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  1 / 17922 MEDLINE  
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[PMID]:28743825
[Au] Autor:Navarro Negredo P; Edgar JR; Wrobel AG; Zaccai NR; Antrobus R; Owen DJ; Robinson MS
[Ad] Endereço:Cambridge Institute for Medical Research, University of Cambridge, Cambridge, England, UK.
[Ti] Título:Contribution of the clathrin adaptor AP-1 subunit µ1 to acidic cluster protein sorting.
[So] Source:J Cell Biol;216(9):2927-2943, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acidic clusters act as sorting signals for packaging cargo into clathrin-coated vesicles (CCVs), and also facilitate down-regulation of MHC-I by HIV-1 Nef. To find acidic cluster sorting machinery, we performed a gene-trap screen and identified the medium subunit (µ1) of the clathrin adaptor AP-1 as a top hit. In µ1 knockout cells, intracellular CCVs still form, but acidic cluster proteins are depleted, although several other CCV components were either unaffected or increased, indicating that cells can compensate for long-term loss of AP-1. In vitro experiments showed that the basic patch on µ1 that interacts with the Nef acidic cluster also contributes to the binding of endogenous acidic cluster proteins. Surprisingly, µ1 mutant proteins lacking the basic patch and/or the tyrosine-based motif binding pocket could rescue the µ1 knockout phenotype completely. In contrast, these mutants failed to rescue Nef-induced down-regulation of MHC class I, suggesting a possible mechanism for attacking the virus while sparing the host cell.
[Mh] Termos MeSH primário: Complexo 1 de Proteínas Adaptadoras/metabolismo
Subunidades mu do Complexo de Proteínas Adaptadoras/metabolismo
Vesículas Revestidas por Clatrina/metabolismo
HIV-1/metabolismo
Produtos do Gene nef do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Complexo 1 de Proteínas Adaptadoras/química
Complexo 1 de Proteínas Adaptadoras/genética
Subunidades mu do Complexo de Proteínas Adaptadoras/química
Subunidades mu do Complexo de Proteínas Adaptadoras/genética
Sistemas CRISPR-Cas
Citometria de Fluxo
Técnicas de Silenciamento de Genes
Genótipo
Células HEK293
HIV-1/genética
Células HeLa
Antígenos de Histocompatibilidade Classe I/genética
Antígenos de Histocompatibilidade Classe I/metabolismo
Interações Hospedeiro-Patógeno
Seres Humanos
Modelos Moleculares
Mutação
Fenótipo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Transporte Proteico
Relação Estrutura-Atividade
Fatores de Tempo
Transfecção
Produtos do Gene nef do Vírus da Imunodeficiência Humana/química
Produtos do Gene nef do Vírus da Imunodeficiência Humana/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AP1M1 protein, human); 0 (Adaptor Protein Complex 1); 0 (Adaptor Protein Complex mu Subunits); 0 (Histocompatibility Antigens Class I); 0 (nef Gene Products, Human Immunodeficiency Virus); 0 (nef protein, Human immunodeficiency virus 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201602058


  2 / 17922 MEDLINE  
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[PMID]:29180808
[Au] Autor:Barkal AA; Weiskopf K; Kao KS; Gordon SR; Rosental B; Yiu YY; George BM; Markovic M; Ring NG; Tsai JM; McKenna KM; Ho PY; Cheng RZ; Chen JY; Barkal LJ; Ring AM; Weissman IL; Maute RL
[Ad] Endereço:Institute for Stem Cell Biology and Regenerative Medicine, Stanford University School of Medicine, Stanford, CA, USA.
[Ti] Título:Engagement of MHC class I by the inhibitory receptor LILRB1 suppresses macrophages and is a target of cancer immunotherapy.
[So] Source:Nat Immunol;19(1):76-84, 2018 Jan.
