159 resultados para HIV

em Chinese Academy of Sciences Institutional Repositories Grid Portal


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Objective: In Old World monkeys, the tripartite motif Sec (TRIM5 alpha) protein confers resistance to HIV-1 infection following virus entry into host cells. However, the pig-tailed macaque (Macaca nemestrina) is an exception and is susceptible to HIV-1 in

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Recent studies showed that nonhuman primate TRIM5 alpha can efficiently block HIV-1 infection in human cell lines. It can also restrict other retroviruses, therefore, suggested as a general defender against retrovirus infection. Here, we present an evolutionary analysis of TRIM5 alpha in primates. Our results demonstrated that TRIM5a has been evolving rapidly in primates, which is likely caused by Darwinian positive selection. The SPRY domain of TRM5 alpha, which may be responsible for recognition of incoming viral capsids showed higher nonsynonymous/synonymous substitution ratios than the non-SPRY domain, indicating that the adaptive evolution of TRIM5a ill primates might be an innate strategy developed in defending retrovirus infection during primate evolution. In addition, the comparative protein sequence analysis suggested that the amino acid substitution pattern at a single site (344R/Q/P) located in the SPRY domain may explain the differences in Susceptibilities of HIV-1 infection in diverse primate species. (c) 2005 Elsevier B.V. All rights reserved.

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Limited information is available on the prevalence among rural Africans of host genetic polymorphisms conferring resistance to HIV-1 infection or slowing HIV disease progression.We report the allelic frequencies of the AIDS-related polymorphisms CCR2-64I, SDF1-3#A, and CCR5-D32 in 321 volunteers from 7 ethnic groups in Cameroon. Allelic frequencies differed among the 7 ethnic groups, ranging from 10.8% to 31.3% for CCR2-64I and 0.0% to 7.1% for SDF1-3#A. No CCR5-D32 alleles were found. HIV seroprevalence was 6.9% in the total population and peaked at younger ages in girls and women than in boys and men. Among 15- to 54-year-olds, HIV seroprevalence varied from 2.0% to 11.1% among the village populations. Conditional logistic regression analysis using data from boys and men aged 15 to 54 years showed the number of CCR2-64I alleles to be a significant risk factor for HIV seropositivity (odds ratio per allele adjusted for age and matched on ethnic group = 6.3, 95% confidence interval: 1.330.3); this association was not found in women. The findings are consistent with the hypothesis that CCR2-64I alleles may delay HIV disease progression without affecting susceptibility to infection among men. We did not observe this relation among women, and other factors, such as multiple pregnancies or maternal stressors (eg, breastfeeding), may have masked any protective effect of CCR2-64I alleles. Further study of this issue among women is warranted. SDF1-3#A did not differ between HIV-seropositive and HIV-seronegative individuals but wasassociated with increasing age among HIV-seronegative women, suggesting a protective effect against HIV-1 infection.

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A novel L-amino acid oxidase, named TSV-LAO, has been purified and cloned from the snake Trimeresurus stejnegeri. Fifty percentage cytotoxic concentrations (CC50) of TSV-LAO on C8166 cells were 24 and 390 nM in the absence or presence of catalase (400nM), respectively. However, at concentrations that showed little effect on cell viability, TSV-LAO displayed dose dependent inhibition on HIV-1 infection and replication. The antiviral selectivity indexes (CC50/EC50) were 16 and 6, respectively, corresponding to the measurements of syncytium formation and HIV-1 p24 antigen expression. Interestingly, the presence of catalase resulted in an increase of its antiviral selectivity to 52 and 38. Under the same conditions, no anti-HIV-1 activity was observed by exogenous addition of H2O2. The complete amino acid sequence of TSV-LAO, as deduced from its cDNA, exhibits a high degree of sequence identity with other snake venom LAOs. (C) 2003 Elsevier Inc. All rights reserved.

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A novel protein, named BAS-AH, was purified and characterized from the skin of the toad Bufo andrewsi. BAS-AH is a single chain protein and the apparent molecular weight is about 63 kDa as judged by SDS-PAGE. BAS-AH was determined to bind heme (0.89 mol heme/mol protein) as determined by pyridine haemochrome analysis. Fifty percentage cytotoxic concentration (CC50) of BAS-AH on C8166 cells was 9.5 mu M. However, at concentrations that showed little effect oil cell viability, BAS-AH displayed dose dependent inhibition oil HIV-1 infection and replication. The antiviral selectivity indexes corresponding to the measurements of syncytium formation and HIV-1 p24 (CC50/EC50) were 14.4 and 11.4, respectively, corresponding to the . BAS-AH also showed an inhibitory effect on the activity of recombinant HIV-1 reverse transcriptase (IC50 = 1.32 mu M). The N-terminal sequence of BAS-AH was determined to be NAKXKADVIGKISILLGQDNLSNIVAM, which exhibited little identity with other known anti-HIV-1 proteins. BAS-AH is devoid of antibacterial, protcolytic, trypsin inhibitory activity, (L)-amino acid oxidase activity and catalase activity. (c) 2005 Elsevier Ltd. All rights reserved.

