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  1 / 59796 MEDLINE  
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[PMID]:29377916
[Au] Autor:Tutykhina I; Esmagambetov I; Bagaev A; Pichugin A; Lysenko A; Shcherbinin D; Sedova E; Logunov D; Shmarov M; Ataullakhanov R; Naroditsky B; Gintsburg A
[Ad] Endereço:Federal Research Centre of Epidemiology and Microbiology named after Honorary Academician N. F. Gamaleya, Ministry of Health, Moscow, Russia.
[Ti] Título:Vaccination potential of B and T epitope-enriched NP and M2 against Influenza A viruses from different clades and hosts.
[So] Source:PLoS One;13(1):e0191574, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To avoid outbreaks of influenza virus epidemics and pandemics among human populations, modern medicine requires the development of new universal vaccines that are able to provide protection from a wide range of influenza A virus strains. In the course of development of a universal vaccine, it is necessary to consider that immunity must be generated even against viruses from different hosts because new human epidemic virus strains have their origins in viruses of birds and other animals. We have enriched conserved viral proteins-nucleoprotein (NP) and matrix protein 2 (M2)-by B and T-cell epitopes not only human origin but also swine and avian origin. For this purpose, we analyzed M2 and NP sequences with respect to changes in the sequences of known T and B-cell epitopes and chose conserved and evolutionarily significant epitopes. Eventually, we found consensus sequences of M2 and NP that have the maximum quantity of epitopes that are 100% coincident with them. Consensus epitope-enriched amino acid sequences of M2 and NP proteins were included in a recombinant adenoviral vector. Immunization with Ad5-tet-M2NP induced strong CD8 and CD4 T cells responses, specific to each of the encoded antigens, i.e. M2 and NP. Eight months after immunization with Ad5-tet-M2NP, high numbers of M2- and NP-responding "effector memory" CD44posCD62neg T cells were found in the mouse spleens, which revealed a long-term T cell immune memory conferred by the immunization. In all, the challenge experiments showed an extraordinarily wide-ranging efficacy of protection by the Ad5-tet-M2NP vaccine, covering 5 different heterosubtypes of influenza A virus (2 human, 2 avian and 1 swine).
[Mh] Termos MeSH primário: Linfócitos B/imunologia
Epitopos/imunologia
Vírus da Influenza A/imunologia
Nucleoproteínas/imunologia
Linfócitos T/imunologia
Vacinação
Proteínas da Matriz Viral/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Antivirais/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Epitopes); 0 (Nucleoproteins); 0 (Viral Matrix Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180130
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191574


  2 / 59796 MEDLINE  
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[PMID]:29231143
[Au] Autor:Vazquez-Prieto S; Paniagua E; Solana H; Ubeira FM
[Ad] Endereço:Laboratorio de Biologia Celular y Molecular, Centro de Investigacion Veterinaria de Tandil (CIVETAN), CONICET, Facultad de Ciencias Veterinarias, UNCPBA, Tandil, Argentina.
[Ti] Título:Complex Network Study of the Immune Epitope Database for Parasitic Organisms.
[So] Source:Curr Top Med Chem;17(30):3249-3255, 2018 Feb 09.
[Is] ISSN:1873-4294
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Complex network approach allows the representation and analysis of complex systems of interacting agents in an ordered and effective manner, thus increasing the probability of discovering significant properties of them. In the present study, we defined and built for the first time a complex network based on data obtained from Immune Epitope Database for parasitic organisms. We then considered the general topology, the node degree distribution, and the local structure (triadic census) of this network. In addition, we calculated 9 node centrality measures for observed network and reported a comparative study of the real network with three theoretical models to detect similarities or deviations from these ideal networks. RESULT: The results obtained corroborate the utility of the complex network approach for handling information and data mining within the database under study. CONCLUSION: They confirm that this type of approach can be considered a valuable tool for preliminary screening of the best experimental conditions to determine whether the amino acid sequences being studied are true epitopes or not.
[Mh] Termos MeSH primário: Bases de Dados Factuais
Epitopos/química
Epitopos/imunologia
Redes Neurais (Computação)
Parasitos/química
Parasitos/imunologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Mineração de Dados
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epitopes)
[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:171213
[St] Status:MEDLINE
[do] DOI:10.2174/1568026618666171211150605


  3 / 59796 MEDLINE  
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[PMID]:28461065
[Au] Autor:Hu D; Bowder D; Wei W; Thompson J; Wilson MA; Xiang SH
[Ad] Endereço:Nebraska Center for Virology, University of Nebraska-Lincoln, Lincoln, NE 68583, United States; School of Veterinary Medicine and Biomedical Sciences, University of Nebraska-Lincoln, Lincoln, NE 68583, United States.