[Is] ISSN:1529-2916
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Exciting progress in the field of cancer immunotherapy has renewed the urgency of the need for basic studies of immunoregulation in both adaptive cell lineages and innate cell lineages. Here we found a central role for major histocompatibility complex (MHC) class I in controlling the phagocytic function of macrophages. Our results demonstrated that expression of the common MHC class I component ß -microglobulin (ß2M) by cancer cells directly protected them from phagocytosis. We further showed that this protection was mediated by the inhibitory receptor LILRB1, whose expression was upregulated on the surface of macrophages, including tumor-associated macrophages. Disruption of either MHC class I or LILRB1 potentiated phagocytosis of tumor cells both in vitro and in vivo, which defines the MHC class I-LILRB1 signaling axis as an important regulator of the effector function of innate immune cells, a potential biomarker for therapeutic response to agents directed against the signal-regulatory protein CD47 and a potential target of anti-cancer immunotherapy.
[Mh] Termos MeSH primário: Antígenos de Histocompatibilidade Classe I/imunologia
Receptor B1 de Leucócitos Semelhante a Imunoglobulina/imunologia
Macrófagos/imunologia
Neoplasias/imunologia
Fagocitose/imunologia
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Antígenos de Histocompatibilidade Classe I/metabolismo
Seres Humanos
Imunoterapia/métodos
Receptor B1 de Leucócitos Semelhante a Imunoglobulina/metabolismo
Macrófagos/metabolismo
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos NOD
Camundongos Knockout
Camundongos SCID
Neoplasias/metabolismo
Neoplasias/terapia
Neoplasias Experimentais/imunologia
Neoplasias Experimentais/metabolismo
Neoplasias Experimentais/terapia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histocompatibility Antigens Class I); 0 (Leukocyte Immunoglobulin-like Receptor B1)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180303
[Lr] Data última revisão:
180303
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.1038/s41590-017-0004-z


  3 / 17922 MEDLINE  
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[PMID]:28450240
[Au] Autor:O'Shannessy DJ; Bendas K; Schweizer C; Wang W; Albone E; Somers EB; Weil S; Meredith RK; Wustner J; Grasso L; Landers M; Nicolaides NC
[Ad] Endereço:Morphotek, Inc., 210 Welsh Pool Rd, Exton, PA, USA.
[Ti] Título:Correlation of FCGRT genomic structure with serum immunoglobulin, albumin and farletuzumab pharmacokinetics in patients with first relapsed ovarian cancer.
[So] Source:Genomics;109(3-4):251-257, 2017 07.
[Is] ISSN:1089-8646
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Farletuzumab (FAR) is a humanized monoclonal antibody (mAb) that binds to folate receptor alpha. A Ph3 trial in ovarian cancer patients treated with carboplatin/taxane plus FAR or placebo did not meet the primary statistical endpoint. Subgroup analysis demonstrated that subjects with high FAR exposure levels (Cmin>57.6µg/mL) showed statistically significant improvements in PFS and OS. The neonatal Fc receptor (fcgrt) plays a central role in albumin/IgG stasis and mAb pharmacokinetics (PK). Here we evaluated fcgrt sequence and association of its promoter variable number tandem repeats (VNTR) and coding single nucleotide variants (SNV) with albumin/IgG levels and FAR PK in the Ph3 patients. A statistical correlation existed between high FAR Cmin and AUC in patients with the highest quartile of albumin and lowest quartile of IgG1. Analysis of fcgrt identified 5 different VNTRs in the promoter region and 9 SNVs within the coding region, 4 which are novel.
[Mh] Termos MeSH primário: Albuminas/farmacocinética
Anticorpos Monoclonais Humanizados/farmacocinética
Antígenos de Histocompatibilidade Classe I/genética
Imunoglobulina G/metabolismo
Neoplasias Ovarianas/tratamento farmacológico
Receptores Fc/genética
[Mh] Termos MeSH secundário: Albuminas/análise
Anticorpos Monoclonais Humanizados/farmacologia
Anticorpos Monoclonais Humanizados/uso terapêutico
Ensaios Clínicos Fase III como Assunto
Feminino
Seres Humanos
Imunoglobulina G/sangue
Repetições Minissatélites
Recidiva Local de Neoplasia
Neoplasias Ovarianas/metabolismo
Neoplasias Ovarianas/patologia
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Albumins); 0 (Antibodies, Monoclonal, Humanized); 0 (Fc receptor, neonatal); 0 (Histocompatibility Antigens Class I); 0 (Immunoglobulin G); 0 (Receptors, Fc); 2O09BG0OWA (farletuzumab)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180218
[Lr] Data última revisão:
180218
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE


  4 / 17922 MEDLINE  
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[PMID]:28747348
[Au] Autor:Ghosh MK; Muller HK; Walker AM
[Ad] Endereço:Division of Biomedical Sciences, School of Medicine, University of California, Riverside, Riverside, CA 92521; and.
