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  1 / 23898 MEDLINE  
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[PMID]:29328338
[Au] Autor:Soler MA; Fortuna S; de Marco A; Laio A
[Ad] Endereço:SISSA, Via Bonomea 265, I-34136 Trieste, Italy. miguelangel.solerbastida@sissa.it fortuna@sissa.it.
[Ti] Título:Binding affinity prediction of nanobody-protein complexes by scoring of molecular dynamics trajectories.
[So] Source:Phys Chem Chem Phys;20(5):3438-3444, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nanobodies offer a viable alternative to antibodies for engineering high affinity binders. Their small size has an additional advantage: it allows exploiting computational protocols for optimizing their biophysical features, such as the binding affinity. The efficient prediction of this quantity is still considered a daunting task especially for modelled complexes. We show how molecular dynamics can successfully assist in the binding affinity prediction of modelled nanobody-protein complexes. The approximate initial configurations obtained by in silico design must undergo large rearrangements before achieving a stable conformation, in which the binding affinity can be meaningfully estimated. The scoring functions developed for the affinity evaluation of crystal structures will provide accurate estimates for modelled binding complexes if the scores are averaged over long finite temperature molecular dynamics simulations.
[Mh] Termos MeSH primário: Complexo Antígeno-Anticorpo/química
Simulação de Dinâmica Molecular
Proteínas/imunologia
Anticorpos de Cadeia Única/imunologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Afinidade de Anticorpos
Complexo Antígeno-Anticorpo/metabolismo
Seres Humanos
Muramidase/química
Muramidase/imunologia
Estrutura Terciária de Proteína
Proteínas/química
Receptor ErbB-2/química
Receptor ErbB-2/metabolismo
Alinhamento de Sequência
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (Proteins); 0 (Single-Chain Antibodies); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2); EC 3.2.1.17 (Muramidase)
[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:10.1039/c7cp08116b


  2 / 23898 MEDLINE  
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[PMID]:29324815
[Au] Autor:Yerabham ASK; Müller-Schiffmann A; Ziehm T; Stadler A; Köber S; Indurkhya X; Marreiros R; Trossbach SV; Bradshaw NJ; Prikulis I; Willbold D; Weiergräber OH; Korth C
[Ad] Endereço:Department of Neuropathology, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
[Ti] Título:Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein.
[So] Source:PLoS One;13(1):e0191162, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accumulating evidence suggests an important role for the Disrupted-in-Schizophrenia 1 (DISC1) protein in neurodevelopment and chronic mental illness. In particular, the C-terminal 300 amino acids of DISC1 have been found to mediate important protein-protein interactions and to harbor functionally important phosphorylation sites and disease-associated polymorphisms. However, long disordered regions and oligomer-forming subdomains have so far impeded structural analysis. VHH domains derived from camelid heavy chain only antibodies are minimal antigen binding modules with appreciable solubility and stability, which makes them well suited for the stabilizing proteins prior to structural investigation. Here, we report on the generation of a VHH domain derived from an immunized Lama glama, displaying high affinity for the human DISC1 C region (aa 691-836), and its characterization by surface plasmon resonance, size exclusion chromatography and immunological techniques. The VHH-DISC1 (C region) complex was also used for structural investigation by small angle X-ray scattering analysis. In combination with molecular modeling, these data support predictions regarding the three-dimensional fold of this DISC1 segment as well as its steric arrangement in complex with our VHH antibody.
