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[PMID]:28460447
[Au] Autor:Dou X; Han J; Song W; Dong N; Xu X; Zhang W; Shan A
[Ad] Endereço:Institute of Animal Nutrition, Northeast Agricultural University, Harbin 150030, P.R. China.
[Ti] Título:Sodium butyrate improves porcine host defense peptide expression and relieves the inflammatory response upon Toll-like receptor 2 activation and histone deacetylase inhibition in porcine kidney cells.
[So] Source:Oncotarget;8(16):26532-26551, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Host defense peptides (HDPs) are an important component of the innate immune system and possess direct antimicrobial and immunomodulatory activities. Dietary regulation of HDPs synthesis has emerged as a novel non-antibiotic approach to combat pathogen infection. There are species- and tissue-dependent characteristics of the regulation and mechanism of HDPs. In this study, we investigated whether the histone deacetylase inhibitor (HDACi) sodium butyrate (NaB) could induce HDP expression and the mechanism underlying NaB-regulated HDP expression in PK-15 cells. Our results revealed that NaB augmented HDP expression in PK-15 cells, including porcine ß-defensin 3 (pBD3), epididymis protein 2 splicing variant C (pEP2C), pBD128, pBD123, and pBD115, but no inflammatory response occurred. Inhibition of HDAC activity was not sufficient to induce the expression of pBD3 and pEP2C in comparisons of NaB and another HDACi, trichostatin A (TSA). Concomitantly, NF-κB activation was involved in the induction of HDP expression by NaB. MAPK pathway inhibition also prevented pBD3 and pEP2C induction by NaB. Furthermore, NaB could still promote pBD3 and pEP2C expression and inhibit IL-6 production in the presence of the toll-like receptor 2 (TLR2) ligand peptidoglycan. Moreover, TLR2 could be activated by both NaB and peptidoglycan, and blocking TLR2 expression suppressed HDP induction. Finally, we further showed that increased pBD3 could decrease cytokine interleukin-18 (IL-18) and increase porcine claudin 15 (pCLDN15) contents, suggesting an immunoregulatory function of pBD3. In conclusion, this work paves the way for using HDACi-NaB to induce porcine kidney defense peptides while limiting the deleterious risk of an inflammatory response.
[Mh] Termos MeSH primário: Ácido Butírico/farmacologia
Defensinas/genética
Células Epiteliais/efeitos dos fármacos
Células Epiteliais/metabolismo
Regulação da Expressão Gênica/efeitos dos fármacos
Inibidores de Histona Desacetilases/farmacologia
Receptor 2 Toll-Like/metabolismo
[Mh] Termos MeSH secundário: Animais
Peptídeos Catiônicos Antimicrobianos/genética
Linhagem Celular
Células Cultivadas
Citocinas/genética
Citocinas/metabolismo
Mediadores da Inflamação
Rim
Ligantes
NF-kappa B/metabolismo
Transdução de Sinais/efeitos dos fármacos
Suínos
Receptor 2 Toll-Like/agonistas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Cytokines); 0 (Defensins); 0 (Histone Deacetylase Inhibitors); 0 (Inflammation Mediators); 0 (Ligands); 0 (NF-kappa B); 0 (Toll-Like Receptor 2); 107-92-6 (Butyric Acid)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15714


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[PMID]:28741756
[Au] Autor:Järvå M; Lay FT; Hulett MD; Kvansakul M
[Ad] Endereço:Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Vic, Australia.
[Ti] Título:Structure of the defensin NsD7 in complex with PIP reveals that defensin : lipid oligomer topologies are dependent on lipid type.
[So] Source:FEBS Lett;591(16):2482-2490, 2017 08.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Defensins are innate immune molecules that upon recognition of specific phospholipids can disrupt microbial membranes by forming oligomeric assemblies. Structures of two related plant defensins, NaD1 and NsD7, bound to phosphatidylinositol 4,5-bisphosphate (PIP ) and phosphatidic acid (PA), respectively, revealed striking differences in their oligomeric topologies. To understand how NsD7 binds different phospholipids and rationalize the different topologies, we determined the structure of an NsD7-PIP complex. This structure reveals fundamental differences in phospholipid binding compared to NsD7-PA, and an oligomeric topology nearly identical to the previously determined NaD1-PIP complex, establishing that the PIP fibril topology is conserved between NaD1 and NsD7. Our findings highlight the remarkable ability of defensins to bind different types of phospholipids to form oligomeric fibrils with diverse topologies.
