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[PMID]:28461446
[Au] Autor:Pequegnat B; Laird RM; Ewing CP; Hill CL; Omari E; Poly F; Monteiro MA; Guerry P
[Ad] Endereço:Department of Chemistry, University of Guelph, Guelph, Ontario, Canada.
[Ti] Título:Phase-Variable Changes in the Position of -Methyl Phosphoramidate Modifications on the Polysaccharide Capsule of Campylobacter jejuni Modulate Serum Resistance.
[So] Source:J Bacteriol;199(14), 2017 07 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:polysaccharide capsules (CPS) are characterized by the presence of nonstoichiometric -methyl phosphoramidate (MeOPN) modifications. The lack of stoichiometry is due to phase variation at homopolymeric tracts within the MeOPN transferase genes. strain 81-176 contains two MeOPN transferase genes and has been shown previously to contain MeOPN modifications at the 2 and 6 positions of the galactose (Gal) moiety in the CPS. We demonstrate here that one of the two MeOPN transferases, encoded by CJJ81176_1435, is bifunctional and is responsible for the addition of MeOPN to both the 2 and the 6 positions of Gal. A new MeOPN at the 4 position of Gal was observed in a mutant lacking the CJJ81176_1435 transferase and this was encoded by the CJJ81176_1420 transferase. During routine growth of 81-176, the CJJ81176_1420 transferase was predominantly in an off configuration, while the CJJ81176_1435 transferase was primarily on. However, exposure to normal human serum selected for cells expressing the CJJ81176_1420 transferase. MeOPN modifications appear to block binding of naturally occurring antibodies to the 81-176 CPS. The absence of MeOPN-4-Gal resulted in enhanced sensitivity to serum killing, whereas the loss of MeOPN-2-Gal and MeOPN-6-Gal resulted in enhanced resistance to serum killing, perhaps by allowing more MeOPN to be put onto the 4 position of Gal. undergoes phase variation in genes encoding surface antigens, leading to the concept that a strain of this organism consists of multiple genotypes that are selected for fitness in various environments. Methyl phosphoramidate modifications on the capsule of block access of preexisting antibodies in normal human sera to the polysaccharide chain, thus preventing activation of the classical arm of the complement cascade. We show that the capsule of strain 81-176 contains more sites of MeOPN modifications than previously recognized and that one site, on the 4 position of galactose, is more critical to complement resistance than the others. Exposure to normal human serum selects for variants in the population expressing this MeOPN modification.
[Mh] Termos MeSH primário: Amidas
Cápsulas Bacterianas/fisiologia
Campylobacter jejuni/metabolismo
Soros Imunes/imunologia
Ácidos Fosfóricos
Polissacarídeos Bacterianos/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos Antibacterianos
Clonagem Molecular
Regulação Bacteriana da Expressão Gênica/fisiologia
Epitopos Imunodominantes
Mutação
Polissacarídeos Bacterianos/química
Polissacarídeos Bacterianos/imunologia
Coelhos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amides); 0 (Antibodies, Bacterial); 0 (Immune Sera); 0 (Immunodominant Epitopes); 0 (Phosphoric Acids); 0 (Polysaccharides, Bacterial); 9Q189608GB (phosphoramidic acid)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


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[PMID]:29323845
[Au] Autor:Lazarenko AA; Alimbarova LM; Mordvintseva EY; Barinsky IF
[Ti] Título:Development of the suppository form of human immunoglobulin preparation with high titers of antibodies to herpes simplex virus types 1 and 2 for the treatment of chronic forms of herpetic disease.
[So] Source:Vopr Virusol;62(1):36-41, 2017.