[Mh] Termos MeSH primário: Camelídeos Americanos/imunologia
Proteínas do Tecido Nervoso/imunologia
Anticorpos de Cadeia Única/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Complexo Antígeno-Anticorpo/química
Complexo Antígeno-Anticorpo/genética
Reações Antígeno-Anticorpo
Fenômenos Biofísicos
Camelídeos Americanos/genética
Mapeamento de Epitopos
Feminino
Seres Humanos
Cadeias Pesadas de Imunoglobulinas/química
Cadeias Pesadas de Imunoglobulinas/genética
Camundongos
Modelos Moleculares
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/genética
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/imunologia
Domínios e Motivos de Interação entre Proteínas
Espalhamento a Baixo Ângulo
Anticorpos de Cadeia Única/genética
Ressonância de Plasmônio de Superfície
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (DISC1 protein, human); 0 (Disc1 protein, mouse); 0 (Immunoglobulin Heavy Chains); 0 (Nerve Tissue Proteins); 0 (Peptide Fragments); 0 (Single-Chain Antibodies)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191162


  3 / 23898 MEDLINE  
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[PMID]:29236386
[Au] Autor:Galkin OY; Besarab AB; Lutsenko TN
[Ti] Título:Characteristics of enzyme-linked immunosorbent assay for detection of IgG antibodies specific to Сhlamydia trachomatis heat shock protein (HSP-60)
[So] Source:Ukr Biochem J;89(1):22-30, 2017 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:The goal of this work was to study sensitivity and specificity of the developed ELISA set for the identification of IgG antibodies against Chlamydia trachomatis HSP-60 (using biotinylated tyramine-based signal amplification system). The study was conducted using a panel of characterized sera, as well as two reference ELISA sets of similar purpose. According to the results of ELISA informative value parameters, the ELISA we have developed showed the highest specificity and sensitivity parameters (no false negative or false positive results were registered). In 4 out of 15 intralaboratory panel serum samples initially identified as negative, anti-HSP-60 IgG-antibodies test result in reference ELISA sets upon dilution changed from negative to positive. The nature of titration curves of false negative sera and commercial monoclonal antibodies А57-В9 against C. trachomatis HSP-60 after incubation for 24 h was indicative of the presence of anti-idiotypic antibodies in these samples. Upon sera dilution, idiotypic-anti-idiotypic complexes dissociated, which caused the change of test result. High informative value of the developed ELISA set for identification of IgG antibodies against C. trachomatis HSP-60 has been proven. Anti-idiotypic antibodies possessing C. trachomatis anti-HSP-60 activity and being one of the causes of false negative results of the relevant ELISA-based tests have been identified in blood sera of individuals infected with chlamydial genitourinary infection agents.
[Mh] Termos MeSH primário: Anticorpos Antibacterianos/análise
Antígenos de Bactérias/sangue
Chaperonina 60/sangue
Infecções por Chlamydia/diagnóstico
Chlamydia trachomatis/imunologia
Ensaio de Imunoadsorção Enzimática/métodos
Imunoglobulina G/análise
[Mh] Termos MeSH secundário: Anticorpos Anti-Idiotípicos/química
Anticorpos Antibacterianos/sangue
Anticorpos Antibacterianos/imunologia
Complexo Antígeno-Anticorpo/química
Antígenos de Bactérias/imunologia
Biotinilação
Chaperonina 60/imunologia
Infecções por Chlamydia/sangue
Infecções por Chlamydia/imunologia
Infecções por Chlamydia/microbiologia
Chlamydia trachomatis/química
Ensaio de Imunoadsorção Enzimática/normas
Reações Falso-Negativas
Seres Humanos
Soros Imunes/química
Imunoglobulina G/sangue
Imunoglobulina G/imunologia
Sensibilidade e Especificidade
Tiramina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Anti-Idiotypic); 0 (Antibodies, Bacterial); 0 (Antigen-Antibody Complex); 0 (Antigens, Bacterial); 0 (Chaperonin 60); 0 (Immune Sera); 0 (Immunoglobulin G); X8ZC7V0OX3 (Tyramine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj89.01.022


  4 / 23898 MEDLINE  
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[PMID]:29190714
[Au] Autor:Pillebout E; Jamin A; Ayari H; Housset P; Pierre M; Sauvaget V; Viglietti D; Deschenes G; Monteiro RC; Berthelot L; HSPrognosis group
[Ad] Endereço:INSERM 1149, Center of Research on Inflammation (CRI), Paris, France.
[Ti] Título:Biomarkers of IgA vasculitis nephritis in children.