[Mh] Termos MeSH primário: Defensinas/química
Defensinas/metabolismo
Fosfatos de Fosfatidilinositol/química
Fosfatos de Fosfatidilinositol/metabolismo
Multimerização Proteica
[Mh] Termos MeSH secundário: Membrana Celular/metabolismo
Seres Humanos
Modelos Moleculares
Ácidos Fosfatídicos/metabolismo
Ligação Proteica
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Defensins); 0 (Phosphatidic Acids); 0 (Phosphatidylinositol Phosphates); 0 (phosphatidylinositol 3,4-diphosphate)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12761


  3 / 1791 MEDLINE  
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[PMID]:28825809
[Au] Autor:Franzoi M; van Heuvel Y; Thomann S; Schürch N; Kallio PT; Venier P; Essig A
[Ad] Endereço:Department of Biology, University of Padova , Via Ugo Bassi 58/B, Padova 35131, Italy.
[Ti] Título:Structural Insights into the Mode of Action of the Peptide Antibiotic Copsin.
[So] Source:Biochemistry;56(37):4992-5001, 2017 Sep 19.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Defensins make up a class of cysteine-rich antimicrobial peptides, expressed by virtually all eukaryotes as part of their innate immune response. Because of their unique mode of action and rapid killing of pathogenic microbes, defensins are considered promising alternatives to clinically applied antibiotics. Copsin is a defensin-like peptide, previously identified in the mushroom Coprinopsis cinerea. It exerts its activity against a range of Gram-positive bacteria by binding to the peptidoglycan precursor lipid II and prevention of proper cell wall formation. In this study, we present a new workflow for the generation, production, and activity-driven selection of copsin derivatives, based on their expression in Pichia pastoris. One hundred fifty-two single-amino acid mutants and combinations thereof allowed the identification of k-copsin, a peptide variant exhibiting significantly enhanced activity against Bacillus subtilis and Staphylococcus aureus. Furthermore, we performed in silico characterizations of membrane interactions of copsin and k-copsin, in the presence and absence of lipid II. The molecular dynamics data highlighted a high variability in lipid II binding, with a preference for the MurNAc moiety with 47 and 35% of the total contacts for copsin and k-copsin, respectively. Mutated amino acids were located in loop regions of k-copsin and shown to be crucial in the perturbation of the bacterial membrane. These structural studies provide a better understanding of how defensins can be developed toward antibacterial therapies less prone to resistance issues.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Peptídeos Catiônicos Antimicrobianos/farmacologia
Bacillus subtilis/efeitos dos fármacos
Defensinas/farmacologia
Desenho de Drogas
Proteínas Fúngicas/farmacologia
Modelos Moleculares
Staphylococcus aureus/efeitos dos fármacos
Uridina Difosfato Ácido N-Acetilmurâmico/análogos & derivados
[Mh] Termos MeSH secundário: Agaricales/metabolismo
Substituição de Aminoácidos
Antibacterianos/química
Antibacterianos/metabolismo
Peptídeos Catiônicos Antimicrobianos/química
Peptídeos Catiônicos Antimicrobianos/genética
Peptídeos Catiônicos Antimicrobianos/metabolismo
Bacillus subtilis/crescimento & desenvolvimento
Sítios de Ligação
Parede Celular/efeitos dos fármacos
Parede Celular/metabolismo
Biologia Computacional
Defensinas/química
Defensinas/metabolismo
Sistemas Especialistas
Fermentação
Proteínas Fúngicas/química
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Testes de Sensibilidade Microbiana
Simulação de Dinâmica Molecular
Mutagênese Sítio-Dirigida
Mutação Puntual
Conformação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Proteínas Recombinantes/farmacologia
Staphylococcus aureus/crescimento & desenvolvimento
Relação Estrutura-Atividade
Uridina Difosfato Ácido N-Acetilmurâmico/química
Uridina Difosfato Ácido N-Acetilmurâmico/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antimicrobial Cationic Peptides); 0 (Defensins); 0 (Fungal Proteins); 0 (Recombinant Proteins); 0 (Uridine Diphosphate N-Acetylmuramic Acid); 0 (copsin protein, Coprinopsis cinerea); 0 (muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170822
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00697


  4 / 1791 MEDLINE  
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[PMID]:28729359
[Au] Autor:Prantner D; Shirey KA; Lai W; Lu W; Cole AM; Vogel SN; Garzino-Demo A
[Ad] Endereço:Department of Microbiology and Immunology, University of Maryland, School of Medicine, Baltimore, Maryland, USA.
