BTat, a trans-acting regulatory protein, contributes to bovine immunodeficiency virus-induced apoptosis

Xuan, Chenghao; Qiao, Wentao; Li, Jian; Peng, Guoyuan; Liu, Min; Chen, Qimin; Zhou, Jun; Geng, Yi

doi:10.1111/j.1462-5822.2007.01011.x

Cited by 8 publications

(5 citation statements)

References 43 publications

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“…This mechanism is also conserved in the lentiviruses Jembra disease virus and bovine immunodeficiency virus [153,154], indicative of an important role in lentivirus biology.…”

Section: Viral Modulation Of Immunity: Emerging Roles For Virus-mt Inmentioning

confidence: 94%

Viral Interactions with Microtubules: Orchestrators of Host Cell Biology?

Brice

Moseley

2013

Future Virol.

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Viral interaction with the microtubule (MT) cytoskeleton is critical to infection by many viruses. Most data regarding virus-MT interaction indicate key roles in the subcellular transport of virions/viral genomic material to sites of replication, assembly and egress. However, the MT cytoskeleton orchestrates diverse processes in addition to subcellular cargo transport including regulation of signalling pathways, cell survival and mitosis, suggesting that viruses, expert manipulators of the host cell, might use the virus-MT interface to control multiple aspects of cell biology. Several lines of evidence support this idea, indicating that specific viral proteins can modify MT dynamics and/or structure and regulate processes such as apoptosis and innate immune signalling through MT-dependent mechanisms. Here, we review general aspects of virus-MT interactions, with emphasis on viral mechanisms to modify MT dynamics and functions to affect processes beyond virion transport. The emerging importance of discrete viral protein-MT interactions in pathogenic processes indicates that these interfaces might represent new targets for future therapeutics and vaccine development.

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“…This mechanism is also conserved in the lentiviruses Jembra disease virus and bovine immunodeficiency virus [153,154], indicative of an important role in lentivirus biology.…”

Section: Viral Modulation Of Immunity: Emerging Roles For Virus-mt Inmentioning

confidence: 94%

Viral Interactions with Microtubules: Orchestrators of Host Cell Biology?

Brice

Moseley

2013

Future Virol.

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“…48,49 Briefly, 2 Â 10 6 cells were collected, washed twice with ice-cold phosphate-buffered saline, and fixed in 70% ethanol for 24 h. Then cells were washed twice with phosphate-buffered saline and incubated with propidium iodide (20 mg/ml)/RNase A (20 mg/ml) in phosphate-buffered saline for 30 min in dark. Samples were analyzed on a BD FACSCalibur flow cytometer (Becton Drive, Franklin Lakes, NJ, USA).…”

Section: Flow Cytometrymentioning

confidence: 99%

RBB, a novel transcription repressor, represses the transcription of HDM2 oncogene

et al. 2012

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The p53 tumor suppressor is important in many aspects of cell biology. Tight regulation of p53 is thus imperative for maintaining cell homeostasis and preventing tumorigenesis. The stabilization and activity of p53 is primarily regulated by MDM2, which is encoded for by HDM2. However, how the expression and activity of MDM2 is regulated remains largely unknown. Here, we report a novel BTB and BEN domains-containing protein, RBB. We demonstrated that RBB is a novel transcriptional repressor binding specific DNA motif via a homodimer and interacting with the nucleosome remodeling and deacetylase (NuRD) complex. Genome wide transcription target analysis by ChIP sequencing revealed that RBB represses the transcription of a series of functionally important genes including HDM2. We showed that RBB recruits the NuRD complex to the internal promoter of HDM2 and inhibits the expression of MDM2 protein, leading to subsequent stabilization of tumor suppressor p53. Significantly, we showed that RBB suppresses cell proliferation and sensitizes cells to DNA damage-induced apoptosis. Our data indicate that RBB is a novel transcriptional repressor and an important regulator of p53 pathway.