[Is] ISSN:0507-4088
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:In spite of the vast arsenal of therapeutic agents, therapy of herpes virus infection (HVI) is very difficult, particularly in pregnant women, newborns and children in the first years of life, as well as in patients with immune deficiency. In this regard, possibility of using immunoglobulins for the treatment of HVI is currently attracting the attention of doctors. The aim of this work was to develop a suppository form of the drug containing donor immunoglobulins with high levels of neutralizing antibodies to herpes simplex virus types 1 and 2 for the treatment of chronic forms of herpetic disease. The study included the following steps: 1) selection of gamma-globulins with high antibody titer for HSV-1 and HSV-2 ELISA test; 2) determination of the level of neutralizing antibodies in the selected series of gamma-globulins in tests in tissue cultures and animals; 3) lyophilization of immunoglobulins; 4) development of the suppository form of the preparation containing gamma-globulin donors with high levels of neutralizing antibodies to HSV-1 and HSV-2; 5) study of the safety of the activity of neutralizing antibodies to HSV-1 and HSV-2 in the suppository form of the drug with hyaluronic acid used as immunomodulator. As the result of this work, immunoglobulin preparation in the suppository form was developed. The developed preparation meets the requirements for safety and efficacy. It is not toxic or pyrogenic. The problems of clinical use of this drug as a method of HVI therapy are discussed.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/administração & dosagem
Anticorpos Antivirais/administração & dosagem
Herpes Simples/tratamento farmacológico
Herpesvirus Humano 1/imunologia
Herpesvirus Humano 2/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Neutralizantes/biossíntese
Anticorpos Neutralizantes/isolamento & purificação
Anticorpos Antivirais/biossíntese
Anticorpos Antivirais/isolamento & purificação
Doença Crônica
Avaliação Pré-Clínica de Medicamentos
Cobaias
Herpes Simples/imunologia
Herpes Simples/virologia
Seres Humanos
Soros Imunes/química
Masculino
Camundongos
Coelhos
Ratos
Supositórios/administração & dosagem
Supositórios/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Immune Sera); 0 (Suppositories)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE


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[PMID]:29323842
[Au] Autor:Kuznetsova TV; Smimova MS; Leonovich OA; Gordeichuk IV; Biriukova IK; Zylkova MV; Tyn'o YY; Belyakova AV; Shevelev AB
[Ti] Título:A new method of producing NS5A antigen of hepatitis C virus.
[So] Source:Vopr Virusol;62(1):17-25, 2017.
[Is] ISSN:0507-4088
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:A task of creating a universal platform for engineering affordable recombinant producers of viral proteins conserving immunogenicity has not been solved yet. High toxicity of the viral proteins for the host cells, low yield and abnormal folding of the products often present severe obstacles to obtaining producers of the viral proteins. In this work, we report a new method of engineering and screening of deletion libraries from the viral antigen genes. This method allows selection of artificial derivatives of these genes adapted for expression in microbial producer cells. The method involves PCR amplification of the gene fragments using a system of randomized and adapter primers, which allows the spontaneous formation of duplexes from the random primers in the absence of the template DNA to be prevented. For selecting variants capable of in vivo expression, the obtained PCR products are cloned to a special vector of a direct phenotypical selection pQL30. It contains E. coli ß-galactosidase gene with an inserted polylinker producing a frame-shift mutation. Using this screening method, an artificial variant of hepatitis C (HCV) NS5a gene with optimal biotechnological properties was established. 27 clinical specimens of 1670 bp long HCV1b NS5a fragments were used as a source gene. A PCR bank of the deletion derivatives was produced. 40 LacZ-positive clones based on pQL30 vector with a 50-700 bp long insertion were selected. The LacZ activity of the cell lysates and the immunogenicity of the products were tested. As a result, a single clone encoding a soluble protein with Mr = 114 kDa was selected. Its yield reached 0.3% of the total cell protein. It was highly reactive with sera of HCV 1b infected patients but not with sera of the healthy donors.
