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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


  2 / 7348 MEDLINE  
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[PMID]:29346393
[Au] Autor:Hollingsworth LR; Brown AM; Gandour RD; Bevan DR
[Ad] Endereço:Department of Chemical Engineering, Virginia Tech, Blacksburg, Virginia, United States of America.
[Ti] Título:Computational study of HIV gp120 as a target for polyanionic entry inhibitors: Exploiting the V3 loop region.
[So] Source:PLoS One;13(1):e0190658, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Multiple approaches are being utilized to develop therapeutics to treat HIV infection. One approach is designed to inhibit entry of HIV into host cells, with a target being the viral envelope glycoprotein, gp120. Polyanionic compounds have been shown to be effective in inhibiting HIV entry, with a mechanism involving electrostatic interactions with the V3 loop of gp120 being proposed. In this study, we applied computational methods to elucidate molecular interactions between the repeat unit of the precisely alternating polyanion, Poly(4,4'-stilbenedicarboxylate-alt-maleic acid) (DCSti-alt-MA) and the V3 loop of gp120 from strains of HIV against which these polyanions were previously tested (IIIb, BaL, 92UG037, JR-CSF) as well as two strains for which gp120 crystal structures are available (YU2, 2B4C). Homology modeling was used to create models of the gp120 proteins. Using monomers of the gp120 protein, we applied extensive molecular dynamics simulations to obtain dominant morphologies that represent a variety of open-closed states of the V3 loop to examine the interaction of 112 ligands of the repeating units of DCSti-alt-MA docked to the V3 loop and surrounding residues. Using the distance between the V1/V2 and V3 loops of gp120 as a metric, we revealed through MD simulations that gp120 from the lab-adapted strains (BaL and IIIb), which are more susceptible to inhibition by DCSti-alt-MA, clearly transitioned to the closed state in one replicate of each simulation set, whereas none of the replicates from the Tier II strains (92UG037 and JR-CSF) did so. Docking repeat unit microspecies to the gp120 protein before and after MD simulation enabled identification of residues that were key for binding. Notably, only a few residues were found to be important for docking both before and after MD simulation as a result of the conformational heterogeneity provided by the simulations. Consideration of the residues that were consistently involved in interactions with the ligand revealed the importance of both hydrophilic and hydrophobic moieties of the ligand for effective binding. The results also suggest that polymers of DCSti-alt-MA with repeating units of different configurations may have advantages for therapeutic efficacy.
[Mh] Termos MeSH primário: Proteína gp120 do Envelope de HIV/metabolismo
Inibidores da Fusão de HIV/farmacologia
Polímeros/metabolismo
[Mh] Termos MeSH secundário: Proteína gp120 do Envelope de HIV/química
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HIV Envelope Protein gp120); 0 (HIV Fusion Inhibitors); 0 (Polymers); 0 (polyanions)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190658


  3 / 7348 MEDLINE  
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[PMID]:29273432
[Au] Autor:Khrustalev VV; Khrustaleva TA; Kahanouskaya EY; Rudnichenko YA; Bandarenka HV; Arutyunyan AM; Girel KV; Khinevich NV; Ksenofontov AL; Kordyukova LV
[Ad] Endereço:Department of General Chemistry, Belarusian State Medical University, Dzerzinskogo 83, Minsk, Belarus. Electronic address: vvkhrustalev@mail.ru.
[Ti] Título:The alpha helix 1 from the first conserved region of HIV1 gp120 is reconstructed in the short NQ21 peptide.
[So] Source:Arch Biochem Biophys;638:66-75, 2018 01 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Investigations of short peptides that can be used in the next phase of synthetic HIV1 vaccine development are an urgent goal, as well as investigations of peptides that can be used in immunological tests with the aim to check the titer of antibodies against the alpha helix 1 from the first conserved region of HIV1 gp120 that are known to cause antibody-dependent cellular cytotoxicity (ADCC). The aim of this work was to study the structure of the NQ21 peptide corresponding to the less mutable part of the first conserved region of HIV1 gp120 (residues 94-114). The NQ21 peptide and its conjugate with biotin (biotin-NQ21) are absolutely alpha-helical in phosphate buffer solutions at pH = 6.8, 7.4 and 8.0, as well as in the dried form, according to the results of surface-enhanced Raman scattering (SERS) spectroscopy. Results of the native gel electrophoresis and thermal analysis under the control of spectrofluorometer and near UV circular dichroism (CD) showed that the peptide exists in form of octamers and tetramers at pH = 7.4, that is important information for further vaccine development. Strong signal of interacting Trp residues in oligomers in the far UV CD obscures the signal from secondary structure, but becomes less intensive during the heating.