[Ti] Título:Lactation-Based Maternal Educational Immunity Crosses MHC Class I Barriers and Can Impart Th1 Immunity to Th2-Biased Recipients.
[So] Source:J Immunol;199(5):1729-1736, 2017 09 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have previously demonstrated lactational transfer of T cell-based immunity from dam to foster pup. In the short term, a significant part of transferred immunity is passive cellular immunity. However, as time progresses, this is replaced by what we have described as maternal educational immunity such that by young adulthood, all immune cells responding to a foster dam immunogen are the product of the foster pup's thymus. To reduce confounding factors, this original demonstration used congenic/syngeneic dam and foster pup pairs. In this study, we investigated lactational transfer of immunity to in MHC class I-mismatched animals, as well as from Th1-biased dams to Th2-biased foster pups. Using immunized C57BL/6J dams, lactational transfer to nonimmunized BALB/cJ foster pups resulted in much greater immunity than direct immunization in 5-wk-old pups (ex vivo assay of pup splenocytes). At this age, 82% of immunogen-responding cells in the pup spleen were produced through maternal educational immunity. FVB/NJ nonimmunized foster recipients had a greater number of maternal cells in the spleen and thymus but a much larger percentage was Foxp3 , resulting in equivalent immunity to direct immunization. Depletion of maternal Foxp3 cells from pup splenocytes illustrated a substantial role for lactationally transferred dam regulatory T cells in suppression of the ex vivo response in FVB/NJ, but not BALB/cJ, recipients. We conclude that lactational transfer of immunity can cross MHC class I barriers and that Th1 immunity can be imparted to Th2-biased offspring; in some instances, it can be greater than that achieved by direct immunization.
[Mh] Termos MeSH primário: Imunidade Materno-Adquirida
Lactação/imunologia
Mycobacterium tuberculosis/imunologia
Linfócitos T Reguladores/imunologia
Células Th1/imunologia
Células Th2/imunologia
Timócitos/imunologia
Tuberculose/imunologia
[Mh] Termos MeSH secundário: Animais
Feminino
Fatores de Transcrição Forkhead/metabolismo
Antígenos de Histocompatibilidade Classe I/imunologia
Isoantígenos/imunologia
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos C57BL
Gravidez
Equilíbrio Th1-Th2
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Forkhead Transcription Factors); 0 (Foxp3 protein, mouse); 0 (Histocompatibility Antigens Class I); 0 (Isoantigens)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180128
[Lr] Data última revisão:
180128
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601375


  5 / 17922 MEDLINE  
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[PMID]:29236750
[Au] Autor:Perri V; Gianchecchi E; Cifaldi L; Pellegrino M; Giorda E; Andreani M; Cappa M; Fierabracci A
[Ad] Endereço:Type 1 Diabetes Centre, Infectivology and Clinical Trials Research Department, Bambino Gesù Children's Hospital, IRCCS, Rome, Italy.
[Ti] Título:Identification of GAD65 AA 114-122 reactive 'memory-like' NK cells in newly diagnosed Type 1 diabetic patients by HLA-class I pentamers.