[Ti] Título:The θ-defensin retrocyclin 101 inhibits TLR4- and TLR2-dependent signaling and protects mice against influenza infection.
[So] Source:J Leukoc Biol;102(4):1103-1113, 2017 Oct.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Despite widespread use of annual influenza vaccines, seasonal influenza-associated deaths number in the thousands each year, in part because of exacerbating bacterial superinfections. Therefore, discovering additional therapeutic options would be a valuable aid to public health. Recently, TLR4 inhibition has emerged as a possible mechanism for protection against influenza-associated lethality and acute lung injury. Based on recent data showing that rhesus macaque θ-defensins could inhibit TLR4-dependent gene expression, we tested the hypothesis that a novel θ-defensin, retrocyclin (RC)-101, could disrupt TLR4-dependent signaling and protect against viral infection. In this study, RC-101, a variant of the humanized θ-defensin RC-1, blocked TLR4-mediated gene expression in mouse and human macrophages in response to LPS, targeting both MyD88- and TRIF-dependent pathways. In a cell-free assay, RC-101 neutralized the biologic activity of LPS at doses ranging from 0.5 to 50 EU/ml, consistent with data showing that RC-101 binds biotinylated LPS. The action of RC-101 was not limited to the TLR4 pathway because RC-101 treatment of macrophages also inhibited gene expression in response to a TLR2 agonist, Pam3CSK4, but failed to bind that biotinylated agonist. Mouse macrophages infected in vitro with mouse-adapted A/PR/8/34 influenza A virus (PR8) also produced lower levels of proinflammatory cytokine gene products in a TLR4-independent fashion when treated with RC-101. Finally, RC-101 decreased both the lethality and clinical severity associated with PR8 infection in mice. Cumulatively, our data demonstrate that RC-101 exhibits therapeutic potential for the mitigation of influenza-related morbidity and mortality, potentially acting through TLR-dependent and TLR-independent mechanisms.
[Mh] Termos MeSH primário: Defensinas/imunologia
Vírus da Influenza A/imunologia
Infecções por Orthomyxoviridae/imunologia
Peptídeos/imunologia
Transdução de Sinais/imunologia
Receptor 2 Toll-Like/imunologia
Receptor 4 Toll-Like/imunologia
[Mh] Termos MeSH secundário: Animais
Defensinas/genética
Camundongos
Camundongos Knockout
Infecções por Orthomyxoviridae/genética
Peptídeos/genética
Transdução de Sinais/genética
Receptor 2 Toll-Like/genética
Receptor 4 Toll-Like/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Defensins); 0 (Peptides); 0 (RC 101); 0 (Tlr2 protein, mouse); 0 (Tlr4 protein, mouse); 0 (Toll-Like Receptor 2); 0 (Toll-Like Receptor 4); 0 (theta-defensin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.2A1215-567RR


  5 / 1791 MEDLINE  
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[PMID]:28715972
[Au] Autor:Holly MK; Diaz K; Smith JG
[Ad] Endereço:Department of Microbiology, University of Washington, Seattle, Washington 98195; email: jgsmith2@uw.edu.
[Ti] Título:Defensins in Viral Infection and Pathogenesis.
[So] Source:Annu Rev Virol;4(1):369-391, 2017 Sep 29.
[Is] ISSN:2327-0578
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:α, ß, and θ defensins are effectors of the innate immune system with potent antibacterial, antiviral, and antifungal activity. Defensins have direct antiviral activity in cell culture, with varied mechanisms for individual viruses, although some common themes have emerged. In addition, defensins have potent immunomodulatory activity that can alter innate and adaptive immune responses to viral infection. In some cases, there is evidence for paradoxical escape from defensin neutralization or enhancement of viral infection. The direct and indirect activities of defensins have led to their development as therapeutics and vaccine components. The major area of investigation that continues to lag is the connection between the effects of defensins in cell culture models and viral pathogenesis in vivo. Model systems to study defensin biology, including more physiologic models designed to bridge this gap, are also discussed.
