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  1 / 2114 MEDLINE  
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[PMID]:29458526
[Au] Autor:Ma J; Wei Y; Zhang L; Wang X; Yao D; Liu D; Liu W; Yu S; Yu Y; Wu Z; Yu L; Zhu Z; Cui Y
[Ad] Endereço:College of Life Science and Technology, Heilongjiang Bayi Agricultural University, Daqing 163319, PR China.
[Ti] Título:Identification of a novel linear B-cell epitope as a vaccine candidate in the N2N3 subdomain of Staphylococcus aureus fibronectin-binding protein A.
[So] Source:J Med Microbiol;67(3):423-431, 2018 Mar.
[Is] ISSN:1473-5644
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To explore an epitope-based vaccine against Staphylococcus aureus, we screened the epitopes in the N2N3 subdomain of fibronectin-binding protein A (FnBPA) as a surface component of S. aureus. METHODOLOGY: We expressed N2N3 proteins and prepared monoclonal antibodies (mAbs) against N2N3 by the hybridoma technique, before screening the B-cell epitopes in N2N3 using a phage-displayed random 12-mer peptide library with these mAbs against N2N3. Finally, we analysed the characters of the screened epitopes using immunofluorescence and an S. aureus infection assay. RESULTS: In this paper, we identified a linear B-cell epitope in N2N3 through screening a phage-displayed peptide library with a 3C3 mAb against the N2N3. The 3C3 mAb recognized the 159IETFNKANNRFSH171 sequence of the N2N3 subdomain. Subsequently, site-directed mutagenic analysis demonstrated that residues F162, K164, N167, R168 and F169 formed the core of 159IETFNKANNRFSH171, and this core motif was the minimal determinant of the B-cell epitope recognized by the 3C3 mAb. The epitope 159IETFNKANNRFSH171 showed high homology among different S. aureus strains. Moreover, this epitope was exposed on the surface of the S. aureus by using an enzyme-linked immunosorbent assay (ELISA) assay and an indirect immunofluorescence assay. As expected, the epitope peptide evoked a protective immune response against S. aureus infection in immunized mice. CONCLUSION: We identified a novel linear B-cell epitope, 159IETFNKANNRFSH171, in the N2N3 subdomain of S. aureus fibronectin-binding protein A that is recognized by 3C3 mAb, which will contribute to the further study of an epitope-based vaccine candidate against S. aureus.
[Mh] Termos MeSH primário: Adesinas Bacterianas/imunologia
Epitopos de Linfócito B/imunologia
Infecções Estafilocócicas/prevenção & controle
Vacinas Antiestafilocócicas/imunologia
Staphylococcus aureus/imunologia
[Mh] Termos MeSH secundário: Adesinas Bacterianas/química
Adesinas Bacterianas/genética
Animais
Anticorpos Monoclonais/imunologia
Anticorpos Monoclonais/isolamento & purificação
Ensaio de Imunoadsorção Enzimática
Mapeamento de Epitopos
Epitopos de Linfócito B/química
Epitopos de Linfócito B/genética
Imunização
Camundongos
Biblioteca de Peptídeos
Ligação Proteica
Infecções Estafilocócicas/imunologia
Staphylococcus aureus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Antibodies, Monoclonal); 0 (Epitopes, B-Lymphocyte); 0 (Peptide Library); 0 (Staphylococcal Vaccines); 0 (fibronectin-binding proteins, bacterial)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180221
[St] Status:MEDLINE
[do] DOI:10.1099/jmm.0.000633


  2 / 2114 MEDLINE  
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[PMID]:29037477
[Au] Autor:Bhatt M; Mohapatra JK; Pandey LK; Mohanty NN; Das B; Prusty BR; Pattnaik B
[Ad] Endereço:ICAR-Directorate of Foot and Mouth Disease, Mukteswar 263 138, Uttarakhand, India.
[Ti] Título:Mutational analysis of foot and mouth disease virus nonstructural polyprotein 3AB-coding region to design a negative marker virus.