[Mh] Termos MeSH primário: Antígenos Virais/genética
Escherichia coli/genética
Hepacivirus/genética
Hepatite C/diagnóstico
Engenharia de Proteínas/métodos
Proteínas Recombinantes/genética
Proteínas não Estruturais Virais/genética
[Mh] Termos MeSH secundário: Antígenos Virais/biossíntese
Antígenos Virais/imunologia
Antígenos Virais/isolamento & purificação
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Primers do DNA/síntese química
Primers do DNA/genética
Escherichia coli/metabolismo
Mutação da Fase de Leitura
Biblioteca Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Hepacivirus/imunologia
Hepatite C/imunologia
Hepatite C/virologia
Seres Humanos
Soros Imunes/química
Óperon Lac
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/imunologia
Proteínas Recombinantes/isolamento & purificação
Proteínas não Estruturais Virais/biossíntese
Proteínas não Estruturais Virais/imunologia
Proteínas não Estruturais Virais/isolamento & purificação
beta-Galactosidase/genética
beta-Galactosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Viral); 0 (Bacterial Proteins); 0 (DNA Primers); 0 (Immune Sera); 0 (NS-5 protein, hepatitis C virus); 0 (Recombinant Proteins); 0 (Viral Nonstructural Proteins); EC 3.2.1.23 (beta-Galactosidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE


  4 / 42500 MEDLINE  
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[PMID]:28461658
[Au] Autor:Kohl TO; Ascoli CA
[Ti] Título:Indirect Immunometric ELISA.
[So] Source:Cold Spring Harb Protoc;2017(5):pdb.prot093708, 2017 May 01.
[Is] ISSN:1559-6095
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This assay facilitates the immunometric determination of assay-associated reagents including the capture and detection antibodies as well as the analyte (i.e., antigen or antibody). It can precede the development of a sandwich enzyme-linked immunosorbent assay (ELISA) in which optimal antibody concentrations are applied for the quantitative measurement of the antigen. This protocol describes the materials and equipment required for the measurement of chromogenic substrate development; however, it can be adapted for use with chemiluminescent- and fluorescent-labeled reporters.
[Mh] Termos MeSH primário: Ensaio de Imunoadsorção Enzimática/métodos
[Mh] Termos MeSH secundário: Anticorpos/análise
Antígenos/análise
Soros Imunes/análise
Indicadores e Reagentes/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Antigens); 0 (Immune Sera); 0 (Indicators and Reagents)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1101/pdb.prot093708


  5 / 42500 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


  6 / 42500 MEDLINE  
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[PMID]:28961244
[Au] Autor:Durante IM; La Spina PE; Carmona SJ; Agüero F; Buscaglia CA
[Ad] Endereço:Instituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús (IIB-INTECh), Universidad Nacional de San Martín (UNSAM) and Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Buenos Aires, Argentina.
[Ti] Título:High-resolution profiling of linear B-cell epitopes from mucin-associated surface proteins (MASPs) of Trypanosoma cruzi during human infections.
[So] Source:PLoS Negl Trop Dis;11(9):e0005986, 2017 Sep.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The Trypanosoma cruzi genome bears a huge family of genes and pseudogenes coding for Mucin-Associated Surface Proteins (MASPs). MASP molecules display a 'mosaic' structure, with highly conserved flanking regions and a strikingly variable central and mature domain made up of different combinations of a large repertoire of short sequence motifs. MASP molecules are highly expressed in mammal-dwelling stages of T. cruzi and may be involved in parasite-host interactions and/or in diverting the immune response. METHODS/PRINCIPLE FINDINGS: High-density microarrays composed of fully overlapped 15mer peptides spanning the entire sequences of 232 non-redundant MASPs (~25% of the total MASP content) were screened with chronic Chagasic sera. This strategy led to the identification of 86 antigenic motifs, each one likely representing a single linear B-cell epitope, which were mapped to 69 different MASPs. These motifs could be further grouped into 31 clusters of structurally- and likely antigenically-related sequences, and fully characterized. In contrast to previous reports, we show that MASP antigenic motifs are restricted to the central and mature region of MASP polypeptides, consistent with their intracellular processing. The antigenicity of these motifs displayed significant positive correlation with their genome dosage and their relative position within the MASP polypeptide. In addition, we verified the biased genetic co-occurrence of certain antigenic motifs within MASP polypeptides, compatible with proposed intra-family recombination events underlying the evolution of their coding genes. Sequences spanning 7 MASP antigenic motifs were further evaluated using distinct synthesis/display approaches and a large panel of serum samples. Overall, the serological recognition of MASP antigenic motifs exhibited a remarkable non normal distribution among the T. cruzi seropositive population, thus reducing their applicability in conventional serodiagnosis. As previously observed in in vitro and animal infection models, immune signatures supported the concurrent expression of several MASPs during human infection. CONCLUSIONS/SIGNIFICANCE: In spite of their conspicuous expression and potential roles in parasite biology, this study constitutes the first unbiased, high-resolution profiling of linear B-cell epitopes from T. cruzi MASPs during human infection.