[So] Source:PLoS One;12(11):e0188718, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Henoch-Schönlein purpura is a systemic vasculitis characterized by IgA deposits, which target the skin, joints, and kidneys, among other organs. In children, prognosis is often good but little is known about biomarkers of pediatric nephritis. We hypothesized that biological markers, including cytokines, immunoglobulins, IgA-immune complexes, IgA glycosylation and neutrophil gelatinase-associated lipocalin (NGAL), may discriminate IgA vasculitis (IgAV) pediatric patients with renal involvement from those without renal involvement. Fifty children at the time of IgAV rash between 2010 and 2015 were prospectively enrolled and compared to 21 controls. All patients were assessed for clinical and biological parameters at the time of diagnosis, including the levels of cytokines, immunoglobulins, immune complexes, IgA glycosylation and NGAL in serum and urine. Among IgAV patients, 33 patients exhibited nephritis (IgAV-N) and 17 children were without nephritis (IgAV-woN). The serum level of galactose-deficient (Gd)-IgA1 (p<0.01) and the urinary concentrations of IgA, IgG, IgM, IL-6, IL-8, IL-10, IgA-IgG complexes and IgA-sCD89 complexes (p<0.001 for all) were higher in the IgAV-N patients than in the IgAV-woN patients. Among those markers, urinary IgA and IgM had the highest AUC (0.86 and 0.87 respectively, p<0.0001). This prospective cohort study furthers our understanding of the pathophysiology of IgAV. We identified biomarkers that are able to distinguish patients initially with or without nephritis. To conclude, serum Gd-IgA1 and urinary IgA, IgG, IgM, IL-6, IL-8, IL-10, and IgA-IgG and IgA-sCD89 complexes could identify IgAV pediatric patients with renal involvement at the time of diagnosis.
[Mh] Termos MeSH primário: Biomarcadores/sangue
Imunoglobulina A/sangue
Púrpura de Schoenlein-Henoch/sangue
[Mh] Termos MeSH secundário: Complexo Antígeno-Anticorpo/sangue
Criança
Citocinas/urina
Ensaio de Imunoadsorção Enzimática
Feminino
Glicosilação
Seres Humanos
Imunoglobulina A/imunologia
Masculino
Estudos Prospectivos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (Biomarkers); 0 (Cytokines); 0 (Immunoglobulin A)
[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.0188718


  5 / 23898 MEDLINE  
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[PMID]:28468888
[Au] Autor:Leemans A; De Schryver M; Van der Gucht W; Heykers A; Pintelon I; Hotard AL; Moore ML; Melero JA; McLellan JS; Graham BS; Broadbent L; Power UF; Caljon G; Cos P; Maes L; Delputte P
[Ad] Endereço:Laboratory of Microbiology, Parasitology and Hygiene, University of Antwerp, Antwerp, Belgium.
[Ti] Título:Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein.
