RÉSUMÉ
An experiment was conducted to determine the effects of the dietary inclusion of different levels of thymoquinone (TQ) of broilers subjected to oxidative stress or not on the antibody titers against Newcastle disease and on the gene expression of interleukine-1 and interferon gamma. A total of 320 one-day-old broilers was randomly assigned to eight treatments with four replicates of 10 birds each, in a 4 × 2 factorial arrangement, consisting of four thymoquinone (TQ) levels (0, 5, 8, or 11 mg/kg body weight) and two levels tert-butyl hydroperoxide (t-BHP) injection (0 or 0.02 mmol/kg of body weight). Blood samples were collected from two birds per replicate to determine antibody titers against Newcastle disease. At the end of experiment, two birds per replicate were randomly selected, sacrificed and their spleens were collected to evaluate the genes expressioninterleukin-1 and interferon gamma (p 0.05). The dietary inclusion of TQ of broilers subjected or not oxidative stress increased antibody production against Newcastle disease (p 0.05). Both individual and combined dietary inclusion of t-BHP and TQ promote the differentiation and proliferation of spleen cells and the gene expression of interleukin-1 and interferon gamma (p 0.05).
Sujet(s)
Animaux , Anticorps/physiologie , Régime alimentaire/médecine vétérinaire , Maladie de Newcastle/physiopathologie , Stress oxydatif , Interférons/physiologie , Plantes médicinales/physiologie , Facteurs nucléaires-90/physiologie , Facteurs nucléaires-90/usage thérapeutique , Autopsie/médecine vétérinaire , Rate/anatomie et histologie , Prélèvement d'échantillon sanguin , Expression des gènesRÉSUMÉ
An experiment was conducted to determine the effects of the dietary inclusion of different levels of thymoquinone (TQ) of broilers subjected to oxidative stress or not on the antibody titers against Newcastle disease and on the gene expression of interleukine-1 and interferon gamma. A total of 320 one-day-old broilers was randomly assigned to eight treatments with four replicates of 10 birds each, in a 4 × 2 factorial arrangement, consisting of four thymoquinone (TQ) levels (0, 5, 8, or 11 mg/kg body weight) and two levels tert-butyl hydroperoxide (t-BHP) injection (0 or 0.02 mmol/kg of body weight). Blood samples were collected from two birds per replicate to determine antibody titers against Newcastle disease. At the end of experiment, two birds per replicate were randomly selected, sacrificed and their spleens were collected to evaluate the genes expressioninterleukin-1 and interferon gamma (p 0.05). The dietary inclusion of TQ of broilers subjected or not oxidative stress increased antibody production against Newcastle disease (p 0.05). Both individual and combined dietary inclusion of t-BHP and TQ promote the differentiation and proliferation of spleen cells and the gene expression of interleukin-1 and interferon gamma (p 0.05). (AU)
Sujet(s)
Animaux , Plantes médicinales/physiologie , Facteurs nucléaires-90/physiologie , Facteurs nucléaires-90/usage thérapeutique , Interférons/physiologie , Anticorps/physiologie , Maladie de Newcastle/physiopathologie , Stress oxydatif , Régime alimentaire/médecine vétérinaire , Prélèvement d'échantillon sanguin , Rate/anatomie et histologie , Expression des gènes , Autopsie/médecine vétérinaireRÉSUMÉ
The Nuclear Factor 90 (NF90) and its isoforms constitute a family of proteins that can interact with double-stranded (ds) RNA, through its dsRNA binding motifs. Due to various potential translational events such as alternative splicing, the human Interleukin enhancer binding factor 3 (ilf3) gene codes for multifunctional proteins that are NF90 and its isoforms, involved in transcription, translation, mRNA export and microRNA biogenesis. These proteins can act as cellular partners affecting viral replication and they are also implicated in host defense. As a result of these numerous functions, these protein isoforms have been given various names over the years, leading to confusion in determining their specific functions. In this review we focus on the role of the human NF90 protein isoforms in DNA and RNA virus replication.