[Mh] Termos MeSH primário: Antígenos de Protozoários
Doença de Chagas/parasitologia
Epitopos de Linfócito B/química
Genoma de Protozoário
Proteínas de Membrana/imunologia
Trypanosoma cruzi/genética
Trypanosoma cruzi/imunologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Antígenos de Protozoários/química
Antígenos de Protozoários/genética
Epitopos de Linfócito B/genética
Epitopos de Linfócito B/imunologia
Seres Humanos
Soros Imunes
Proteínas de Membrana/química
Proteínas de Membrana/genética
Mucinas/química
Análise Serial de Proteínas
Proteínas de Protozoários/química
Proteínas de Protozoários/genética
Proteínas de Protozoários/imunologia
Trypanosoma cruzi/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Protozoan); 0 (Epitopes, B-Lymphocyte); 0 (Immune Sera); 0 (Membrane Proteins); 0 (Mucins); 0 (Protozoan Proteins)
[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:170930
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005986


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[PMID]:28780630
[Au] Autor:Song Y; Fan Z; Zuo Y; Wei H; Hu B; Chen M; Qiu R; Xue J; Wang F
[Ad] Endereço:Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, National Center for Engineering Research of Veterinary Bio-products, Nanjing, 210014, China.
[Ti] Título:Binding of rabbit hemorrhagic disease virus-like particles to host histo-blood group antigens is blocked by antisera from experimentally vaccinated rabbits.
[So] Source:Arch Virol;162(11):3425-3430, 2017 Nov.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:During infection host histo-blood group antigens (HBGAs) act as attachment factors that interact with rabbit hemorrhagic disease virus (RHDV) and participate in the infectious process. In the present study, baculovirus expressing recombinant RHDV capsid protein (VP60r) as a vaccine immunogen was used to test its antigenicity and immunogenicity via immunization experiments. Each group of rabbits immunized with VP60r was found to be fully protected against RHDV challenge. The duration of immunity of the vaccine following the inoculation of a single dose was determined to be at least 240 days. RHDV-specific humoral responses in antisera from inoculated rabbits were analyzed using VP60r virus-like particle (VLP)-based ELISA. Anti-VP60-specific antibody was produced by 7 days post-primary immunization. Following this stage, the levels of this antibody increased steadily, peaking at 90 days and maintaining a high level until 240 days. We developed a synthetic carbohydrate assay to detect blockage in attachment of RHDV VLPs to HBGAs by the rabbit antisera. On day 7 post-immunization, serum samples were demonstrated to block the binding of H type 2 to RHDV VLPs, with a blocking rate of almost 60%, a value that then increased steadily over time. From day 60 to day 240 post-immunization, serum samples completely blocked the binding of H type 2 to RHDV VLPs, with a blocking rate of almost 100%. This indicated that VP60-induced antibodies neutralize the interaction of RHDV with HBGAs.
[Mh] Termos MeSH primário: Antígenos de Grupos Sanguíneos/classificação
Infecções por Caliciviridae/veterinária
Vírus da Doença Hemorrágica de Coelhos
Soros Imunes/imunologia
Coelhos/sangue
Vacinas Virais/imunologia
[Mh] Termos MeSH secundário: Animais
Antígenos de Grupos Sanguíneos/química
Antígenos de Grupos Sanguíneos/metabolismo
Infecções por Caliciviridae/prevenção & controle
Infecções por Caliciviridae/virologia
Proteínas do Capsídeo/genética
Proteínas do Capsídeo/metabolismo
Regulação Viral da Expressão Gênica/fisiologia
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Group Antigens); 0 (Capsid Proteins); 0 (Immune Sera); 0 (Viral Vaccines)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170807
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3509-8


  8 / 42500 MEDLINE  
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[PMID]:28652011
[Au] Autor:Jirapongpairoj W; Hirono I; Kondo H
[Ad] Endereço:Laboratory of Genome Science, Graduate School, Tokyo University of Marine Science and Technology, Konan 4-5-7, Minato-ku, Tokyo 108-8477, Japan.