[So] Source:Virus Res;243:36-43, 2018 01 02.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Inactivated purified whole virus vaccines are used for control of foot and mouth disease (FMD). ELISAs detecting antibodies to the nonstructural proteins (NSP), a marker of infection, are primarily used to differentiate FMD virus (FMDV) infected from vaccinated animals (DIVA). However, such DIVA assays have a limitation to their specificity since residual NSPs present in the relatively impure vaccines are suspected to induce an NSP-antibody response in the repeatedly vaccinated animals. Epitope-deleted negative marker vaccine strategy seems to have an advantage over the conventional vaccines in identifying the infected animals with accuracy. NSP 3AB contains an abundance of immunodominant B-cell epitopes of diagnostic importance. This study addresses the feasibility of producing 3AB-truncated FMDV mutant as a potential negative marker vaccine candidate. An infectious cDNA clone of FMDV serotype Asia 1 strain was used to engineer an array of deletion mutations in the established antigenic domain of 3AB. The maximum length of deletion tolerated by the virus was found to be restricted to amino acid residues 87-144 in the C-terminal half of 3A protein along with deletion of the first two copies of 3B peptide. The 3AB-truncated marker virus (Asia 1 IND 491/1997Δ3A 3B +FLAG) demonstrated infectivity titres comparable to that of the parental virus in BHK-21 (log 7.42 TCID /ml) and LFBK-α ß (log 8.30 TCID /ml) cell monolayer culture. The protein fragment corresponding to the viable deletion in the 3AB region was expressed in a prokaryotic system to standardize a companion assay (3A 3B I-ELISA) for the negative marker virus which showed reasonably high diagnostic sensitivity (96.9%) and specificity (100% for naïve and 97.1% for uninfected vaccinated samples). The marker virus and its companion ELISA designed in this study provide a basis to devise a marker vaccine strategy for FMD control.
[Mh] Termos MeSH primário: Vírus da Febre Aftosa/genética
Febre Aftosa/virologia
Poliproteínas/genética
Proteínas não Estruturais Virais/genética
Proteínas Virais/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Antivirais/imunologia
Análise Mutacional de DNA
Epitopos de Linfócito B/genética
Epitopos de Linfócito B/imunologia
Febre Aftosa/imunologia
Febre Aftosa/prevenção & controle
Vírus da Febre Aftosa/imunologia
Poliproteínas/imunologia
Proteínas não Estruturais Virais/imunologia
Proteínas Virais/genética
Vacinas Virais/genética
Vacinas Virais/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Epitopes, B-Lymphocyte); 0 (Polyproteins); 0 (Viral Nonstructural Proteins); 0 (Viral Proteins); 0 (Viral Vaccines)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE


  3 / 2114 MEDLINE  
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[PMID]:29284249
[Au] Autor:Schreterova E; Bhide M; Potocnakova L; Borszekova Pulzova L
[Ad] Endereço:Laboratory of Biomedical Microbiology and Immunology, Department of Microbiology and Immunology, University of Veterinary Medicine and Pharmacy, 041 81 Kosice, Slovakia. eva.kendrovska@gmail.com.
[Ti] Título:Design, construction and evaluation of multi-epitope antigens for diagnosis of Lyme disease.
[So] Source:Ann Agric Environ Med;24(4):696-701, 2017 Dec 23.
