosaccharides); EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160417
[St] Status:MEDLINE
[do] DOI:10.1128/AEM.00547-16


  10 / 1020 MEDLINE  
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[PMID]:27058295
[Au] Autor:Priyanka P; Fairbanks AJ
[Ad] Endereço:Department of Chemistry, University of Canterbury, Private Bag 4800, Christchurch 8140, New Zealand.
[Ti] Título:Synthesis of a hybrid type N-glycan heptasaccharide oxazoline for Endo M catalysed glycosylation.
[So] Source:Carbohydr Res;426:40-5, 2016 May 13.
[Is] ISSN:1873-426X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Endo-ß-N-acetylglucosaminidases (ENGases) are versatile biocatalysts that allow access to a wide variety of defined homogenous N-linked glycoconjugates in a convergent manner. A hybrid-type N-glycan was accessed by total synthesis, converted to an oxazoline, and used as a donor substrate with both wild type Endo M and an N175Q glycosynthase Endo M mutant allowing the convergent synthesis of a glycosylated amino acid bearing a hybrid N-glycan structure.
[Mh] Termos MeSH primário: Biocatálise
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/metabolismo
Oxazóis/química
Oxazóis/metabolismo
Polissacarídeos/biossíntese
Polissacarídeos/química
[Mh] Termos MeSH secundário: Configuração de Carboidratos
Glicosilação
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/química
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Oxazoles); 0 (Polysaccharides); EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161231
[Lr] Data última revisão:
161231
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160409
[St] Status:MEDLINE



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