[Mh] Termos MeSH primário: Proteína gp120 do Envelope de HIV/química
HIV-1/química
Peptídeos/química
[Mh] Termos MeSH secundário: Vacinas contra a AIDS/química
Dicroísmo Circular
Concentração de Íons de Hidrogênio
Estrutura Secundária de Proteína
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AIDS Vaccines); 0 (HIV Envelope Protein gp120); 0 (Peptides); 0 (gp120 protein, Human immunodeficiency virus 1)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171224
[St] Status:MEDLINE


  4 / 7348 MEDLINE  
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[PMID]:27771810
[Au] Autor:Conceição de Souza R; de Medeiros Muniz G; Siqueira AS; de Melo Lima A; da Silva AP; Gonçalves EC; da Silva Gonçalves Vianez Júnior JL
[Ad] Endereço:Center for Technological Innovation, Evandro Chagas Institute, Ministry of Health, Ananindeua, PA, 67030-000, Brazil.
[Ti] Título:Investigating the effects of point mutations on the affinity between the cyanobacterial lectin microvirin and high mannose-type glycans present on the HIV envelope glycoprotein.
[So] Source:J Mol Model;22(11):269, 2016 Nov.
[Is] ISSN:0948-5023
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Human immunodeficiency virus (HIV) infections continue to exert an enormous impact on global human health. This led experts to emphasize the importance of new measures for preventing HIV infections, including the development of vaccines and novel drugs. In this context, a promising approach involves the use of lectins that can bind the surface envelope glycoprotein gp120 of HIV with high affinity, preventing viral entry. The cyanobacterial lectin microvirin (MVN) has been proposed as a candidate for development as a topical microbicide because of its ability to bind to high mannose-type glycans, potently inhibiting HIV-1 entry. Thus, the aim of this computational study was to investigate the effects of four point mutations (D53Q, D53E, D53K, and D53W) on the structure and affinity of MVN with di-mannose (MAN). Molecular dynamics simulations followed by binding free energy calculations using MM-GBSA were employed. The calculated binding free energy of ligand-receptor complexation of MVN with MAN was -26.02 kcal mol . We identified in the wild-type protein that residues I45, T59, and Q81 have a major contribution to the binding free energy of di-mannose. Among the investigated mutants, the most promising one was the D53W mutation, with a theoretical binding free energy value of -29.16 kcal mol . We suggest that this increased stability is due to the introduction of extra rigidity on the hinge region connecting two key structural elements of the MVN binding site.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Cianobactérias/química
Proteína gp120 do Envelope de HIV/química
HIV-1/química
Lectina de Ligação a Manose/química
Simulação de Dinâmica Molecular
Mutação Puntual
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Proteínas de Bactérias/genética
Sítios de Ligação
Proteína gp120 do Envelope de HIV/genética
HIV-1/genética
Lectina de Ligação a Manose/genética
Simulação de Acoplamento Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (HIV Envelope Protein gp120); 0 (Mannose-Binding Lectin); 0 (gp120 protein, Human immunodeficiency virus 1)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  5 / 7348 MEDLINE  
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[PMID]:28468877
[Au] Autor:Buranapraditkun S; Pissani F; Teigler JE; Schultz BT; Alter G; Marovich M; Robb ML; Eller MA; Martin J; Deeks S; Michael NL; Streeck H
[Ad] Endereço:U.S. Military HIV Research Program, Walter Reed Army Institute of Research, Silver Spring, Maryland, USA.
[Ti] Título:Preservation of Peripheral T Follicular Helper Cell Function in HIV Controllers.
[So] Source:J Virol;91(14), 2017 Jul 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The maturation process of high-affinity antibodies is a result of intricate interactions between B cells and follicular helper T (Tfh) cells occurring in lymphoid germinal centers. HIV infection induces significant chronic immune activation, phenotypic skewing, and inflammation driven by years of continuous viral replication. High levels of viremia as well as immune activation and dysfunction have been demonstrated to have a perturbing impact on the B cell memory compartment and contribute to B cell exhaustion. Counterintuitively, the factors associated with perturbation of the B cell compartment seem to be favorable for the generation of highly affinity-matured Env-specific antibodies in a minority of HIV-infected individuals. Thus, the impact of HIV antigenemia on B cells and Tfh cell interactions warrants further exploration. We therefore studied immunophenotypes of HIV-specific B cells in individuals with differing levels of viral control using HIV Env gp120 probes and characterized the functionality of matched T cells in peripheral blood. While CXCR5 CD4 T cells were significantly diminished in HIV progressors, we found that a small subset of gp120-specific interleukin-21 (IL-21)-secreting CXCR5 CD4 T cells were significantly associated with gp120-specific B cell frequencies. In contrast, neither bulk CXCR5 CD4 T cells nor other HIV antigen specificities were associated with gp120-specific B cell levels. HIV-specific B cells derived from elite controllers displayed greater amounts of gp120-specific B cells in the resting memory subset, whereas HIV-specific B cells in progressors accumulated in tissue-like and activated memory subsets. Furthermore, CXCR5 CD4 T cells from elite controllers showed a stronger capacity to induce B cell maturation and immunoglobulin class switching than cells from HIV progressors. Dissecting the factors that are involved in B cell maturation and antibody development is important for HIV vaccine design. In this study, we found that HIV Env-specific CXCR5 CD4 T cells that secrete interleukin-21 are strongly associated with B cell memory phenotypes and function. Moreover, we found that the immune responses of HIV controllers showed intrinsically better helper activity than those of HIV progressors.