[Is] ISSN:1898-2263
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Introduction and objective. Lyme disease (LD) is the most common vector-borne disease in the temperate zone of the Northern Hemisphere. Diagnosis of LD is mainly based on clinical symptoms supported with serology (detection of anti-Borrelia antibodies) and is often misdiagnosed in areas of endemicity. MATERIAL AND METHODS: In this study, the chimeric proteins (A/C-2, A/C-4 and A/C-7.1) consisting of B-cell epitopes of outer surface proteins OspA and OspC from Borrelia genospecies prevalent in Eastern Slovakia, were designed, over-expressed in E. coli, and used to detect specific anti-Borrelia antibodies in serologically characterized sera from patients with Lyme-like symptoms to evaluate their diagnostic potential. RESULTS: Results showed that chimeras vary in their immuno-reactivity when tested with human sera. Compared with the results obtained from a two-tier test, the application of recombinant multi-epitope chimeric proteins as diagnosis antigens, produced fair agreement in the case of A/C-2 (0.20<κ<0.40) and good agreement (0.60<κ<0.80) when A/C-7.1 was used as capture antigen. Chimera A/C-4 were excluded from further study due to loss of reactivity with OspA-specific antibodies. CONCLUSIONS: The combination of specific B-cell epitopes from OspA and OspC proteins may improve the diagnostic accuracy of serologic assays, but further studies are required to address this hypothesis.
[Mh] Termos MeSH primário: Borrelia burgdorferi/isolamento & purificação
Ensaio de Imunoadsorção Enzimática/métodos
Epitopos de Linfócito B/análise
Doença de Lyme/diagnóstico
[Mh] Termos MeSH secundário: Anticorpos Antibacterianos/análise
Anticorpos Antibacterianos/imunologia
Antígenos de Superfície/análise
Antígenos de Superfície/genética
Antígenos de Superfície/imunologia
Proteínas da Membrana Bacteriana Externa/análise
Proteínas da Membrana Bacteriana Externa/genética
Proteínas da Membrana Bacteriana Externa/imunologia
Vacinas Bacterianas/análise
Vacinas Bacterianas/genética
Vacinas Bacterianas/imunologia
Borrelia burgdorferi/genética
Borrelia burgdorferi/imunologia
Epitopos de Linfócito B/imunologia
Seres Humanos
Lipoproteínas/análise
Lipoproteínas/genética
Lipoproteínas/imunologia
Doença de Lyme/imunologia
Doença de Lyme/microbiologia
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Bacterial); 0 (Antigens, Surface); 0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Vaccines); 0 (Epitopes, B-Lymphocyte); 0 (Lipoproteins); 0 (OspA protein)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171230
[St] Status:MEDLINE


  4 / 2114 MEDLINE  
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[PMID]:29186182
[Au] Autor:Jiang N; Jin H; Li Y; Ge X; Han J; Guo X; Zhou L; Yang H
[Ad] Endereço:Key Laboratory of Animal Epidemiology of Ministry of Agriculture, College of Veterinary Medicine, China Agricultural University, Beijing, People's Republic of China.
[Ti] Título:Identification of a novel linear B-cell epitope in nonstructural protein 11 of porcine reproductive and respiratory syndrome virus that are conserved in both genotypes.
[So] Source:PLoS One;12(11):e0188946, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Porcine reproductive and respiratory syndrome virus (PRRSV) is one of the most economically important pathogens, that hinder the development of global pork industry. Its nonstructural protein 11 (nsp11), with the nidoviral uridylate-specific endoribonuclease (NendoU) domain, is essential for PRRSV genome replication and it also contributes to host innate immunity suppression. However, the immunogenicity and immune structure of PRRSV nsp11 have not been well investigated yet. In this study, a monoclonal antibody (mAb), designated 3F9, that against nsp11 was generated. Subsequently, a series of partially overlapped fragments, covered the nsp1140-223aa, were expressed to test the reactivity with mAb 3F9, and the 111DCREY115 was found to be the core unit of the B-cell epitope recognized by mAb 3F9. Further investigation indicated that both genotype 1 and genotype 2 PRRSV can be recognized by mAb 3F9, due to the 111DCREY115 is conserved in both genotype virus. Meanwhile, this epitope, localized at the surface of nsp11 in 3D structure, is confirmed to be able to induce humoral immune response in PRRSV infected pigs. These findings do not only provide an mAb tool to further investigate the function of nsp11, they also indicate the diagnostic potential for this epitope.