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A new lupane acid, 2 beta-carboxyl, 3 beta-hydroxyl-norlupA (1)-20 (29)-en-28-oic acid (1), together with five known lupane acid derivatives (2-6), were isolated from the stings of Gleditsia sinensis Lam.. Their structures were elucidated on the basis of

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2 : S-DABO HIV AZTHIV-1 HIV HIV HAART FDA HIV 23 S-DABO 8 AZTHIV 23 S-DABO C8166 HIV-1B HIV-1B MT-4 HIV-1 HIV 22 HIV-1 RZK-4 RZK-5 HIV-1B SI Selective index>16666 >38462 RZK-4 RZK-5 HIV-1B MT-4 SI 2666.67 2150.54NVPNevirapineSI p24 20 HIV-1 20 HIV-1B p24 RZK-4 RZK-5 EC50 5.93 5.74ng/mlNVPNevirapineEC50 27.3ng/mlHIV-1MNHIV-1KM018 HIV-1B A17 23 S-DABO HIV-2 HIV-1 H9 H9/HIV-1BHIV-1 20 HIV-1 PR17 HIV-1 RT H9 23 S-DABO HIV-1 RT 8 AZTC8166 HIV-1B HIV-1BMT-4 HIV-1 2 SRLZ SROZ HIV-1 HIV-1BSI >41667 >105263HIV-1B MT-4 SI 30162 6368AZTZidothymidineSI p24 HIV-1SRLZSROZHIV-1B p24 EC50 0.71 2.1ng/ml,AZT EC50 3.5ng/mlSRLZ SROZ HIV-1KM018 EC50 1.4 22ng/ml H9 H9/HIV-1BHIV-1 SRLZ SROZ H9 SRLZ SROZ MICMinimum inhibitory concentration14.65 7.32g/ml MIC AZTHIV

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Dendritic cellsDCsHuman Immunodeficiency VirusHIV HIV-1 DC THIV-1 lentivirusHIV-16NefRev TatVifVprVpu HIV-1CD4+ TDC DCHIV-1 HIV/AIDS HIV-1THP-1 THP-1DCDCDC 6 THP-1NefTat RevVprTHP-1 RevVprDC VifVpuTHP-1 APOBEC3GVpuAPOBEC3G HIV/AIDS

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DCHIV/AIDS HIV/AIDS DC T NefRevTatVifVpr VpuHIV-1 DC HIV-1 DC 6 DC DNA mRNA DCDC DC HIV/AIDS DC 6 pEGFP-N2 pCS2+ DNA mRNA DCK562 mRNA CD14 22DC Amaxa DNA DC GFP 5h 48hNefTatVpuRevVifVpr 35.42%34.42%43.42% 17.07%13.65%10.29% CD14HLA-DRCD80CD83CD86DC-SIGN NefVpu Rev 10Vpr IL-10 Nef IL-6 DC mRNA DC DC

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HIV-1HIV-1HIV-11 (Human Immunodeficiency Virustype IHIV-1)

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Human immunodeficiency virus-1(HIV-1).Regulator of expression of virion proteins(Rev)HIV-1,mRNA,.Rev,,HIV-1revTHP-1,G418Rev;RT-PCR,mRNA.revTHP-1,rev.

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AZT-SRLZSROZHIV-1. HIV-1HIV-1 p24HIV-1;. AZT-SRLZSROZHIV-1,;SRLZSROZHIV-1;SRLZSROZHIV-1AZT;AZT-,MIC. SRLZSROZHIV-1.

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HIV-1 Cgp120,293gp120. PCR,HIV-1 Cgp120,pTrack-CMV,pAd-easy-1BJ5183,prAd-gp120,Pac293,vAd-gp120. PCRDNA,,vAd-gp120;Western ,293120 kD. HIV-1 Cgp120,.

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PDF HIV-1,. HIV-1HIV-1 p24HIV-1;HIV-1,. (P3)HIV-1,P3HIV-1C8166EC505.64 pg/mL,C8166,CC50200 g/mL,(T1)35.46;P3HIV-1p24EC5023.04 g/mL,C8166Hg/HIV-1-BEC508.00 g/mL;P3200g/mL,HIV-128.86%;P3HIV-1EC501.77g/mL. (P3)HIV-1,HIV-1.