[Mh] Termos MeSH primário: Linfócitos B/imunologia
Centro Germinativo/imunologia
Proteína gp120 do Envelope de HIV/imunologia
Infecções por HIV/imunologia
Sobreviventes de Longo Prazo ao HIV
Linfócitos T Auxiliares-Indutores/imunologia
[Mh] Termos MeSH secundário: Adulto
Linfócitos T CD4-Positivos/química
Linfócitos T CD4-Positivos/imunologia
Feminino
Seres Humanos
Imunofenotipagem
Interleucinas/secreção
Masculino
Meia-Idade
Receptores CXCR5/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CXCR5 protein, human); 0 (HIV Envelope Protein gp120); 0 (Interleukins); 0 (Receptors, CXCR5); 0 (interleukin-21)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  6 / 7348 MEDLINE  
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[PMID]:29049306
[Au] Autor:Jiang X; Feyertag F; Robertson DL
[Ad] Endereço:Evolution & Genomic Sciences, School of Biological Sciences, Faculty of Life Sciences, University of Manchester, Manchester, United Kingdom.
[Ti] Título:Protein structural disorder of the envelope V3 loop contributes to the switch in human immunodeficiency virus type 1 cell tropism.
[So] Source:PLoS One;12(10):e0185790, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human immunodeficiency virus type 1 (HIV-1) envelope gp120 is partly an intrinsically disordered (unstructured/disordered) protein as it contains regions that do not fold into well-defined protein structures. These disordered regions play important roles in HIV's life cycle, particularly, V3 loop-dependent cell entry, which determines how the virus uses two coreceptors on immune cells, the chemokine receptors CCR5 (R5), CXCR4 (X4) or both (R5X4 virus). Most infecting HIV-1 variants utilise CCR5, while a switch to CXCR4-use occurs in the majority of infections. Why does this 'rewiring' event occur in HIV-1 infected patients? As changes in the charge of the V3 loop are associated with this receptor switch and it has been suggested that charged residues promote structure disorder, we hypothesise that the intrinsic disorder of the V3 loop is permissive to sequence variation thus contributing to the switch in cell tropism. To test this we use three independent data sets of gp120 to analyse V3 loop disorder. We find that the V3 loop of X4 virus has significantly higher intrinsic disorder tendency than R5 and R5X4 virus, while R5X4 virus has the lowest. These results indicate that structural disorder plays an important role in HIV-1 cell tropism and CXCR4 binding. We discuss the potential evolutionary mechanisms leading to the fixation of disorder promoting mutations and the adaptive potential of protein structural disorder in viral host adaptation.
[Mh] Termos MeSH primário: Proteína gp120 do Envelope de HIV/metabolismo
HIV-1/fisiologia
Proteínas Virais/fisiologia
[Mh] Termos MeSH secundário: Proteína gp120 do Envelope de HIV/química
Infecções por HIV/metabolismo
Seres Humanos
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HIV Envelope Protein gp120); 0 (Viral Proteins)
[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:171020
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185790


  7 / 7348 MEDLINE  
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[PMID]:29045410
[Au] Autor:Dapp MJ; Kober KM; Chen L; Westfall DH; Wong K; Zhao H; Hall BM; Deng W; Sibley T; Ghorai S; Kim K; Chen N; McHugh S; Au L; Cohen M; Anastos K; Mullins JI
[Ad] Endereço:Department of Microbiology, University of Washington School of Medicine, Seattle, Washington, United States of America.
[Ti] Título:Patterns and rates of viral evolution in HIV-1 subtype B infected females and males.