[Mh] Termos MeSH primário: Epitopos de Linfócito B/química
Vírus da Síndrome Respiratória e Reprodutiva Suína/imunologia
Proteínas não Estruturais Virais/imunologia
[Mh] Termos MeSH secundário: Animais
Genótipo
Vírus da Síndrome Respiratória e Reprodutiva Suína/genética
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epitopes, B-Lymphocyte); 0 (Viral Nonstructural Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180101
[Lr] Data última revisão:
180101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188946


  5 / 2114 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


  6 / 2114 MEDLINE  
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[PMID]:28902916
[Au] Autor:Dubrovskaya V; Guenaga J; de Val N; Wilson R; Feng Y; Movsesyan A; Karlsson Hedestam GB; Ward AB; Wyatt RT
[Ad] Endereço:Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, California, United States of America.
[Ti] Título:Targeted N-glycan deletion at the receptor-binding site retains HIV Env NFL trimer integrity and accelerates the elicited antibody response.
[So] Source:PLoS Pathog;13(9):e1006614, 2017 Sep.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Extensive shielding by N-glycans on the surface of the HIV envelope glycoproteins (Env) restricts B cell recognition of conserved neutralizing determinants. Elicitation of broadly neutralizing antibodies (bNAbs) in selected HIV-infected individuals reveals that Abs capable of penetrating the glycan shield can be generated by the B cell repertoire. Accordingly, we sought to determine if targeted N-glycan deletion might alter antibody responses to Env. We focused on the conserved CD4 binding site (CD4bs) since this is a known neutralizing determinant that is devoid of glycosylation to allow CD4 receptor engagement, but is ringed by surrounding N-glycans. We selectively deleted potential N-glycan sites (PNGS) proximal to the CD4bs on well-ordered clade C 16055 native flexibly linked (NFL) trimers to potentially increase recognition by naïve B cells in vivo. We generated glycan-deleted trimer variants that maintained native-like conformation and stability. Using a panel of CD4bs-directed bNAbs, we demonstrated improved accessibility of the CD4bs on the N-glycan-deleted trimer variants. We showed that pseudoviruses lacking these Env PNGSs were more sensitive to neutralization by CD4bs-specific bNAbs but remained resistant to non-neutralizing mAbs. We performed rabbit immunogenicity experiments using two approaches comparing glycan-deleted to fully glycosylated NFL trimers. The first was to delete 4 PNGS sites and then boost with fully glycosylated Env; the second was to delete 4 sites and gradually re-introduce these N-glycans in subsequent boosts. We demonstrated that the 16055 PNGS-deleted trimers more rapidly elicited serum antibodies that more potently neutralized the CD4bs-proximal-PNGS-deleted viruses in a statistically significant manner and strongly trended towards increased neutralization of fully glycosylated autologous virus. This approach elicited serum IgG capable of cross-neutralizing selected tier 2 viruses lacking N-glycans at residue N276 (natural or engineered), indicating that PNGS deletion of well-ordered trimers is a promising strategy to prime B cell responses to this conserved neutralizing determinant.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/imunologia
Anticorpos Anti-HIV/imunologia
Polissacarídeos/imunologia
Produtos do Gene env do Vírus da Imunodeficiência Humana/imunologia
[Mh] Termos MeSH secundário: Animais
Linfócitos B/imunologia
Antígenos CD4/imunologia
Ensaio de Imunoadsorção Enzimática
Epitopos de Linfócito B/imunologia
Feminino
HIV-1/imunologia
Imagem Tridimensional
Ativação Linfocitária/imunologia
Microscopia Eletrônica
Mutagênese Sítio-Dirigida
Coelhos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (CD4 Antigens); 0 (Epitopes, B-Lymphocyte); 0 (HIV Antibodies); 0 (Polysaccharides); 0 (env Gene Products, Human Immunodeficiency Virus)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006614


  7 / 2114 MEDLINE  
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[PMID]:28902877
[Au] Autor:Cai NL; Lau ATY; Yu FY; Wu DD; Dai LJ; Mo HY; Lin CM; Xu YM
[Ad] Endereço:Laboratory of Cancer Biology and Epigenetics, Department of Cell Biology and Genetics, Shantou University Medical College, Shantou, Guangdong, P. R. China.