[Mh] Termos MeSH primário: Defensinas/metabolismo
Viroses/imunologia
alfa-Defensinas/metabolismo
beta-Defensinas/metabolismo
[Mh] Termos MeSH secundário: Adenoviridae/efeitos dos fármacos
Adenoviridae/patogenicidade
Animais
Antivirais/farmacologia
Defensinas/genética
Defensinas/farmacologia
Defensinas/uso terapêutico
HIV/efeitos dos fármacos
HIV/patogenicidade
Herpesviridae/efeitos dos fármacos
Herpesviridae/patogenicidade
Seres Humanos
Imunidade Inata
Imunomodulação
Camundongos
Papillomaviridae/efeitos dos fármacos
Papillomaviridae/patogenicidade
Viroses/tratamento farmacológico
alfa-Defensinas/genética
alfa-Defensinas/farmacologia
alfa-Defensinas/uso terapêutico
beta-Defensinas/genética
beta-Defensinas/farmacologia
beta-Defensinas/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Defensins); 0 (alpha-Defensins); 0 (beta-Defensins); 0 (theta-defensin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-virology-101416-041734


  6 / 1791 MEDLINE  
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[PMID]:28709869
[Au] Autor:Sharmila GR; Venkateswaran G
[Ad] Endereço:Academy of Scientific and Innovative Research, CSIR-Central Food Technological Research Institute, Mysuru 570020, India; Microbiology and Fermentation Technology Department, CSIR-Central Food Technological Research Institute, Mysuru 570020, India.
[Ti] Título:Protective effect of bacillopeptidase CFR5 from Bacillus subtilis CFR5 on cerulein-induced pancreatitis.
[So] Source:Biochem Biophys Res Commun;491(2):455-462, 2017 Sep 16.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacillopeptidase is a serine peptidase, known for its fibrinolytic activity. However, a very little information is known about its in vivo inflammatory and/or anti-inflammatory properties. Thus, to understand whether bacillopeptidase incorporation can regulate pancreatitis or not, the cerulein-induced pancreatitis model was used, and the role of bacillopeptidase on pancreatitis was studied. In this study, 46 kDa protein was purified from Bacillus subtilis and identified as bacillopeptidase CFR5 (BPC) through MS/MS analysis. The nutritional prophylactic group was orally fed with two doses of BPC (100 µg/Kg/BW of rat) 6 h before cerulein administration and analyzed for its effect on intestine and pancreas inflammation, cytokines, and pancreatitis marker gene expression. BPC administration significantly reduced the severity of pancreatitis by decreasing serum amylase, lipase, pancreatic edema and myeloperoxidase activity. The pretreatment with BPC suppressed the pancreatic pro-inflammatory and inflammatory cytokines production including IL-6, IL-1ß, TNF-α, IL-2, IL-4, IL-5, IL-10, and IL-13 in both pancreas and serum samples. Moreover, BPC supplementation restored pancreatitis mediated disruption of intestinal barrier integrity by upregulating tight junction proteins (ZO-1, occludin), antimicrobial peptides (DEFB1, CRAMP), MUC-2, TFF3 expression and by enhancing SCFA's production. Pretreatment with BPC suppressed the intestinal inflammation with reduced cytokines production in the colon and ileal region of cerulein-induced pancreatitis. Thus, BPC based pretreatment protocol is a novel intervention to prevent acute pancreatitis.
[Mh] Termos MeSH primário: Anti-Inflamatórios não Esteroides/farmacologia
Bacillus subtilis/química
Proteínas de Bactérias/farmacologia
Edema/tratamento farmacológico
Pancreatite/tratamento farmacológico
Serina Endopeptidases/farmacologia
[Mh] Termos MeSH secundário: Administração Oral
Animais
Anti-Inflamatórios não Esteroides/isolamento & purificação
Proteínas de Bactérias/isolamento & purificação
Catelicidinas/genética
Catelicidinas/metabolismo
Ceruletídeo
Citocinas/biossíntese
Defensinas/genética
Defensinas/metabolismo
Edema/induzido quimicamente
Edema/genética
Edema/patologia
Regulação da Expressão Gênica
Masculino
Mucina-2/genética
Mucina-2/metabolismo
Ocludina/genética
Ocludina/metabolismo
Pâncreas/efeitos dos fármacos
Pâncreas/metabolismo
Pâncreas/patologia
Pancreatite/induzido quimicamente
Pancreatite/genética
Pancreatite/patologia
Ratos
Ratos Wistar
Serina Endopeptidases/isolamento & purificação
Fator Trefoil-3/genética
Fator Trefoil-3/metabolismo
Proteína da Zônula de Oclusão-1/genética
Proteína da Zônula de Oclusão-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (Bacterial Proteins); 0 (Cathelicidins); 0 (Cytokines); 0 (Defb1 protein, rat); 0 (Defensins); 0 (Muc2 protein, rat); 0 (Mucin-2); 0 (Occludin); 0 (Ocln protein, rat); 0 (TFF3 protein, rat); 0 (Tjp1 protein, rat); 0 (Trefoil Factor-3); 0 (Zonula Occludens-1 Protein); 0 (cathelicidin antimicrobial peptide); 888Y08971B (Ceruletide); EC 3.4.21.- (Serine Endopeptidases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE


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[PMID]:28642103
[Au] Autor:Mathew B; Olli S; Guru A; Nagaraj R
[Ad] Endereço:CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India. Electronic address: basil011986@gmail.com.