[So] Source:PLoS One;12(10):e0182443, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biological sex differences affect the course of HIV infection, with untreated women having lower viral loads compared to their male counterparts but, for a given viral load, women have a higher rate of progression to AIDS. However, the vast majority of data on viral evolution, a process that is clearly impacted by host immunity and could be impacted by sex differences, has been derived from men. We conducted an intensive analysis of HIV-1 gag and env-gp120 evolution taken over the first 6-11 years of infection from 8 Women's Interagency HIV Study (WIHS) participants who had not received combination antiretroviral therapy (ART). This was compared to similar data previously collected from men, with both groups infected with HIV-1 subtype B. Early virus populations in men and women were generally homogenous with no differences in diversity between sexes. No differences in ensuing nucleotide substitution rates were found between the female and male cohorts studied herein. As previously reported for men, time to peak diversity in env-gp120 in women was positively associated with time to CD4+ cell count below 200 (P = 0.017), and the number of predicted N-linked glycosylation sites generally increased over time, followed by a plateau or decline, with the majority of changes localized to the V1-V2 region. These findings strongly suggest that the sex differences in HIV-1 disease progression attributed to immune system composition and sensitivities are not revealed by, nor do they impact, global patterns of viral evolution, the latter of which proceeds similarly in women and men.
[Mh] Termos MeSH primário: Infecções por HIV/virologia
HIV-1/fisiologia
Caracteres Sexuais
[Mh] Termos MeSH secundário: Estudos de Coortes
Progressão da Doença
Evolução Molecular
Feminino
Glicosilação
Proteína gp120 do Envelope de HIV/genética
Infecções por HIV/genética
Seres Humanos
Funções Verossimilhança
Masculino
Nucleotídeos/genética
Filogenia
Fatores de Tempo
Produtos do Gene gag do Vírus da Imunodeficiência Humana/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HIV Envelope Protein gp120); 0 (Nucleotides); 0 (gag Gene Products, Human Immunodeficiency Virus)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171019
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182443


  8 / 7348 MEDLINE  
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[PMID]:28994411
[Au] Autor:Gristick HB; Wang H; Bjorkman PJ
[Ad] Endereço:Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
[Ti] Título:X-ray and EM structures of a natively glycosylated HIV-1 envelope trimer.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 10):822-828, 2017 Oct 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The structural and biochemical characterization of broadly neutralizing anti-HIV-1 antibodies (bNAbs) has been essential in guiding the design of potential vaccines to prevent infection by HIV-1. While these studies have revealed critical mechanisms by which bNAbs recognize and/or accommodate N-glycans on the trimeric envelope glycoprotein (Env), they have been limited to the visualization of high-mannose glycan forms only, since heterogeneity introduced from the presence of complex glycans makes it difficult to obtain high-resolution structures. 3.5 and 3.9 Šresolution crystal structures of the HIV-1 Env trimer with fully processed and native glycosylation were solved, revealing a glycan shield of high-mannose and complex-type N-glycans that were used to define the complete epitopes of two bNAbs. Here, the refinement of the N-glycans in the crystal structures is discussed and comparisons are made with glycan densities in glycosylated Env structures derived by single-particle cryo-electron microscopy.
[Mh] Termos MeSH primário: HIV-1/química
Manose/análise
Polissacarídeos/análise
Produtos do Gene env do Vírus da Imunodeficiência Humana/química
[Mh] Termos MeSH secundário: Anticorpos Neutralizantes/química
Microscopia Crioeletrônica
Cristalografia por Raios X
Glicosilação
Anticorpos Anti-HIV/química
Proteína gp120 do Envelope de HIV/química
Proteína gp120 do Envelope de HIV/ultraestrutura
Proteína gp41 do Envelope de HIV/química
Proteína gp41 do Envelope de HIV/ultraestrutura
Infecções por HIV/virologia
HIV-1/ultraestrutura
Seres Humanos
Modelos Moleculares
Conformação Proteica
Multimerização Proteica
Produtos do Gene env do Vírus da Imunodeficiência Humana/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (HIV Antibodies); 0 (HIV Envelope Protein gp120); 0 (HIV Envelope Protein gp41); 0 (Polysaccharides); 0 (env Gene Products, Human Immunodeficiency Virus); PHA4727WTP (Mannose)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE
[do] DOI:10.1107/S2059798317013353


  9 / 7348 MEDLINE  
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[PMID]:28945790
[Au] Autor:Del Prete GQ; Keele BF; Fode J; Thummar K; Swanstrom AE; Rodriguez A; Raymond A; Estes JD; LaBranche CC; Montefiori DC; KewalRamani VN; Lifson JD; Bieniasz PD; Hatziioannou T
[Ad] Endereço:AIDS and Cancer Virus Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, MD, United States of America.