[Ti] Título:Purification and characterization of a highly specific polyclonal antibody against human extracellular signal-regulated kinase 8 and its detection in lung cancer.
[So] Source:PLoS One;12(9):e0184755, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Extracellular signal-regulated kinase 8 (ERK8), proposed as a novel potential therapeutic target for cancer, has been implicated in cell transformation, apoptosis, the protection of genomic integrity, and autophagy. To facilitate ERK8 research, a highly specific anti-ERK8 antibody is needed. In this article, we use the Immune Epitope Database and Analysis Resource online tool to predict B-cell epitopes of human ERK8 protein, and choose a 28 aa-peptide sequence to generate the GST-ERK8(28aa) fusion protein as the antigen for developing polyclonal antibody against ERK8. The specificity and sensitivity of anti-ERK8 antibody were robustly validated by immunoblotting, immunocytochemical and immunohistochemical analyses; and we found that both the endogenous and ectopically-expressed human ERK8 proteins can be recognized by our anti-ERK8 antibody. This suggested that our characterized anti-ERK8 antibody will be a valuable tool for the elucidation of the distribution of ERK8 at cellular and histological levels. Finally, our tissue array analysis also demonstrated that the ERK8 protein was localized in both the nucleus and cytoplasm of human lung cancers.
[Mh] Termos MeSH primário: Anticorpos/química
Epitopos de Linfócito B/química
MAP Quinases Reguladas por Sinal Extracelular/imunologia
Neoplasias Pulmonares/metabolismo
[Mh] Termos MeSH secundário: Anticorpos/isolamento & purificação
Especificidade de Anticorpos
Linhagem Celular Tumoral
Núcleo Celular/metabolismo
Citoplasma/metabolismo
Bases de Dados Factuais
MAP Quinases Reguladas por Sinal Extracelular/análise
Seres Humanos
Imuno-Histoquímica
Software
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Epitopes, B-Lymphocyte); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 2.7.11.24 (MAPK15 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184755


  8 / 2114 MEDLINE  
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[PMID]:28800475
[Au] Autor:Shabani SH; Zakeri S; Salmanian AH; Amani J; Mehrizi AA; Snounou G; Nosten F; Andolina C; Mourtazavi Y; Djadid ND
[Ad] Endereço:Malaria and Vector Research Group (MVRG), Biotechnology Research Center (BRC), Pasteur Institute of Iran, Pasteur Avenue, P.O. Box 1316943551, Tehran, Iran; Department of Medical Biotechnology and Nanotechnology, Faculty of Medicine, Zanjan University of Medical Sciences (ZUMS), Zanjan, Iran.
[Ti] Título:Biological, immunological and functional properties of two novel multi-variant chimeric recombinant proteins of CSP antigens for vaccine development against Plasmodium vivax infection.