[Ti] Título:Chimeric analogs of human ß-defensin 1 and θ-defensin disrupt pre-established bacterial biofilms.
[So] Source:Bioorg Med Chem Lett;27(15):3264-3266, 2017 08 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Antibiofilm activity of several human defensin analogs that have the ability to kill planktonic bacteria, against pre-established biofilms of Escherichia coli MG1655 and Staphylococcus aureus NCTC 8530 were examined. Linear and linear fatty acylated analogs did not show any activity while disulfide constrained analogs disrupted pre-established S. aureus biofilms. Chimeric analogs of human ß-defensin 1 and θ-defensin, hBTD-1 and [d]hBTD-1 were highly active against S. aureus biofilms. Among the analogs tested, only the d-enantiomer [d]hBTD-1 showed activity against E. coli biofilm. Our study provides insights into the structural requirements for the eradication of pre-established biofilms in defensin analogs.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Biofilmes/efeitos dos fármacos
Defensinas/farmacologia
Escherichia coli/efeitos dos fármacos
Staphylococcus aureus/efeitos dos fármacos
beta-Defensinas/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Antibacterianos/química
Defensinas/química
Escherichia coli/fisiologia
Infecções por Escherichia coli/microbiologia
Infecções por Escherichia coli/prevenção & controle
Seres Humanos
Infecções Estafilocócicas/microbiologia
Infecções Estafilocócicas/prevenção & controle
Staphylococcus aureus/fisiologia
beta-Defensinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (DEFB1 protein, human); 0 (Defensins); 0 (beta-Defensins); 0 (theta-defensin)
[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:170624
[St] Status:MEDLINE


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[PMID]:28624494
[Au] Autor:Guillén-Chable F; Arenas-Sosa I; Islas-Flores I; Corzo G; Martinez-Liu C; Estrada G
[Ad] Endereço:Unidad de Bioquímica y Biología Molecular de Plantas. Centro de Investigación Científica de Yucatán A.C., Calle 43 No. 130, Col. Chuburná de Hidalgo, Mérida, Yucatán 97205, México.
[Ti] Título:Antibacterial activity and phospholipid recognition of the recombinant defensin J1-1 from Capsicum genus.
[So] Source:Protein Expr Purif;136:45-51, 2017 Aug.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The gene of the four disulfide-bridged defensin J1-1 from Capsicum was cloned into the expression vector pQE30 containing a 6His-tag as fusion protein. This construct was transfected into Origami strain of Escherichia coli and expressed after induction with isopropyl thiogalactoside (IPTG). The level of expression was 4 mg/L of culture medium, and the His-tagged recombinant defensin (HisXarJ1-1) was expressed exclusively into inclusion bodies. After solubilization, HisXarJ1-1 was purified by affinity and hydrophobic interaction chromatography. The reverse-phase HPLC profile of the HisXarJ1-1 product obtained from the affinity chromatography step showed single main peptide fraction of molecular masses of 7050.6 Da and after treatment with DTT a single fraction of 7, 042.6 Da corresponding to the reduced peptide was observed. An in vitro folding step of the HisXarJ1-1 generated a distinct profile of oxidized forms of the peptide this oxidized peptide was capable of binding phosphatidic acid in vitro. Possible dimer and oligomer of HisXarJ1-1 were visible in gel electrophoresis and immunodetected with anti-His antibodies. Pure recombinant defensin HisXarJ1-1 exhibited antibacterial activity against Pseudomonas aeruginosa.