[So] Source:PLoS One;12(12):e0189615, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Type 1 diabetes is an autoimmune disease, in which pancreatic ß cells are destroyed by autoreactive T cells in genetically predisposed individuals. Serum beta cell autoantibody specificities have represented the mainstay for classifying diabetes as autoimmune-mediated and for stratifying risk in first-degree relatives. In recent years, approaches were attempted to solve the difficult issue of detecting rare antigen-specific autoreactive T cells and their significance to etiopathogenesis such as the use of the MHC multimer technology. This tool allowed the specific detection of increased percentages of GAD65 autoreactive T cells by means of HLA A*02:01 GAD65 AA 114-122 pentamers in newly diagnosed diabetics. Here we provide evidence that GAD65 AA 114-122 pentamers can depict a GAD65 AA114-122 peptide expandable population of functionally and phenotypically skewed, preliminary characterized CD3-CD8dullCD56+ 'memory-like' NK cells in PBMC of newly diagnosed diabetics. Our data suggest that the NK cell subset could bind the HLA class I GAD65 AA 114-122 pentamer through ILT2 inhibitory receptor. CD107a expression revealed increased degranulation of CD3-CD8dullCD56+ NK cells in GAD65 AA 114-122 and FLU peptide expanded peripheral blood mononuclear cells of diabetics following GAD65 AA 114-122 peptide HLA A*02:01 presentation in respect to the unpulsed condition. CD107a expression was enriched in ILT2 positive NK cells. As opposite to basal conditions where similar percentages of CD3-CD56+ILT2+ cells were detected in diabetics and controls, CD3-CD56+CD107a+ and CD3-CD56+ILT2+CD107a+ cells were significantly increased in T1D PBMC either GAD65 AA 114-122 or FLU peptides stimulated after co-culture with GAD65 AA 114-122 pulsed APCs. As control, healthy donor NK cells showed similar degranulation against both GAD65 AA 114-122 pulsed and unpulsed APCs. The pathogenetic significance of the CD3-CD8dullCD56+ 'memory-like NK cell subset' with increased response upon secondary challenge in diabetics remains to be elucidated.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 1/metabolismo
Glutamato Descarboxilase/metabolismo
Antígenos de Histocompatibilidade Classe I/metabolismo
Memória Imunológica
Células Matadoras Naturais/metabolismo
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Feminino
Seres Humanos
Masculino
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histocompatibility Antigens Class I); EC 4.1.1.15 (Glutamate Decarboxylase); EC 4.1.1.15 (glutamate decarboxylase 2)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189615


  6 / 17922 MEDLINE  
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[PMID]:29176828
[Au] Autor:McMurtrey C; Harriff MJ; Swarbrick GM; Duncan A; Cansler M; Null M; Bardet W; Jackson KW; Lewinsohn DA; Hildebrand W; Lewinsohn DM
[Ad] Endereço:Department of Microbiology and Immunology, University of Oklahoma Health Science Center, Oklahoma City, OK, United States of America.
[Ti] Título:T cell recognition of Mycobacterium tuberculosis peptides presented by HLA-E derived from infected human cells.
[So] Source:PLoS One;12(11):e0188288, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:HLA-E is a non-conventional MHC Class I molecule that has been recently demonstrated to present pathogen-derived ligands, resulting in the TCR-dependent activation of αß CD8+ T cells. The goal of this study was to characterize the ligandome displayed by HLA-E following infection with Mycobacterium tuberculosis (Mtb) using an in-depth mass spectrometry approach. Here we identified 28 Mtb ligands derived from 13 different source proteins, including the Esx family of proteins. When tested for activity with CD8+ T cells isolated from sixteen donors, nine of the ligands elicited an IFN-γ response from at least one donor, with fourteen of 16 donors responding to the Rv0634A19-29 peptide. Further evaluation of this immunodominant peptide response confirmed HLA-E restriction and the presence of Rv0634A19-29-reactive CD8+ T cells in the peripheral blood of human donors. The identification of an Mtb HLA-E ligand that is commonly recognized may provide a target for a non-traditional vaccine strategy.