[So] Source:Mol Immunol;90:158-171, 2017 Oct.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The circumsporozoite protein (CSP) of the malaria parasite Plasmodium vivax is a major pre-erythrocyte vaccine candidate. The protein has a central repeat region that belongs to one of repeat families (VK210, VK247, and the P. vivax-like). In the present study, computer modelling was employed to select chimeric proteins, comprising the conserved regions and different arrangements of the repeat elements (VK210 and VK247), whose structure is similar to that of the native counterparts. DNA encoding the selected chimeras (named CS127 and CS712) were synthetically constructed based on E. coli codons, then cloned and expressed. Mouse monoclonal antibodies (mAbs; anti-Pv-210-CDC and -Pv-247-CDC), recognized the chimeric antigens in ELISA, indicating correct conformation and accessibility of the B-cell epitopes. ELISA using IgG from plasma samples collected from 221 Iranian patients with acute P. vivax showed that only 49.32% of the samples reacted to both CS127 and CS712 proteins. The dominant subclass for the two chimeras was IgG1 (48% of the positive responders, OD =0.777±0.420 for CS127; 48.41% of the positive responders, OD =0.862±0.423 for CS712, with no statistically significant difference P>0.05; Wilcoxon signed ranks test). Binding assays showed that both chimeric proteins bound to immobilized heparan sulphate and HepG2 hepatocyte cells in a concentration-dependent manner, saturable at 80µg/mL. Additionally, anti-CS127 and -CS712 antibodies raised in mice recognized the native protein on the surface of P. vivax sporozoite with high intensity, confirming the presence of common epitopes between the recombinant forms and the native proteins. In summary, despite structural differences at the molecular level, the expression levels of both chimeras were satisfactory, and their conformational structure retained biological function, thus supporting their potential for use in the development of vivax-based vaccine.
[Mh] Termos MeSH primário: Anticorpos Antiprotozoários/imunologia
Vacinas Antimaláricas/imunologia
Malária Vivax/imunologia
Malária Vivax/prevenção & controle
Plasmodium vivax/imunologia
Proteínas de Protozoários/imunologia
Proteínas Recombinantes de Fusão/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/imunologia
Linhagem Celular Tumoral
Ensaio de Imunoadsorção Enzimática
Epitopos de Linfócito B/imunologia
Feminino
Células Hep G2
Seres Humanos
Imunização
Malária Vivax/parasitologia
Camundongos
Camundongos Endogâmicos C57BL
Ligação Proteica
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Proteínas de Protozoários/genética
Proteínas Recombinantes de Fusão/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antibodies, Protozoan); 0 (Epitopes, B-Lymphocyte); 0 (Malaria Vaccines); 0 (Protozoan Proteins); 0 (Recombinant Fusion Proteins); 0 (circumsporozoite protein, Protozoan)
[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:170812
[St] Status:MEDLINE


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[PMID]:28779686
[Au] Autor:Lau JW; Kim YI; Murphy R; Newman R; Yang X; Zody M; DeVincenzo J; Grad YH
[Ad] Endereço:Department of Immunology and Infectious Diseases, Harvard TH Chan School of Public Health, Boston, MA 02115, United States.
[Ti] Título:Deep sequencing of RSV from an adult challenge study and from naturally infected infants reveals heterogeneous diversification dynamics.
[So] Source:Virology;510:289-296, 2017 Oct.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:As RNA virus mutation occurs during replication within host cells, we hypothesized that viral evolution during acute infections in healthy hosts reflects host immune pressure. We therefore investigated the within-host diversification of human respiratory syncytial virus (RSV), a highly prevalent cause of acute respiratory infections. We evaluated healthy adults experimentally infected with an identical inoculum and infants hospitalized with naturally acquired infections. In aggregate, viral diversification in adults peaked at day 3, with overrepresentation of diversity in the matrix protein 2 (M2) and non-structural protein 2 (NS2) genes. In one subject, delayed viral clearance was accompanied by a late peak of diversity at day 10 in known and predicted B and T cell epitopes. In contrast, infant infections showed much less viral diversity. Our findings suggest multiple overlapping mechanisms for early control of acute viral infections, which may differ between age groups and host immune responses.
[Mh] Termos MeSH primário: Variação Genética
Infecções por Vírus Respiratório Sincicial/virologia
Vírus Sincicial Respiratório Humano/classificação
Vírus Sincicial Respiratório Humano/genética
[Mh] Termos MeSH secundário: Adulto
Epitopos de Linfócito B/genética
Epitopos de Linfócito T/genética
Evolução Molecular
Sequenciamento de Nucleotídeos em Larga Escala
Seres Humanos
Lactente
Mutação
Infecções por Vírus Respiratório Sincicial/imunologia
Vírus Sincicial Respiratório Humano/isolamento & purificação
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epitopes, B-Lymphocyte); 0 (Epitopes, T-Lymphocyte); 0 (Viral Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170903
[Lr] Data última revisão:
170903
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170806
[St] Status:MEDLINE


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[PMID]:28736824
[Au] Autor:Wei Y; Wahome N; VanSlyke G; Whitaker N; Kumar P; Barta ML; Picking WL; Volkin DB; Mantis NJ; Middaugh CR
[Ad] Endereço:Macromolecule and Vaccine Stabilization Center, Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, Kansas, 66047.