[Ti] Título:Tryptophan 375 stabilizes the outer-domain core of gp120 for HIV vaccine immunogen design.
[So] Source:Vaccine;35(23):3067-3075, 2017 05 25.
[Is] ISSN:1873-2518
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The outer-domain core of gp120 may serve as a better HIV vaccine immunogen than the full-length gp120 because of its greater stability and immunogenicity. In our previous report, we introduced two disulfide bonds to the outer-domain core of gp120 to fix its conformation into a CD4-bound state, which resulted in a significant increase in its immunogenicity when compared to the wild-type outer-domain core. In this report, to further improve the immunogenicity of the outer-domain core based immunogen, we have introduced a Tryptophan residue at gp120 amino acid sequence position 375 (375S/W). Our data from immunized guinea pigs indeed shows a striking increase in the immune response due to this stabilized core outer-domain. Therefore, we conclude that the addition of 375W to the outer-domain core of gp120 further stabilizes the structure of immunogen and increases the immunogenicity.
[Mh] Termos MeSH primário: Vacinas contra a AIDS/imunologia
Anticorpos Anti-HIV/imunologia
Proteína gp120 do Envelope de HIV/química
Proteína gp120 do Envelope de HIV/imunologia
Imunogenicidade da Vacina
Triptofano/química
[Mh] Termos MeSH secundário: Vacinas contra a AIDS/administração & dosagem
Vacinas contra a AIDS/química
Substituição de Aminoácidos
Animais
Anticorpos Neutralizantes/imunologia
Antígenos CD4
Desenho de Drogas
Epitopos/química
Cobaias
Anticorpos Anti-HIV/sangue
HIV-1/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AIDS Vaccines); 0 (Antibodies, Neutralizing); 0 (CD4 Antigens); 0 (Epitopes); 0 (HIV Antibodies); 0 (HIV Envelope Protein gp120); 8DUH1N11BX (Tryptophan)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  4 / 59796 MEDLINE  
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[PMID]:28456528
[Au] Autor:Jiang P; Cai Y; Chen J; Ye X; Mao S; Zhu S; Xue X; Chen S; Zhang L
[Ad] Endereço:Institute of Molecular Virology and Immunology, Department of Microbiology and Immunology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou 325035, Zhejiang, PR China.
[Ti] Título:Evaluation of tandem Chlamydia trachomatis MOMP multi-epitopes vaccine in BALB/c mice model.
[So] Source:Vaccine;35(23):3096-3103, 2017 05 25.
[Is] ISSN:1873-2518
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Chlamydia trachomatis (Ct), an obligate intracellular parasite, is the leading cause of bacterial sexually transmitted diseases worldwide. The best solution to control the spread of Ct is to develop safe and effective vaccines. However, an effective vaccine has not been developed due to some challenges such as selection of appropriate candidate antigens and an effective delivery system. In our previous study, we have developed a Ct vaccine that comprises a multi-epitope peptide of Ct major outer membrane protein (MOMP ) and Hepatitis B virus core antigen (HBcAg). The vaccine was evaluated in a murine model with chlamydial genital infection. The results indicated that Ct MOMP multi-epitope delivered by HBcAg could be an effective vaccine for the prevention of Ct. In this study, another two epitopes were selected from the MOMP protein and tandemly linked with MOMP to enhance the immunogenicity and the protective effect of the candidate vaccine. Our results revealed that both the immunogenicity and the protective effect of the tandem Ct MOMP multi-epitopes were much better than that of the single epitope. Therefore, vaccines based on the tandem Ct MOMP multi-epitopes could be more effective immune prophylactics to prevent Ct infection than the single epitope in murine model system.