[Mh] Termos MeSH primário: Apresentação do Antígeno/imunologia
Linfócitos T CD8-Positivos/imunologia
Antígenos de Histocompatibilidade Classe I/imunologia
Mycobacterium tuberculosis/imunologia
Peptídeos/imunologia
Tuberculose/imunologia
Tuberculose/microbiologia
[Mh] Termos MeSH secundário: Células A549
Adulto
Sequência de Aminoácidos
Seres Humanos
Ligantes
Peptídeos/química
Solubilidade
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HLA-E antigen); 0 (Histocompatibility Antigens Class I); 0 (Ligands); 0 (Peptides)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188288


  7 / 17922 MEDLINE  
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[PMID]:29078849
[Au] Autor:Yu P; Zhu Q; Chen C; Fu X; Li Y; Liu L; Luo Q; Wang F; Wang Y
[Ad] Endereço:Department of Immunology, School of Basic Medical Science, Xiangya School of Medicine, Central South University, Changsha, Hunan, China.
[Ti] Título:Association Between Major Histocompatibility Complex Class I Chain-Related Gene Polymorphisms and Susceptibility of Systemic Lupus Erythematosus.
[So] Source:Am J Med Sci;354(4):430-435, 2017 Oct.
[Is] ISSN:1538-2990
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Major histocompatibility complex class I chain-related gene (MIC) polymorphisms have been associated with many autoimmune diseases. To explore the correlation between MIC polymorphisms and systemic lupus erythematosus (SLE), we compared the sequence of the MIC gene in Han Chinese patients with SLE from Hainan Island, China, with healthy individuals. METHODS: In this study, the MIC polymorphisms in 296 subjects (159 patients with SLE and 137 healthy volunteers) of Han ethnicity from Hainan Island were characterized. A chi-square test was performed to evaluate the differences in the allelic frequency of the MIC genes between patients with SLE and the control subjects. RESULTS: The genotyping results indicated that the frequencies of the MICA*010, MICB*014, and MICB*002 alleles were significantly higher in the control subjects than the patients with SLE. Additionally, the results also indicated that the frequency of the MICB*009N in the SLE group was significantly increased compared to that in the matched control subjects. CONCLUSIONS: The results of this study suggested that the MICB*009N allele might be a risk factor for SLE, whereas the MICB*014, MICA*010 and MICB*002 alleles were associated with reduced incidence of SLE in the study population.
[Mh] Termos MeSH primário: Alelos
Frequência do Gene
Predisposição Genética para Doença
Antígenos de Histocompatibilidade Classe I/genética
Lúpus Eritematoso Sistêmico/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Grupo com Ancestrais do Continente Asiático
China
Feminino
Antígenos de Histocompatibilidade Classe I/imunologia
Seres Humanos
Lúpus Eritematoso Sistêmico/etnologia
Lúpus Eritematoso Sistêmico/imunologia
Masculino
Meia-Idade
Polimorfismo Genético
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histocompatibility Antigens Class I); 0 (MHC class I-related chain A); 0 (MICB antigen)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171029
[St] Status:MEDLINE


  8 / 17922 MEDLINE  
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[PMID]:28991911
[Au] Autor:Dechavanne C; Dechavanne S; Sadissou I; Lokossou AG; Alvarado F; Dambrun M; Moutairou K; Courtin D; Nuel G; Garcia A; Migot-Nabias F; King CL
[Ad] Endereço:Center for Global Health and Diseases, Case Western Reserve University, Cleveland, Ohio, United States of America.
[Ti] Título:Associations between an IgG3 polymorphism in the binding domain for FcRn, transplacental transfer of malaria-specific IgG3, and protection against Plasmodium falciparum malaria during infancy: A birth cohort study in Benin.
[So] Source:PLoS Med;14(10):e1002403, 2017 Oct.