[Ti] Título:Development and evaluation of polyclonal antisera for detection of the IgM heavy chain of multiple fish species.
[So] Source:J Immunol Methods;449:71-75, 2017 Oct.
[Is] ISSN:1872-7905
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Antibodies are widely considered to be essential tools for detection of immune responses in various fish species. Here we produced the peptide polyclonal antisera (anti-fish IgH-1 and anti-fish IgH-2) to detect IgM of various fish species. The peptides were designed based on the conserved sequence of the fish immunoglobulin heavy chains of seven fish species (Japanese flounder, seabream, yellowtail, carp, rainbow trout, hybrid sturgeon and banded houndshark). By Western blotting, anti-fish IgH-1 antiserum detected the IgMs of all fish species except banded houndshark. Anti-fish IgH-2 antiserum clearly reacted with the IgMs of only three of the fish species (seabream, yellowtail and rainbow trout). Attempts to use the antisera to measure fish antibody titer by ELISA were unsuccessful. These results demonstrate that anti-fish IgH-1 peptide polyclonal antiserum is a potentially applicable tool for detecting immunoglobulins in various fish species by Western blotting.
[Mh] Termos MeSH primário: Peixes/imunologia
Soros Imunes/análise
Soros Imunes/imunologia
Cadeias Pesadas de Imunoglobulinas/imunologia
Imunoglobulina M/sangue
[Mh] Termos MeSH secundário: Animais
Especificidade de Anticorpos
Western Blotting
Reações Cruzadas
Ensaio de Imunoadsorção Enzimática
Fragmentos de Peptídeos/imunologia
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immune Sera); 0 (Immunoglobulin Heavy Chains); 0 (Immunoglobulin M); 0 (Peptide Fragments)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE


  9 / 42500 MEDLINE  
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[PMID]:28644752
[Au] Autor:Jin YB; Yang WT; Huang KY; Chen HL; Shonyela SM; Liu J; Liu Q; Feng B; Zhou Y; Zhi SL; Jiang YL; Wang JZ; Huang HB; Shi CW; Yang GL; Wang CF
[Ad] Endereço:a College of Animal Science and Technology, Jilin Provincial Engineering Research Center of Animal Probiotics, Key Laboratory of Animal Production and Product Quality Safety of Ministry of Education , Jilin Agricultural University , Changchun , China.
[Ti] Título:Expression and purification of swine RAG2 in E. coli for production of porcine RAG2 polyclonal antibodies.
[So] Source:Biosci Biotechnol Biochem;81(8):1489-1496, 2017 Aug.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Recombination activating gene 2 (RAG2) is necessary for immature B cell differentiation. Antibodies to human and rabbit RAG2 are currently commercially available, but antibodies to swine RAG remain unavailable to date. In this study, the swine RAG2 genes sequence was synthesized and then cloned into a pET-28a vector. The recombinant fusion protein was successfully expressed in E. coli, purified through nickel column chromatography, and further digested with Tobacco Etch Virus protease. The cleaved protein was purified by molecular-exclusion chromatography and named pRAG2. We used pRAG2 to immunize rabbits, collected the serum and purified rabbit anti-pRAG2 polyclonal antibodies. The rabbit anti-pRAG2 polyclonal antibodies were tested via immunofluorescence on eukaryotic cells overexpressing pRAG2 and also able to recognize pig natural RAG2 and human RAG2 protein in western blotting. These results indicated that the prepared rabbit anti-pRAG2 polyclonal antibodies may serve as a tool to detect immature B cell differentiation of swine.