[Mh] Termos MeSH primário: Vacinas Bacterianas/imunologia
Infecções por Chlamydia/prevenção & controle
Chlamydia trachomatis/imunologia
Epitopos/imunologia
Porinas/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Antibacterianos/sangue
Vacinas Bacterianas/administração & dosagem
Vacinas Bacterianas/química
Infecções por Chlamydia/microbiologia
Chlamydia trachomatis/química
Modelos Animais de Doenças
Epitopos/química
Feminino
Imunogenicidade da Vacina
Camundongos
Camundongos Endogâmicos BALB C
Porinas/química
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Bacterial); 0 (Bacterial Vaccines); 0 (Epitopes); 0 (Porins); 146409-23-6 (omp1 protein, Chlamydia trachomatis)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


  5 / 59796 MEDLINE  
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[PMID]:28453838
[Au] Autor:Lindesmith LC; Mallory ML; Jones TA; Richardson C; Goodwin RR; Baehner F; Mendelman PM; Bargatze RF; Baric RS
[Ad] Endereço:Department of Epidemiology, University of North Carolina, Chapel Hill, NC, USA.
[Ti] Título:Impact of Pre-exposure History and Host Genetics on Antibody Avidity Following Norovirus Vaccination.
[So] Source:J Infect Dis;215(6):984-991, 2017 03 15.
[Is] ISSN:1537-6613
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Background: Development of high avidity, broadly neutralizing antibodies (Abs) is a priority after vaccination against rapidly evolving, widely disseminated viruses like human norovirus. After vaccination with a multivalent GI.1 and GII.4c norovirus virus-like particle (VLP) vaccine candidate adjuvanted with alum and monophosphoryl lipid A (MPL), blockade Ab titers peaked early, with no increase in titer following a second vaccine dose. Methods: Blockade Ab relative avidity was evaluated by measuring the slope of blockade Ab neutralization curves. Results: Blockade Ab avidity to the GI.1 vaccine component peaked at day 35 (7 days after dose 2). Avidities to heterotypic genogroup I VLPs were not sustained at day 35 after vaccination or GI.1 infection, as measured from archived sera. Only secretor-positive participants maintained high avidity blockade Ab to GI.1 at day 180. Avidity to the GII.4c vaccine component peaked at day 7, remained elevated through day 180, and was not secretor dependent. Avidity to an immunologically novel GII.4 strain VLP correlated with preexisting Ab titer to an ancestral strain Epitope A. Conclusions: Host genetics and pre-exposure history shape norovirus vaccine Ab responses, including blockade Ab avidity. Avidity of potentially neutralizing Ab may be an important metric for evaluating vaccine responses to highly penetrant viruses with cross-reactive serotypes.
[Mh] Termos MeSH primário: Afinidade de Anticorpos
Infecções por Caliciviridae/prevenção & controle
Vacinas de Partículas Semelhantes a Vírus/uso terapêutico
Vacinas Virais/uso terapêutico
[Mh] Termos MeSH secundário: Adjuvantes Imunológicos/administração & dosagem
Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Anticorpos Neutralizantes/sangue
Anticorpos Antivirais/sangue
Infecções por Caliciviridae/genética
Reações Cruzadas
Método Duplo-Cego
Epitopos/imunologia
Feminino
Seres Humanos
Masculino
Meia-Idade
Norovirus
Estados Unidos
Vacinação
Vacinas de Partículas Semelhantes a Vírus/administração & dosagem
Vacinas Virais/administração & dosagem
Adulto Jovem
[Pt] Tipo de publicação:CLINICAL TRIAL, PHASE I; JOURNAL ARTICLE; MULTICENTER STUDY; RANDOMIZED CONTROLLED TRIAL
[Nm] Nome de substância:
0 (Adjuvants, Immunologic); 0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Epitopes); 0 (Vaccines, Virus-Like Particle); 0 (Viral Vaccines)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1093/infdis/jix045


  6 / 59796 MEDLINE  
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[PMID]:29295972
[Au] Autor:Jabs F; Plum M; Laursen NS; Jensen RK; Mølgaard B; Miehe M; Mandolesi M; Rauber MM; Pfützner W; Jakob T; Möbs C; Andersen GR; Spillner E
[Ad] Endereço:Immunological Engineering, Department of Engineering, Aarhus University, 8000, Aarhus, Denmark.
[Ti] Título:Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction.
[So] Source:Nat Commun;9(1):7, 2018 01 02.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Anti-IgE therapeutics interfere with the ability of IgE to bind to its receptors on effector cells. Here we report the crystal structure of an anti-IgE single-domain antibody in complex with an IgE Fc fragment, revealing how the antibody inhibits interactions between IgE and the two receptors FcεRI and CD23. The epitope overlaps only slightly with the FcεRI-binding site but significantly with the CD23-binding site. Solution scattering studies of the IgE Fc reveal that antibody binding induces a half-bent conformation in between the well-known bent and extended IgE Fc conformations. The antibody acts as functional homolog of CD23 and induces a closed conformation of IgE Fc incompatible with FcεRI binding. Notably the antibody displaces IgE from both CD23 and FcεRI, and abrogates allergen-mediated basophil activation and facilitated allergen binding. The inhibitory mechanism might facilitate strategies for the future development of anti-IgE therapeutics for treatment of allergic diseases.