[Ti] Título:Evaluation of lumazine synthase from Bacillus anthracis as a presentation platform for polyvalent antigen display.
[So] Source:Protein Sci;26(10):2059-2072, 2017 Oct.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Polyvalent antigen display is an effective strategy to enhance the immunogenicity of subunit vaccines by clustering them in an array-like manner on a scaffold system. This strategy results in a higher local density of antigens, increased high avidity interactions with B cells and other antigen presenting cells, and therefore a more effective presentation of vaccine antigens. In this study, we used lumazine synthase (LS), an icosahedral symmetry capsid derived from Bacillus anthracis, as a scaffold to present 60 copies of a linear B cell epitope (PB10) from the ricin toxin fused to the C terminus of LS via four different linkers. We then investigated the effects of linker length, linker rigidity and formaldehyde crosslinking on the protein assembly, conformational integrity, thermal stability, in vitro antibody binding, and immunogenicity in mice. Fusion of the PB10 peptide onto LS, with varying linker lengths, did not affect protein assembly, thermal stability or exposure of the epitope, but had a minor impact on protein conformation. Formaldehyde crosslinking considerably improved protein thermal stability with only minor impact on protein conformation. All LS_PB10 constructs, when administered to mice by injection without adjuvant, elicited measurable anti-ricin serum IgG titers, although the titers were not sufficient to confer protection against a 10× lethal dose ricin challenge. This work sheds light on the biophysical properties, immunogenicity and potential feasibility of LS from B. anthracis as a scaffold system for polyvalent antigen display.
[Mh] Termos MeSH primário: Vacinas contra Antraz
Antígenos de Bactérias
Bacillus anthracis
Epitopos de Linfócito B
Complexos Multienzimáticos
Vacinas de Subunidades
[Mh] Termos MeSH secundário: Animais
Vacinas contra Antraz/química
Vacinas contra Antraz/genética
Vacinas contra Antraz/imunologia
Vacinas contra Antraz/metabolismo
Anticorpos Antibacterianos/sangue
Anticorpos Antibacterianos/imunologia
Antígenos de Bactérias/química
Antígenos de Bactérias/genética
Antígenos de Bactérias/imunologia
Antígenos de Bactérias/metabolismo
Bacillus anthracis/enzimologia
Bacillus anthracis/imunologia
Epitopos de Linfócito B/química
Epitopos de Linfócito B/genética
Epitopos de Linfócito B/imunologia
Epitopos de Linfócito B/metabolismo
Feminino
Imunoglobulina G/sangue
Imunoglobulina G/imunologia
Camundongos
Modelos Moleculares
Complexos Multienzimáticos/química
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/imunologia
Complexos Multienzimáticos/metabolismo
Estabilidade Proteica
Ricina/química
Ricina/genética
Ricina/imunologia
Ricina/metabolismo
Vacinas de Subunidades/química
Vacinas de Subunidades/genética
Vacinas de Subunidades/imunologia
Vacinas de Subunidades/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anthrax Vaccines); 0 (Antibodies, Bacterial); 0 (Antigens, Bacterial); 0 (Epitopes, B-Lymphocyte); 0 (Immunoglobulin G); 0 (Multienzyme Complexes); 0 (Vaccines, Subunit); 89287-46-7 (6,7-dimethyl-8-ribityllumazine synthase); 9009-86-3 (Ricin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3243



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