[So] Source:J Virol;91(14), 2017 Jul 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Respiratory syncytial virus (RSV) infections remain a major cause of respiratory disease and hospitalizations among infants. Infection recurs frequently and establishes a weak and short-lived immunity. To date, RSV immunoprophylaxis and vaccine research is mainly focused on the RSV fusion (F) protein, but a vaccine remains elusive. The RSV F protein is a highly conserved surface glycoprotein and is the main target of neutralizing antibodies induced by natural infection. Here, we analyzed an internalization process of antigen-antibody complexes after binding of RSV-specific antibodies to RSV antigens expressed on the surface of infected cells. The RSV F protein and attachment (G) protein were found to be internalized in both infected and transfected cells after the addition of either RSV-specific polyclonal antibodies (PAbs) or RSV glycoprotein-specific monoclonal antibodies (MAbs), as determined by indirect immunofluorescence staining and flow-cytometric analysis. Internalization experiments with different cell lines, well-differentiated primary bronchial epithelial cells (WD-PBECs), and RSV isolates suggest that antibody internalization can be considered a general feature of RSV. More specifically for RSV F, the mechanism of internalization was shown to be clathrin dependent. All RSV F-targeted MAbs tested, regardless of their epitopes, induced internalization of RSV F. No differences could be observed between the different MAbs, indicating that RSV F internalization was epitope independent. Since this process can be either antiviral, by affecting virus assembly and production, or beneficial for the virus, by limiting the efficacy of antibodies and effector mechanism, further research is required to determine the extent to which this occurs and how this might impact RSV replication. Current research into the development of new immunoprophylaxis and vaccines is mainly focused on the RSV F protein since, among others, RSV F-specific antibodies are able to protect infants from severe disease, if administered prophylactically. However, antibody responses established after natural RSV infections are poorly protective against reinfection, and high levels of antibodies do not always correlate with protection. Therefore, RSV might be capable of interfering, at least partially, with antibody-induced neutralization. In this study, a process through which surface-expressed RSV F proteins are internalized after interaction with RSV-specific antibodies is described. One the one hand, this antigen-antibody complex internalization could result in an antiviral effect, since it may interfere with virus particle formation and virus production. On the other hand, this mechanism may also reduce the efficacy of antibody-mediated effector mechanisms toward infected cells.
[Mh] Termos MeSH primário: Anticorpos Antivirais/metabolismo
Endocitose
Vírus Sincicial Respiratório Humano/imunologia
Proteínas Virais de Fusão/metabolismo
[Mh] Termos MeSH secundário: Complexo Antígeno-Anticorpo/metabolismo
Células Cultivadas
Citometria de Fluxo
Técnica Indireta de Fluorescência para Anticorpo
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Antigen-Antibody Complex); 0 (Viral Fusion Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


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[PMID]:28471362
[Au] Autor:Teplyakov A; Obmolova G; Malia TJ; Gilliland GL
[Ad] Endereço:Janssen Research and Development LLC, 1400 McKean Road, Spring House, PA 19477, USA.
[Ti] Título:Crystal structure of CD27 in complex with a neutralizing noncompeting antibody.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 5):294-299, 2017 May 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CD27 is a T-cell and B-cell co-stimulatory glycoprotein of the tumor necrosis factor (TNF) receptor superfamily that is dependent on the availability of the TNF-like ligand CD70. Therapeutic approaches to treating autoimmune diseases and cancers with antagonistic and agonistic anti-CD27 monoclonal antibodies (mAbs), respectively, have recently been developed. Mouse anti-human CD27 mAb 2177 shows potency in neutralizing CD70-induced signaling; however, it does not block the binding of soluble CD70. To provide insight into the mechanism of action of the mAb, the crystal structure of the CD27 extracellular domain in complex with the Fab fragment of mAb 2177 was determined at 1.8 Šresolution. CD27 exhibits the assembly of cysteine-rich domains characteristic of the TNF receptor superfamily. The structure reveals a unique binding site of mAb 2177 at the edge of the receptor molecule, which allows the mAb to sterically block the cell-bound form of CD70 from reaching CD27 while leaving the ligand epitope clear. This mode of action suggests a potential dual use of mAb 2177 either as an antagonist or as an agonist.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/química
Anticorpos Neutralizantes/química
Complexo Antígeno-Anticorpo/química
Ligante CD27/química
Fragmentos Fab das Imunoglobulinas/química
Membro 7 da Superfamília de Receptores de Fatores de Necrose Tumoral/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Anticorpos Monoclonais/genética
Anticorpos Neutralizantes/genética
Complexo Antígeno-Anticorpo/genética
Baculoviridae/genética
Baculoviridae/metabolismo
Sítios de Ligação
Ligante CD27/genética
Ligante CD27/imunologia
Clonagem Molecular
Cristalografia por Raios X
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Células HEK293
Seres Humanos
Fragmentos Fab das Imunoglobulinas/genética
Ligantes
Camundongos
Modelos Moleculares
Ligação Proteica
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/imunologia
Alinhamento de Sequência
Células Sf9
Spodoptera
Membro 7 da Superfamília de Receptores de Fatores de Necrose Tumoral/genética
Membro 7 da Superfamília de Receptores de Fatores de Necrose Tumoral/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antibodies, Neutralizing); 0 (Antigen-Antibody Complex); 0 (CD27 Ligand); 0 (CD70 protein, human); 0 (Immunoglobulin Fab Fragments); 0 (Ligands); 0 (Recombinant Fusion Proteins); 0 (Tumor Necrosis Factor Receptor Superfamily, Member 7)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17005957


  7 / 23898 MEDLINE  
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[PMID]:28846748
[Au] Autor:Berggren O; Hagberg N; Alexsson A; Weber G; Rönnblom L; Eloranta ML
[Ad] Endereço:Department of Medical Sciences, Rheumatology, Science for Life Laboratory, Uppsala University, Uppsala, Sweden.