[Mh] Termos MeSH primário: Epitopos/química
Imunoglobulina E/química
Receptores de IgE/química
[Mh] Termos MeSH secundário: Anticorpos Anti-Idiotípicos/química
Anticorpos Anti-Idiotípicos/metabolismo
Sítios de Ligação
Cristalografia por Raios X
Epitopos/metabolismo
Seres Humanos
Imunoglobulina E/metabolismo
Fragmentos Fc das Imunoglobulinas/química
Fragmentos Fc das Imunoglobulinas/metabolismo
Modelos Moleculares
Ligação Proteica
Conformação Proteica
Receptores de IgE/metabolismo
Anticorpos de Domínio Único/química
Anticorpos de Domínio Único/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Anti-Idiotypic); 0 (Epitopes); 0 (Immunoglobulin Fc Fragments); 0 (Receptors, IgE); 0 (Single-Domain Antibodies); 0 (anti-IgE antibodies); 37341-29-0 (Immunoglobulin E)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02312-7


  7 / 59796 MEDLINE  
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[PMID]:28741733
[Au] Autor:Tsukamoto H; Yamagata Y; Ukai I; Takeuchi S; Okubo M; Kobayashi Y; Kozakai S; Kubota K; Numasaki M; Kanemitsu Y; Matsumoto Y; Tomioka Y
[Ad] Endereço:Laboratory of Oncology, Pharmacy Practice and Sciences, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
[Ti] Título:An inhibitory epitope of human Toll-like receptor 4 resides on leucine-rich repeat 13 and is recognized by a monoclonal antibody.
[So] Source:FEBS Lett;591(16):2406-2416, 2017 08.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lipopolysaccharide (LPS)-induced activation of Toll-like receptor 4 (TLR4) elicits the innate immune response and can trigger septic shock if excessive. Two antibodies (HT4 and HT52) inhibit LPS-induced human TLR4 activation via novel LPS binding-independent mechanisms. The HT52 epitope resides on leucine-rich repeat 2 (LRR2) and is a feature of many inhibitory antibodies; antigen specificity of HT4 does not reside in LRR2. Here, we identified an HT4 epitope on LRR13 located close to the TLR4 dimerization interface that plays a role in NFκB activation. HT4 and HT52 mutually enhanced TLR4 inhibition. LRR13 is a novel inhibitory epitope and may be useful for developing anti-TLR4 antibodies. Combination therapy with LRR2 and LRR13 may effectively inhibit TLR4 activation.
[Mh] Termos MeSH primário: Motivos de Aminoácidos
Anticorpos Monoclonais/imunologia
Epitopos/imunologia
Receptor 4 Toll-Like/química
Receptor 4 Toll-Like/imunologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Seres Humanos
Lipopolissacarídeos/farmacologia
Camundongos
Multimerização Proteica
Estrutura Quaternária de Proteína
Receptor 4 Toll-Like/metabolismo
[Pt] Tipo de publicação:LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Epitopes); 0 (Lipopolysaccharides); 0 (TLR4 protein, human); 0 (Toll-Like Receptor 4)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12768


  8 / 59796 MEDLINE  
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[PMID]:28741237
[Au] Autor:Zhand S; Tabarraei A; Nazari A; Moradi A
[Ad] Endereço:Department of Microbiology, School of Medicine, Golestan University of Medical Sciences, Gorgan, Iran.
[Ti] Título:Cytotoxic T lymphocytes and CD4 epitope mutations in the pre-core/core region of hepatitis B virus in chronic hepatitis B carriers in Northeast Iran.
[So] Source:Indian J Gastroenterol;36(4):253-257, 2017 Jul.