[Is] ISSN:1549-1676
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Transplacental transfer of maternal immunoglobulin G (IgG) to the fetus helps to protect against malaria and other infections in infancy. Recent studies have emphasized the important role of malaria-specific IgG3 in malaria immunity, and its transfer may reduce the risk of malaria in infancy. Human IgGs are actively transferred across the placenta by binding the neonatal Fc receptor (FcRn) expressed within the endosomes of the syncytiotrophoblastic membrane. Histidine at position 435 (H435) provides for optimal Fc-IgG binding. In contrast to other IgG subclasses, IgG3 is highly polymorphic and usually contains an arginine at position 435, which reduces its binding affinity to FcRn in vitro. The reduced binding to FcRn is associated with reduced transplacental transfer and reduced half-life of IgG3 in vivo. Some haplotypes of IgG3 have histidine at position 435. This study examines the hypotheses that the IgG3-H435 variant promotes increased transplacental transfer of malaria-specific antibodies and a prolonged IgG3 half-life in infants and that its presence correlates with protection against clinical malaria during infancy. METHODS AND FINDINGS: In Benin, 497 mother-infant pairs were included in a longitudinal birth cohort. Both maternal and cord serum samples were assayed for levels of IgG1 and IgG3 specific for MSP119, MSP2 (both allelic families, 3D7 and FC27), MSP3, GLURP (both regions, R0 and R2), and AMA1 antigens of Plasmodium falciparum. Cord:maternal ratios were calculated. The maternal IgG3 gene was sequenced to identify the IgG3-H435 polymorphism. A multivariate logistic regression was used to examine the association between maternal IgG3-H435 polymorphism and transplacental transfer of IgG3, adjusting for hypergammaglobulinemia, maternal malaria, and infant malaria exposure. Twenty-four percent of Beninese women living in an area highly endemic for malaria had the IgG3-H435 allele (377 women homozygous for the IgG3-R435 allele, 117 women heterozygous for the IgG3-R/H alleles, and 3 women homozygous for the IgG3-H435 allele). Women with the IgG3-H435 allele had a 78% (95% CI 17%, 170%, p = 0.007) increased transplacental transfer of GLURP-R2 IgG3 compared to those without the IgG3-H435 allele. Furthermore, in infants born to mothers with the IgG3-H435 variant, a 28% longer IgG3 half-life was noted (95% CI 4%, 59%, p = 0.02) compared to infants born to mothers homozygous for the IgG3-R435 allele. Similar findings were observed for AMA1, MSP2-3D7, MSP3, GLURP-R0, and GLURP-R2 but not for MSP119 and MSP2-FC27. Infants born to women with IgG3-H435 had a 32% lower risk of symptomatic malaria during infancy (incidence rate ratio [IRR] = 0.68 [95% CI 0.51, 0.91], p = 0.01) compared to infants born to mothers homozygous for IgG3-R435. We did not find a lower risk of asymptomatic malaria in infants born to women with or without IgG3-H435. Limitations of the study were the inability to determine (i) the actual amount of IgG3-H435 relative to IgG-R435 in serum samples and (ii) the proportion of malaria-specific IgG produced by infants versus acquired from their mothers. CONCLUSIONS: An arginine-to-histidine replacement at residue 435 in the binding domain of IgG3 to FcRn increases the transplacental transfer and half-life of malaria-specific IgG3 in young infants and is associated with reduced risk of clinical malaria during infancy. The IgG3-H435 allele may be under positive selection, given its relatively high frequency in malaria endemic areas.
[Mh] Termos MeSH primário: Antígenos de Histocompatibilidade Classe I/genética
Imunoglobulina G/sangue
Transmissão Vertical de Doença Infecciosa
Malária Falciparum/prevenção & controle
Troca Materno-Fetal
Circulação Placentária
Plasmodium falciparum/imunologia
Polimorfismo Genético
Receptores Fc/genética
[Mh] Termos MeSH secundário: Adulto
Benin
Distribuição de Qui-Quadrado
Feminino
Predisposição Genética para Doença
Meia-Vida
Heterozigoto
Antígenos de Histocompatibilidade Classe I/metabolismo
Homozigoto
Seres Humanos
Lactente
Recém-Nascido
Estimativa de Kaplan-Meier
Modelos Logísticos
Estudos Longitudinais
Malária Falciparum/genética
Malária Falciparum/imunologia
Malária Falciparum/transmissão
Análise Multivariada
Fenótipo
Plasmodium falciparum/patogenicidade
Gravidez
Modelos de Riscos Proporcionais
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteólise
Receptores Fc/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fc receptor, neonatal); 0 (Histocompatibility Antigens Class I); 0 (Immunoglobulin G); 0 (Receptors, Fc)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171010
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pmed.1002403


  9 / 17922 MEDLINE  
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[PMID]:28978689
[Au] Autor:Jurtz V; Paul S; Andreatta M; Marcatili P; Peters B; Nielsen M
[Ad] Endereço:Department of Bio and Health Informatics, Technical University of Denmark, DK-2800 Lyngby, Denmark.