[Ti] Título:Plasmacytoid dendritic cells and RNA-containing immune complexes drive expansion of peripheral B cell subsets with an SLE-like phenotype.
[So] Source:PLoS One;12(8):e0183946, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hyperactive B cells and a continuous interferon (IFN)-α production by plasmacytoid dendritic cells (pDCs) play a key role in systemic lupus erythematosus (SLE). We asked whether the interaction between B cells and pDCs stimulated with RNA-containing immune complexes affects peripheral B cell subsets. METHODS: B cells and pDCs were isolated from blood of healthy individuals and stimulated with immune complexes consisting of SLE-IgG and U1snRNP (RNA-IC). Expression of cell surface molecules as well as IL-6 and IL-10 production were determined by flow cytometry and immunoassays. Gene expression profiles were determined by a NanoString nCounter expression array. RESULTS: We found a remarkable increase of double negative CD27-IgD- B cells, from 7% within fresh CD19+ B cells to 37% in the RNA-IC-stimulated co-cultures of B cells and pDCs, comparable to the frequency of double negative B cells in SLE patients. Gene expression analysis of the double negative CD27-IgD- and the CD27+IgD- memory B cells revealed that twenty-one genes were differentially expressed between the two B cell subsets (≥ 2-fold, p<0.001). The, IL21R, IL4R, CCL4, CCL3, CD83 and the IKAROS Family Zinc Finger 2 (IKZ2) showed higher expression in the double negative CD27-IgD- B cells. CONCLUSION: The interactions between B cells and pDCs together with RNA-containing IC led to an expansion of B cells with similar phenotype as seen in SLE, suggesting that the pDC-B cell crosstalk contributes to the autoimmune feed-forward loop in SLE.
[Mh] Termos MeSH primário: Complexo Antígeno-Anticorpo/imunologia
Linfócitos B/imunologia
Células Dendríticas/imunologia
Lúpus Eritematoso Sistêmico/imunologia
RNA/imunologia
[Mh] Termos MeSH secundário: Antígenos CD/imunologia
Subpopulações de Linfócitos B
Linfócitos B/metabolismo
Técnicas de Cocultura
Perfilação da Expressão Gênica
Células HeLa
Seres Humanos
Memória Imunológica
Interleucina-10/biossíntese
Interleucina-6/biossíntese
Fenótipo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (Antigens, CD); 0 (Interleukin-6); 130068-27-8 (Interleukin-10); 63231-63-0 (RNA)
[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:170829
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183946


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[PMID]:28820895
[Au] Autor:Jamal F; Shivam P; Kumari S; Singh MK; Sardar AH; Pushpanjali; Murugesan S; Narayan S; Gupta AK; Pandey K; Das VNR; Ali V; Bimal S; Das P; Singh SK
[Ad] Endereço:Department of Microbiology, Rajendra Memorial Research Institute of Medical Sciences, Patna, India.
[Ti] Título:Identification of Leishmania donovani antigen in circulating immune complexes of visceral leishmaniasis subjects for diagnosis.