[Is] ISSN:0975-0711
[Cp] País de publicação:India
[La] Idioma:eng
[Ab] Resumo:BACKGROUNDS: Hepatitis B virus (HBV) is vulnerable to many various mutations. Those within epitopes recognized by sensitized T cells may influence the re-emergence of the virus. This study was designed to investigate the mutation in immune epitope regions of HBV pre-core/core among chronic HBV patients of Golestan province, Northeast Iran. METHODS: In 120 chronic HBV carriers, HBV DNA was extracted from blood plasma samples and PCR was done using specific primers. Direct sequencing and alignment of the pre-core/core region were applied using reference sequence from Gene Bank database (Accession Number AB033559). RESULTS: The study showed 27 inferred amino acid substitutions, 9 of which (33.3%) were in CD4 and 2 (7.4%) in cytotoxic T lymphocytes' (CTL) epitopes and 16 other mutations (59.2%) were observed in other regions. CONCLUSIONS: CTL escape mutations were not commonly observed in pre-core/core sequences of chronic HBV carriers in the locale of study. It can be concluded that most of the inferred amino acid substitutions occur in different immune epitopes other than CTL and CD4.
[Mh] Termos MeSH primário: Antígenos CD4/genética
Portador Sadio/virologia
Epitopos/genética
Vírus da Hepatite B/genética
Vírus da Hepatite B/imunologia
Hepatite B Crônica/virologia
Mutação Puntual
Linfócitos T Citotóxicos/imunologia
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Portador Sadio/imunologia
Epitopos/química
Epitopos/imunologia
Hepatite B Crônica/imunologia
Seres Humanos
Irã (Geográfico)
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD4 Antigens); 0 (Epitopes)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1007/s12664-017-0767-z


  9 / 59796 MEDLINE  
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[PMID]:29329339
[Au] Autor:Granger BL
[Ad] Endereço:Department of Microbiology and Immunology, Montana State University, Bozeman, Montana, United States of America.
[Ti] Título:Accessibility and contribution to glucan masking of natural and genetically tagged versions of yeast wall protein 1 of Candida albicans.
[So] Source:PLoS One;13(1):e0191194, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Yeast wall protein 1 (Ywp1) is an abundant glycoprotein of the cell wall of the yeast form of Candida albicans, the most prevalent fungal pathogen of humans. Antibodies that bind to the polypeptide backbone of isolated Ywp1 show little binding to intact yeast cells, presumably because the Ywp1 epitopes are masked by the polysaccharides of the mannoproteins that form the outer layer of the cell wall. Rare cells do exhibit much greater anti-Ywp1 binding, however, and one of these was isolated and characterized. No differences were seen in its Ywp1, but it exhibited greater adhesiveness, sensitivity to wall perturbing agents, and exposure of its underlying ß-1,3-glucan layer to external antibodies. The molecular basis for this greater epitope accessibility has not been determined, but has facilitated exploration of how these properties change as a function of cell growth and morphology. In addition, previously engineered strains with reduced quantities of Ywp1 in their cell walls were also found to have greater ß-1,3-glucan exposure, indicating that Ywp1 itself contributes to the masking of wall epitopes, which may be important for understanding the anti-adhesive effect of Ywp1. Ectopic production of Ywp1 by hyphae, which reduces the adhesivity of these filamentous forms of C. albicans, was similarly found to reduce exposure of the ß-1,3-glucan in their walls. To monitor Ywp1 in the cell wall irrespective of its accessibility, green fluorescent protein (Gfp) was genetically inserted into wall-anchored Ywp1 using a bifunctional cassette that also allowed production from a single transfection of a soluble, anchor-free version. The wall-anchored Ywp1-Gfp-Ywp1 accumulated in the wall of the yeast forms but not hyphae, and appeared to have properties similar to native Ywp1, including its adhesion-inhibiting effect. Some pseudohyphal walls also detectably accumulated this probe. Strains of C. albicans with tandem hemagglutinin (HA) epitopes inserted into wall-anchored Ywp1 were previously created by others, and were further explored here. As above, rare cells with much greater accessibility of the HA epitopes were isolated, and also found to exhibit greater exposure of Ywp1 and ß-1,3-glucan. The placement of the HA cassette inhibited the normal N-glycosylation and propeptide cleavage of Ywp1, but the wall-anchored Ywp1-HA-Ywp1 still accumulated in the cell wall of yeast forms. Bifunctional transformation cassettes were used to additionally tag these molecules with Gfp, generating soluble Ywp1-HA-Gfp and wall-anchored Ywp1-HA-Gfp-Ywp1 molecules. The former revealed unexpected electrophoretic properties caused by the HA insertion, while the latter further highlighted differences between the presence of a tagged Ywp1 molecule (as revealed by Gfp fluorescence) and its accessibility in the cell wall to externally applied antibodies specific for HA, Gfp and Ywp1, with accessibility being greatest in the rapidly expanding walls of budding daughter cells. These strains and results increase our understanding of cell wall properties and how C. albicans masks itself from recognition by the human immune system.