[Mh] Termos MeSH primário: Anticorpos/química
Proteínas de Ligação a DNA/biossíntese
Escherichia coli/genética
Expressão Gênica
Proteínas Nucleares/biossíntese
VDJ Recombinases/biossíntese
[Mh] Termos MeSH secundário: Animais
Anticorpos/isolamento & purificação
Anticorpos/metabolismo
Western Blotting
Clonagem Molecular
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/imunologia
Endopeptidases/química
Escherichia coli/metabolismo
Imunofluorescência
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Seres Humanos
Soros Imunes/química
Isoenzimas/biossíntese
Isoenzimas/genética
Isoenzimas/imunologia
Proteínas Nucleares/genética
Proteínas Nucleares/imunologia
Coelhos
Proteínas Recombinantes de Fusão/biossíntese
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/imunologia
Suínos
VDJ Recombinases/genética
VDJ Recombinases/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (DNA-Binding Proteins); 0 (Immune Sera); 0 (Isoenzymes); 0 (Nuclear Proteins); 0 (RAG2 protein, human); 0 (Recombinant Fusion Proteins); EC 2.7.7.- (VDJ Recombinases); EC 3.4.- (Endopeptidases); EC 3.4.- (TEV protease)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1340086


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[PMID]:28582388
[Au] Autor:Nadugala MN; Jeewandara C; Malavige GN; Premaratne PH; Goonasekara CL
[Ad] Endereço:Faculty of Medicine, General Sir John Kotelawala Defence University, Ratmalana, Sri Lanka.
[Ti] Título:Natural antibody responses to the capsid protein in sera of Dengue infected patients from Sri Lanka.
[So] Source:PLoS One;12(6):e0178009, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This study aims to characterize the antigenicity of the Capsid (C) protein and the human antibody responses to C protein from the four dengue virus (DENV) serotypes. Parker hydrophilicity prediction, Emini surface accessibility prediction and Karplus & Schulz flexibility predictions were used to bioinformatically characterize antigenicity. The human antibody response to C protein was assessed by ELISA using immune sera and an array of overlapping DENV2 C peptides. DENV2 C protein peptides P1 (located on C protein at 2-18 a.a), P11 (79-95 a.a) and P12 (86-101 a.a) were recognized by most individuals exposed to infections with only one of the 4 DENV serotypes as well as people exposed to infections with two serotypes. These conserved peptide epitopes are located on the amino (1-40 a.a) and carboxy (70-100 a.a) terminal regions of C protein, which were predicted to be antigenic using different bioinformatic tools. DENV2 C peptide P6 (39-56 a.a) was recognized by all individuals exposed to DENV2 infections, some individuals exposed to DENV4 infections and none of the individuals exposed to DENV1 or 3 infections. Thus, unlike C peptides P1, P11 and P12, which contain epitopes, recognized by DENV serotype cross-reactive antibodies, DENV2 peptide P6 contains an epitope that is preferentially recognized by antibodies in people exposed to this serotype compared to other serotypes. We discuss our results in the context of the known structure of C protein and recent work on the human B-cell response to DENV infection.
[Mh] Termos MeSH primário: Anticorpos Antivirais/química
Proteínas do Capsídeo/imunologia
Vírus da Dengue/imunologia
Dengue/imunologia
Epitopos/química
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Sequência de Aminoácidos
Anticorpos Antivirais/biossíntese
Antígenos Virais/química
Antígenos Virais/genética
Antígenos Virais/imunologia
Sítios de Ligação
Proteínas do Capsídeo/química
Proteínas do Capsídeo/genética
Criança
Dengue/virologia
Vírus da Dengue/classificação
Vírus da Dengue/genética
Mapeamento de Epitopos
Epitopos/genética
Feminino
Seres Humanos
Soros Imunes/química
Imunidade Inata
Masculino
Meia-Idade
Peptídeos/química
Peptídeos/genética
Peptídeos/imunologia
Filogenia
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Sorogrupo
Sri Lanka
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Antigens, Viral); 0 (Capsid Proteins); 0 (Epitopes); 0 (Immune Sera); 0 (Peptides)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178009



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