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“…Only the Tat and Rev proteins have been reported to regulate viral expression at the transcriptional and posttranscriptional levels, respectively (21)(22)(23)68). Among the latter proteins, only the Tat protein and its transactivator response element (TAR) located within the long terminal repeat sequence have been intensively studied (3,6,10,19,58,60,72).…”

Section: Bovine Immunodeficiency Virus (Biv) Is a Lentivirus Of Thementioning

confidence: 99%

The Bovine Immunodeficiency Virus Rev Protein: Identification of a Novel Lentiviral Bipartite Nuclear Localization Signal Harboring an Atypical Spacer Sequence

Corredor

Archambault

2009

J Virol

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Bovine immunodeficiency virus (BIV) is a lentivirus of theRetroviridae family which shares morphological, genetic, antigenic, and/or biologic properties with human immunodeficiency virus type 1 (HIV-1) and other animal lentiviruses including equine infectious anemia virus (EIAV) (22,23,68). Although the association of clinical diseases with BIV is still controversial, persistent lymphocytosis, neurological disorders associated with central nervous system lesions, weight loss, diminished milk production, lymphoid hyperplasia, and the presence of opportunistic bacterial infections have been associated with BIV infection (5,47,57,70). Interestingly, studies of rabbits experimentally infected with BIV have shown the development of a disease characterized by a fatal dysfunction of the immune system similar to that observed in humans, nonhuman primates, and cats infected with HIV-1 (or HIV-2), simian immunodeficiency virus, and feline immunodeficiency virus, respectively (34,35).BIV is categorized as a complex nonprimate lentivirus (68). The BIV provirus DNA is 8,960 nucleotides in length with a typical retroviral genomic structure containing the gag, pol, and env genes flanked by long terminal repeats of 589 nucleotides in length at the 5Ј and 3Ј termini (23,68). In proximity to the pol/env junction, the BIV genome also contains additional open reading frames that may encode nonstructural regulatory/ accessory proteins (23,68). These open reading frames are designated vif (viral infectivity factor), tat (trans-activator factor of transcription), rev (regulator of virus expression), vpw, vpy, and tmx. Only the Tat and Rev proteins have been reported to regulate viral expression at the transcriptional and posttranscriptional levels, respectively (21)(22)(23)68). Among the latter proteins, only the Tat protein and its transactivator response element (TAR) located within the long terminal repeat sequence have been intensively studied (3,6,10,19,58,60,72).BIV Rev is a 23-kDa (186-aa-long) phosphoprotein produced from a multiply spliced mRNA that contains the untranslated leader (exon 1) and two encoding exons (exons 2 and 3) (55). It has been shown previously that BIV Rev localizes to the nucleus and nucleoli of BIV-infected cells (56). As reported for HIV-1 Rev, BIV Rev mediates the nuclear exportation of partially spliced viral RNAs encoding structural proteins and of unspliced RNAs that serve as genomic RNA by interacting with a stem-loop structure termed Rev-responsive element (RRE) present in these RNAs (59). The Rev proteins contain at least three central functional domains: a basic arginine-rich domain that mediates RNA binding (RBD) and contains the nuclear/nucleolar localization signal (NLS/NoLS), a multimerization domain, and a leucine-rich domain that is necessary for the nuclear exportation of Rev (51, 59).In HIV-1, the Rev protein shuttles between the nucleus and the cytoplasm of the infected cells via the importin/exportin proteins or nucleoporin pathway (59). The shuttling of HIV-1 Rev into the nucleus is m...

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BTat, a trans-acting regulatory protein, contributes to bovine immunodeficiency virus-induced apoptosis

Cited by 8 publications

References 43 publications

Viral Interactions with Microtubules: Orchestrators of Host Cell Biology?

Viral Interactions with Microtubules: Orchestrators of Host Cell Biology?

RBB, a novel transcription repressor, represses the transcription of HDM2 oncogene

The Bovine Immunodeficiency Virus Rev Protein: Identification of a Novel Lentiviral Bipartite Nuclear Localization Signal Harboring an Atypical Spacer Sequence

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