[Mh] Termos MeSH primário: Candida albicans/genética
Candida albicans/metabolismo
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
beta-Glucanas/metabolismo
[Mh] Termos MeSH secundário: Anticorpos Antifúngicos
Antígenos de Fungos/química
Antígenos de Fungos/genética
Antígenos de Fungos/metabolismo
Candida albicans/imunologia
Parede Celular/genética
Parede Celular/imunologia
Parede Celular/metabolismo
Epitopos/química
Epitopos/genética
Epitopos/metabolismo
Proteínas Fúngicas/imunologia
Glicosilação
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/imunologia
Proteínas de Fluorescência Verde/metabolismo
Hemaglutininas/genética
Hemaglutininas/imunologia
Hemaglutininas/metabolismo
Seres Humanos
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/imunologia
Glicoproteínas de Membrana/metabolismo
Engenharia de Proteínas
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/imunologia
Proteínas Recombinantes de Fusão/metabolismo
beta-Glucanas/química
beta-Glucanas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Fungal); 0 (Antigens, Fungal); 0 (Epitopes); 0 (Fungal Proteins); 0 (Hemagglutinins); 0 (Membrane Glycoproteins); 0 (Recombinant Fusion Proteins); 0 (beta-Glucans); 0 (mannoproteins); 147336-22-9 (Green Fluorescent Proteins); 9051-97-2 (beta-1,3-glucan)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191194


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[PMID]:28465158
[Au] Autor:Muñoz-Alía MA; Casasnovas JM; Celma ML; Carabaña J; Liton PB; Fernandez-Muñoz R
[Ad] Endereço:Virology Unit, Ramón y Cajal Hospital, Madrid, Spain.
[Ti] Título:Measles Virus Hemagglutinin epitopes immunogenic in natural infection and vaccination are targeted by broad or genotype-specific neutralizing monoclonal antibodies.
[So] Source:Virus Res;236:30-43, 2017 05 15.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Measles virus (MV) remains a leading cause of vaccine-preventable deaths in children. Protection against MV is associated with neutralizing antibodies that preferentially recognize the viral hemagglutinin (MV-H), and to a lesser extent, the fusion protein (MV-F). Although MV is serologically monotypic, 24 genotypes have been identified. Here we report three neutralization epitopes conserved in the more prevalent circulating MV genotypes, two located in the MV-H receptor binding site (RBS) (antigenic site III) and a third in MV-H/MV-F interphase (antigenic site Ia) which are essential for MV multiplication. In contrast, two MV-H neutralization epitopes, showed a genotype-specific neutralization escape due to a single amino acid change, that we mapped in the "noose" antigenic site, or an enhanced neutralization epitope (antigenic site IIa). The monoclonal antibody (mAb) neutralization potency correlated with its binding affinity and was mainly driven by kinetic dissociation rate (k ). We developed an immunoassay for mAb binding to MV-H in its native hetero-oligomeric structure with MV-F on the surface of a MV productive steady-state persistently infected (p.i.) human cell lines, and a competitive-binding assay with serum from individuals with past infection by different MV genotypes. Binding assays revealed that a broad neutralization epitope, in RBS antigenic site, a genotype specific neutralization epitopes, in noose and IIa sites, were immunogenic in natural infection and vaccination and may elicit long-lasting humoral immunity that might contribute to explain MV immunogenic stability. These results support the design of improved measles vaccines, broad-spectrum prophylactic or therapeutic antibodies and MV-used in oncolytic therapies.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/imunologia
Anticorpos Antivirais/imunologia
Hemaglutininas Virais/imunologia
Vírus do Sarampo/imunologia
Sarampo/imunologia
[Mh] Termos MeSH secundário: Anticorpos Neutralizantes/imunologia
Epitopos/administração & dosagem
Epitopos/imunologia
Genótipo
Hemaglutininas Virais/administração & dosagem
Hemaglutininas Virais/genética
Seres Humanos
Sarampo/prevenção & controle
Sarampo/virologia
Vacina contra Sarampo/administração & dosagem
Vacina contra Sarampo/imunologia
Vírus do Sarampo/classificação
Vírus do Sarampo/genética
Vírus do Sarampo/isolamento & purificação
Testes de Neutralização
Vacinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Epitopes); 0 (Hemagglutinins, Viral); 0 (Measles Vaccine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE



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