[So] Source:PLoS One;12(8):e0182474, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The unreliability of most of the existing antibody-based diagnostic kits to discriminate between active and treated VL cases, relapse situation and reinfection are a major hurdle in controlling the cases of Kala-azar in an endemic area. An antigen targeted diagnostic approaches can be an attractive strategy to overcome these problems. Hence, this study was focused on identifying the Leishmania antigens, lies in circulating immune complex (CICs), can be used for diagnostic as well as prognostic purposes. The present study was conducted on peripheral blood samples of 115 human subjects, based on isolation of CICs. The SDS-PAGE patterns showed an up-regulated expression of 55 kDa and 23 kDa fractions in an antigens obtained from CICs of all clinical and parasitologically proven untreated visceral leishmaniasis patients before treatment (VL-BT), which ensured absolute sensitivity. However, light expressions of these bands were observed in some VL treated cases. To ascertain the prognostic value, 2D expression profiles of circulating antigens were carried out, which revealed 3 upregulated and 12 induced immunoreactive spots. Out of these, ten prominent spots were excised and subjected for enzymatic digestion to generate peptides. Mass spectrometry (MS) analysis successfully explored 20 peptides derived from kinase, kinesin, acetyl Co-A carboxylase, dynein heavy chains (cytoplasmic and axonemal/flagellar), 60S ribosomal protein, nucleoporin protein, RNA polymeraseII, protease gp63, tubulin, DNA polymerase epsilon subunit, GTP-binding protein and tyrosyl-methionyl t-RNA synthetase-like protein and 19 hypothetical protein of unknown function. Presence of L. donovani proteins in circulating antigens were further validated using anti-Ld actin and anti-α tubulin antibody. Besides, MS derived peptides confirmed its reactivity with patients' sera. Therefore, these shortlisted potential antigens can be explored as antigen-based diagnostic as well as prognostic kit.
[Mh] Termos MeSH primário: Complexo Antígeno-Anticorpo/sangue
Antígenos de Protozoários/imunologia
Leishmania donovani/imunologia
Leishmaniose Visceral/sangue
[Mh] Termos MeSH secundário: Western Blotting
Cromatografia Líquida de Alta Pressão
Eletroforese em Gel de Poliacrilamida
Ensaio de Imunoadsorção Enzimática
Seres Humanos
Leishmaniose Visceral/imunologia
Espectrometria de Massas por Ionização por Electrospray
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (Antigens, Protozoan)
[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:170819
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182474


  9 / 23898 MEDLINE  
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[PMID]:28814603
[Au] Autor:Brandsma AM; Ten Broeke T; van Dueren den Hollander E; Caniels TG; Kardol-Hoefnagel T; Kuball J; Leusen JHW
[Ad] Endereço:Laboratory of Translational Immunology, University Medical Center Utrecht, 3584 CX Utrecht, the Netherlands.
[Ti] Título:Single Nucleotide Polymorphisms of the High Affinity IgG Receptor FcγRI Reduce Immune Complex Binding and Downstream Effector Functions.
[So] Source:J Immunol;199(7):2432-2439, 2017 Oct 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Binding of IgG Abs to FcγRs on immune cells induces FcγR cross-linking that leads to cellular effector functions, such as phagocytosis, Ab-dependent cellular cytotoxicity, and cytokine release. However, polymorphisms in low affinity FcγRs have been associated with altered avidity toward IgG, thereby substantially impacting clinical outcomes of multimodular therapy when targeting cancer or autoimmune diseases with mAbs as well as the frequency and severity of autoimmune diseases. In this context, we investigated the consequences of three nonsynonymous single nucleotide polymorphisms (SNPs) for the high affinity receptor for IgG, FcγRI. Only SNP V39I, located in the extracellular domain of FcγRI, reduces immune-complex binding of FcγRI whereas monomeric IgG binding is unaffected. This leads to reduced FcγRI effector functions, including Fc receptor γ-chain signaling and intracellular calcium mobilization. SNPs I301M and I338T, located in the transmembrane or intracellular domain, respectively, have no influence on monomeric IgG or immune complex binding, but FcRγ signaling is decreased for both SNPs, especially for I338T. We also found that the frequency of these SNPs in a cohort of healthy Dutch individuals is very low within the population. To our knowledge, this study addresses for the first time the biological consequences of SNPs in the high affinity FcγR, and reveals reduction in several FcγRI functions, which have the potential to alter efficacy of therapeutic Abs.