[Ti] Título:NetMHCpan-4.0: Improved Peptide-MHC Class I Interaction Predictions Integrating Eluted Ligand and Peptide Binding Affinity Data.
[So] Source:J Immunol;199(9):3360-3368, 2017 Nov 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytotoxic T cells are of central importance in the immune system's response to disease. They recognize defective cells by binding to peptides presented on the cell surface by MHC class I molecules. Peptide binding to MHC molecules is the single most selective step in the Ag-presentation pathway. Therefore, in the quest for T cell epitopes, the prediction of peptide binding to MHC molecules has attracted widespread attention. In the past, predictors of peptide-MHC interactions have primarily been trained on binding affinity data. Recently, an increasing number of MHC-presented peptides identified by mass spectrometry have been reported containing information about peptide-processing steps in the presentation pathway and the length distribution of naturally presented peptides. In this article, we present NetMHCpan-4.0, a method trained on binding affinity and eluted ligand data leveraging the information from both data types. Large-scale benchmarking of the method demonstrates an increase in predictive performance compared with state-of-the-art methods when it comes to identification of naturally processed ligands, cancer neoantigens, and T cell epitopes.
[Mh] Termos MeSH primário: Bases de Dados de Proteínas
Epitopos de Linfócito T/imunologia
Antígenos de Histocompatibilidade Classe I/imunologia
Peptídeos/imunologia
Software
[Mh] Termos MeSH secundário: Seres Humanos
Valor Preditivo dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epitopes, T-Lymphocyte); 0 (Histocompatibility Antigens Class I); 0 (Peptides)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171006
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700893


  10 / 17922 MEDLINE  
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[PMID]:28957416
[Au] Autor:Szikora B; Hiripi L; Bender B; Kacskovics I; Iliás A
[Ad] Endereço:Department of Immunology, ELTE Eötvös Loránd University, Budapest, Hungary.
[Ti] Título:Characterization of the interactions of rabbit neonatal Fc receptor (FcRn) with rabbit and human IgG isotypes.
[So] Source:PLoS One;12(9):e0185662, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Despite the increasing importance of rabbit as an animal model in pharmacological studies like investigating placental transfer of therapeutic IgGs, little is known about the molecular interaction of the rabbit neonatal Fc receptor (FcRn) with rabbit and human IgG molecules. We analyzed the interactions of the rabbit and human FcRn with rabbit and human IgG isotypes using surface plasmon resonance assay. Similar to FcRn of other species, rabbit FcRn functions in pH-dependent manner, as it binds IgGs at pH 6.0, but no binding occurs at pH 7.4. We also showed that rabbit FcRn binds rabbit IgG and human IgG1 with nearly identical affinity, whereas it has stronger interactions with the other human IgG isotypes. The similar affinity of rabbit IgG and human IgG1 for rabbit FcRn was confirmed by in vitro FcRn-mediated recycling assay. These data verify that rabbit is an appropriate animal model for analyzing the pharmacokinetics of human therapeutic monoclonal antibodies.
[Mh] Termos MeSH primário: Antígenos de Histocompatibilidade Classe I/metabolismo
Imunoglobulina G/metabolismo
Receptores Fc/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Cromatografia em Gel
Antígenos de Histocompatibilidade Classe I/química
Seres Humanos
Imunoglobulina G/química
Macrófagos/metabolismo
Coelhos
Receptores Fc/química
Homologia de Sequência de Aminoácidos
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fc receptor, neonatal); 0 (Histocompatibility Antigens Class I); 0 (Immunoglobulin G); 0 (Receptors, Fc)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170929
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185662



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