[Mh] Termos MeSH primário: Antibacterianos
Capsicum/genética
Defensinas
Proteínas de Plantas
Pseudomonas aeruginosa/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Antibacterianos/biossíntese
Antibacterianos/isolamento & purificação
Antibacterianos/farmacologia
Capsicum/metabolismo
Defensinas/biossíntese
Defensinas/genética
Defensinas/isolamento & purificação
Defensinas/farmacologia
Escherichia coli/genética
Escherichia coli/metabolismo
Corpos de Inclusão/química
Corpos de Inclusão/genética
Corpos de Inclusão/metabolismo
Proteínas de Plantas/biossíntese
Proteínas de Plantas/genética
Proteínas de Plantas/isolamento & purificação
Proteínas de Plantas/farmacologia
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Defensins); 0 (Plant Proteins); 0 (Recombinant Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170619
[St] Status:MEDLINE


  9 / 1791 MEDLINE  
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[PMID]:28593905
[Au] Autor:Kudryashova E; Seveau SM; Kudryashov DS
[Ti] Título:Targeting and inactivation of bacterial toxins by human defensins.
[So] Source:Biol Chem;398(10):1069-1085, 2017 Sep 26.
[Is] ISSN:1437-4315
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Defensins, as a prominent family of antimicrobial peptides (AMP), are major effectors of the innate immunity with a broad range of immune modulatory and antimicrobial activities. In particular, defensins are the only recognized fast-response molecules that can neutralize a broad range of bacterial toxins, many of which are among the deadliest compounds on the planet. For a decade, the mystery of how a small and structurally conserved group of peptides can neutralize a heterogeneous group of toxins with little to no sequential and structural similarity remained unresolved. Recently, it was found that defensins recognize and target structural plasticity/thermodynamic instability, fundamental physicochemical properties that unite many bacterial toxins and distinguish them from the majority of host proteins. Binding of human defensins promotes local unfolding of the affected toxins, destabilizes their secondary and tertiary structures, increases susceptibility to proteolysis, and leads to their precipitation. While the details of toxin destabilization by defensins remain obscure, here we briefly review properties and activities of bacterial toxins known to be affected by or resilient to defensins, and discuss how recognized features of defensins correlate with the observed inactivation.
[Mh] Termos MeSH primário: Toxinas Bacterianas/imunologia
Defensinas/imunologia
[Mh] Termos MeSH secundário: Toxinas Bacterianas/química
Defensinas/química
Seres Humanos
Conformação Proteica
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Toxins); 0 (Defensins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE


  10 / 1791 MEDLINE  
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[PMID]:28528214
[Au] Autor:Khairutdinov BI; Ermakova EA; Yusypovych YM; Bessolicina EK; Tarasova NB; Toporkova YY; Kovaleva V; Zuev YF; Nesmelova IV
[Ad] Endereço:Kazan Institute of Biochemistry and Biophysics, Lobachevsky St. 2/31, Kazan 420111, Russia; Kazan Federal University, Kremlyovskaya Str. 18, Kazan 420008, Russia.
[Ti] Título:NMR structure, conformational dynamics, and biological activity of PsDef1 defensin from Pinus sylvestris.
[So] Source:Biochim Biophys Acta;1865(8):1085-1094, 2017 08.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Plants have developed a complex defense response system against pests and pathogens. Defensins, produced by plants as part of their innate immune response, form the family of small, basic, cysteine-rich proteins with activity primarily directed against fungal pathogens. In addition, plant defensins can show antibacterial activity and protease and insect amylase inhibitory activities. However, in gymnosperms, only antifungal activity of defensins has been described thus far. Here, we report antibacterial and insect α-amylase inhibition activities for defensin PsDef1 from P. sylvestris, the first defensin from gymnosperms with a broad range of biological activities described. We also report the solution NMR structure of PsDef1 and its dynamics properties assessed by a combination of experimental NMR and computational techniques. Collectively, our data provide an insight into structure, dynamics, and functional properties of PsDef1 that could be common between defensins from this taxonomic group.
[Mh] Termos MeSH primário: Defensinas/química
Defensinas/farmacologia
Pinus sylvestris/metabolismo
Proteínas de Plantas/química
Proteínas de Plantas/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Antibacterianos/química
Antibacterianos/farmacologia
Antifúngicos/química
Antifúngicos/farmacologia
Espectroscopia de Ressonância Magnética/métodos
Modelos Moleculares
Alinhamento de Sequência
alfa-Amilases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antifungal Agents); 0 (Defensins); 0 (Plant Proteins); EC 3.2.1.1 (alpha-Amylases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170522
[St] Status:MEDLINE



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