[Mh] Termos MeSH primário: Complexo Antígeno-Anticorpo/metabolismo
Imunoglobulina G/metabolismo
Polimorfismo de Nucleotídeo Único
Receptores de IgG/genética
[Mh] Termos MeSH secundário: Animais
Genótipo
Seres Humanos
Imunoglobulina G/genética
Camundongos
Fagocitose
Ligação Proteica
Receptores de IgG/deficiência
Receptores de IgG/imunologia
Receptores de IgG/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (FCGR1A protein, human); 0 (Fcgr1 protein, mouse); 0 (Immunoglobulin G); 0 (Receptors, IgG)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170818
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601929


  10 / 23898 MEDLINE  
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[PMID]:28739878
[Au] Autor:Banda NK; Acharya S; Scheinman RI; Mehta G; Takahashi M; Endo Y; Zhou W; Farrar CA; Sacks SH; Fujita T; Sekine H; Holers VM
[Ad] Endereço:Division of Rheumatology, Department of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045; nirmal.banda@ucdenver.edu.
[Ti] Título:Deconstructing the Lectin Pathway in the Pathogenesis of Experimental Inflammatory Arthritis: Essential Role of the Lectin Ficolin B and Mannose-Binding Protein-Associated Serine Protease 2.
[So] Source:J Immunol;199(5):1835-1845, 2017 Sep 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Complement plays an important role in the pathogenesis of rheumatoid arthritis. Although the alternative pathway (AP) is known to play a key pathogenic role in models of rheumatoid arthritis, the importance of the lectin pathway (LP) pattern recognition molecules such as ficolin (FCN) A, FCN B, and collectin (CL)-11, as well as the activating enzyme mannose-binding lectin-associated serine protease-2 (MASP-2), are less well understood. We show in this article that and mice are fully susceptible to collagen Ab-induced arthritis (CAIA). In contrast, and mice are substantially protected, with clinical disease activity decreased significantly ( < 0.05) by 47 and 70%, respectively. Histopathology scores, C3, factor D, FCN B deposition, and infiltration of synovial macrophages and neutrophils were similarly decreased in and mice. Our data support that FCN B plays an important role in the development of CAIA, likely through ligand recognition in the joint and MASP activation, and that MASP-2 also contributes to the development of CAIA, likely in a C4-independent manner. Decreased AP activity in the sera from and mice with arthritis on adherent anti-collagen Abs also support the hypothesis that pathogenic Abs, as well as additional inflammation-related ligands, are recognized by the LP and operate in vivo to activate complement. Finally, we also speculate that the residual disease seen in our studies is driven by the AP and/or the C2/C4 bypass pathway via the direct cleavage of C3 through an LP-dependent mechanism.
[Mh] Termos MeSH primário: Artrite Experimental/imunologia
Artrite Reumatoide/imunologia
Lectina de Ligação a Manose da Via do Complemento
Inflamação/imunologia
Lectinas/metabolismo
Serina Proteases Associadas a Proteína de Ligação a Manose/metabolismo
[Mh] Termos MeSH secundário: Animais
Complexo Antígeno-Anticorpo/metabolismo
Células Cultivadas
Colágeno/imunologia
Colectinas/genética
Colectinas/metabolismo
Proteínas do Sistema Complemento/metabolismo
Seres Humanos
Lectinas/genética
Serina Proteases Associadas a Proteína de Ligação a Manose/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (Collectins); 0 (Lectins); 0 (ficolin); 9007-34-5 (Collagen); 9007-36-7 (Complement System Proteins); EC 3.4.21.- (MASP-2 protein, mouse); EC 3.4.21.- (Mannose-Binding Protein-Associated Serine Proteases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700119



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