[Ti] Título:A single gp120 residue can affect HIV-1 tropism in macaques.
[So] Source:PLoS Pathog;13(9):e1006572, 2017 Sep.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Species-dependent variation in proteins that aid or limit virus replication determines the ability of lentiviruses to jump between host species. Identifying and overcoming these differences facilitates the development of animal models for HIV-1, including models based on chimeric SIVs that express HIV-1 envelope (Env) glycoproteins, (SHIVs) and simian-tropic HIV-1 (stHIV) strains. Here, we demonstrate that the inherently poor ability of most HIV-1 Env proteins to use macaque CD4 as a receptor is improved during adaptation by virus passage in macaques. We identify a single amino acid, A281, in HIV-1 Env that consistently changes during adaptation in macaques and affects the ability of HIV-1 Env to use macaque CD4. Importantly, mutations at A281 do not markedly affect HIV-1 Env neutralization properties. Our findings should facilitate the design of HIV-1 Env proteins for use in non-human primate models and thus expedite the development of clinically relevant reagents for testing interventions against HIV-1.
[Mh] Termos MeSH primário: Proteína gp120 do Envelope de HIV/química
Infecções por HIV/virologia
HIV-1/fisiologia
Tropismo Viral/fisiologia
[Mh] Termos MeSH secundário: Adaptação Fisiológica/fisiologia
Animais
Antígenos CD4/metabolismo
Modelos Animais de Doenças
Feminino
Citometria de Fluxo
Proteína gp120 do Envelope de HIV/genética
Infecções por HIV/genética
Seres Humanos
Immunoblotting
Macaca mulatta
Masculino
Reação em Cadeia da Polimerase
Vírus da Imunodeficiência Símia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD4 Antigens); 0 (HIV Envelope Protein gp120); 0 (gp120 protein, Human immunodeficiency virus 1)
[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:170926
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006572


  10 / 7348 MEDLINE  
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[PMID]:28916265
[Au] Autor:Andrabi R; Su CY; Liang CH; Shivatare SS; Briney B; Voss JE; Nawazi SK; Wu CY; Wong CH; Burton DR
[Ad] Endereço:Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA; International AIDS Vaccine Initiative, Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA; Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, The Scripp
[Ti] Título:Glycans Function as Anchors for Antibodies and Help Drive HIV Broadly Neutralizing Antibody Development.
[So] Source:Immunity;47(3):524-537.e3, 2017 Sep 19.
[Is] ISSN:1097-4180
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Apex broadly neutralizing HIV antibodies (bnAbs) recognize glycans and protein surface close to the 3-fold axis of the envelope (Env) trimer and are among the most potent and broad Abs described. The evolution of apex bnAbs from one donor (CAP256) has been studied in detail and many Abs at different stages of maturation have been described. Using diverse engineering tools, we investigated the involvement of glycan recognition in the development of the CAP256.VRC26 Ab lineage. We found that sialic acid-bearing glycans were recognized by germline-encoded and somatically mutated residues on the Ab heavy chain. This recognition provided an "anchor" for the Abs as the core protein epitope varies, prevented complete neutralization escape, and eventually led to broadening of the response. These findings illustrate how glycan-specific maturation enables a human Ab to cope with pathogen escape mechanisms and will aid in optimization of immunization strategies to induce V2 apex bnAb responses.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/imunologia
Anticorpos Anti-HIV/imunologia
Infecções por HIV/imunologia
Infecções por HIV/metabolismo
HIV-1/imunologia
Polissacarídeos/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Afinidade de Anticorpos/imunologia
Formação de Anticorpos/imunologia
Sítios de Ligação
Epitopos/imunologia
Anticorpos Anti-HIV/química
Anticorpos Anti-HIV/classificação
Anticorpos Anti-HIV/genética
Proteína gp120 do Envelope de HIV/química
Proteína gp120 do Envelope de HIV/imunologia
Infecções por HIV/virologia
Seres Humanos
Cadeias Pesadas de Imunoglobulinas/genética
Modelos Moleculares
Ácido N-Acetilneuramínico/metabolismo
Testes de Neutralização
Fragmentos de Peptídeos/imunologia
Filogenia
Ligação Proteica/imunologia
Conformação Proteica
Multimerização Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Epitopes); 0 (HIV Antibodies); 0 (HIV Envelope Protein gp120); 0 (Immunoglobulin Heavy Chains); 0 (Peptide Fragments); 0 (Polysaccharides); GZP2782OP0 (N-Acetylneuraminic Acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170917
[St] Status:MEDLINE



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