Sujet(s)
Facteurs nucléaires-90/métabolisme , Réplication virale , Génome viral , Humains , Facteurs nucléaires-90/composition chimique , Isoformes de protéines/composition chimique , Isoformes de protéines/métabolisme , ARN viral/métabolisme , Protéines virales/métabolismeRÉSUMÉ
Human immunodeficiency virus (HIV)-1 encoded Rev is essential for export from the nucleus to the cytoplasm, of unspliced and singly spliced transcripts coding for structural and nonstructural viral proteins. This process is spatially and temporally coordinated resulting from the interactions between cellular and viral proteins. Here we examined the effects of the sub-cellular localization and dynamics of Rev on the efficiency of nucleocytoplasmic transport of HIV-1 Gag transcripts and virus particle production. Using confocal microscopy and fluorescence recovery after bleaching (FRAP), we report that NF90ctv, a cellular protein involved in Rev function, alters both the sub-cellular localization and dynamics of Rev in vivo, which drastically affects the accumulation of the viral protein p24. The CRM1-dependent nuclear export of Gag mRNA linked to the Rev Response Element (RRE) is dependent on specific domains of the NF90ctv protein. Taken together, our results demonstrate that the appropriate intracellular localization and dynamics of Rev could regulate Gag assembly and HIV-1 replication.
Sujet(s)
Infections à VIH/virologie , VIH-1 (Virus de l'Immunodéficience Humaine de type 1)/métabolisme , VIH-1 (Virus de l'Immunodéficience Humaine de type 1)/physiologie , Facteurs nucléaires-90/physiologie , Produits du gène rev du virus de l'immunodéficience humaine/métabolisme , Cellules cultivées , Redistribution de fluorescence après photoblanchiment , Protéines à fluorescence verte/génétique , Protéines à fluorescence verte/métabolisme , Protéines à fluorescence verte/physiologie , Infections à VIH/métabolisme , Cellules HeLa , Humains , Facteurs nucléaires-90/composition chimique , Facteurs nucléaires-90/génétique , Facteurs nucléaires-90/métabolisme , Structure tertiaire des protéines/génétique , Structure tertiaire des protéines/physiologie , Transport des protéines/physiologie , Protéines de fusion recombinantes/génétique , Protéines de fusion recombinantes/métabolisme , Protéines de fusion recombinantes/physiologie , Distribution tissulaire , Virion/métabolisme , Virion/physiologie , Assemblage viral/physiologie , Réplication virale/génétique , Réplication virale/physiologie , Produits du gène rev du virus de l'immunodéficience humaine/génétique , Produits du gène rev du virus de l'immunodéficience humaine/physiologieRÉSUMÉ
BACKGROUND: The HIV Rev protein is known to facilitate export of incompletely spliced and unspliced viral transcripts to the cytoplasm, a necessary step in virus life cycle. The Rev-mediated nucleo-cytoplasmic transport of nascent viral transcripts, dependents on interaction of Rev with the RRE RNA structural element present in the target RNAs. The C-terminal variant of dsRNA-binding nuclear protein 90 (NF90ctv) has been shown to markedly attenuate viral replication in stably transduced HIV-1 target cell line. Here we examined a mechanism of interference of viral life cycle involving Rev-NF90ctv interaction. RESULTS: Since Rev:RRE complex formations depend on protein:RNA and protein:protein interactions, we investigated whether the expression of NF90ctv might interfere with Rev-mediated export of RRE-containing transcripts. When HeLa cells expressed both NF90ctv and Rev protein, we observed that NF90ctv inhibited the Rev-mediated RNA transport. In particular, three regions of NF90ctv protein are involved in blocking Rev function. Moreover, interaction of NF90ctv with the RRE RNA resulted in the expression of a reporter protein coding sequences linked to the RRE structure. Moreover, Rev influenced the subcellular localization of NF90ctv, and this process is leptomycin B sensitive. CONCLUSION: The dsRNA binding protein, NF90ctv competes with HIV Rev function at two levels, by competitive protein:protein interaction involving Rev binding to specific domains of NF90ctv, as well as by its binding to the RRE-RNA structure. Our results are consistent with a model of Rev-mediated HIV-1 RNA export that envisions Rev-multimerization, a process interrupted by NF90ctv.