Adhesion of Human Neuroblasts to HIV-1 tat

Cornaglia-Ferraris, P.; Maria, Andrea De; Cirillo, C.; Cara, Andrea; Alessandri, Giulio

doi:10.1203/00006450-199511000-00025

Cited by 5 publications

(3 citation statements)

References 23 publications

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“…Beside ECs, Tat induces substratum adhesion of Kaposi's sarcoma-derived spindle cells (Barillari et al, 1993), neurons (Cornaglia-Ferraris et al, 1995), myoblasts (Vogel et al, 1993), and epithelial cells (C.U. and C. Ravelli, unpublished), FAK phosphorylation in neurons (Milani et al, 1998) and NF-B activation in various cell types (see above).…”

Section: Tat/␣ V ␤ 3 Interaction Promotes Fak Activationmentioning

confidence: 99%

αvβ3-integrin-dependent activation of focal adhesion kinase mediates NF-κB activation and motogenic activity by HIV-1 Tat in endothelial cells

Urbinati

Bugatti

Giacca

et al. 2005

Journal of Cell Science

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Once in the extracellular environment, the transactivator protein HIV-1 Tat exerts several pleiotropic effects by interacting with different cellular receptors, including integrin αvβ3. Real-time surface plasmon resonance analysis reveals that Tat/αVβ3 interaction occurs with rapid kinetics (association and dissociation rates equal to 1.16×107 M-1 s-1 and 3.78×10-1 s-1, respectively) and high affinity (dissociation constant = 32 nM). Through this interaction, substratum-immobilized Tat promotes adhesion and motogenic activity in endothelial cells. Also, αvβ3/Tat interaction triggers the activation of focal adhesion kinase, RhoA and pp60src. Overexpression of the dominant negative form of focal adhesion kinase, but not of an inactive Leu1034Ser substitution mutant isoform, impairs the activation of focal adhesion kinase and RhoA, but not that of pp60src, without affecting endothelial cell adhesion and spreading. αvβ3/Tat interaction triggers the activation of NF-κB in endothelial cells in a focal adhesion kinase-, RhoA- and pp60src-dependent manner, as shown in dominant negative focal adhesion kinase transfectants or using specific pharmacological inhibitors. Finally, the activation of focal adhesion kinase, RhoA, NF-κB and pp60src are required to mediate the motogenic activity of Tat in endothelial cells. Since Tat accumulates in an immobilized form in the extracellular matrix, these results provide new biochemical and biological insights about αvβ3/Tat interaction exploitable for the design of anti-Tat strategies.

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Section: Tat/␣ V ␤ 3 Interaction Promotes Fak Activationmentioning

confidence: 99%

αvβ3-integrin-dependent activation of focal adhesion kinase mediates NF-κB activation and motogenic activity by HIV-1 Tat in endothelial cells

Urbinati

Bugatti

Giacca

et al. 2005

Journal of Cell Science

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“…The regulation of collagens has been shown to be altered by the HIV-1 Tat protein during the later stages of infection, along with other extracellular matrix proteins, such as fibronectin and laminin [50]. Moreover, in neuroblastoma cells, extracellular Tat was found to compete with type I collagens of the extracellular matrix, and thus, dysregulating neuronal differentiation [51]. Similarly, the cellular level of cytokeratins can be altered by HIV and other viruses as well, such as human papillomavirus (HPV) [52,53].…”

Section: Discussionmentioning

confidence: 99%

Cellular Proteo-Transcriptomic Changes in the Immediate Early-Phase of Lentiviral Transduction

et al. 2021

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Lentivirus-based vectors derived from human immunodeficiency viruses type 1 and 2 (HIV-1 and 2) are widely used tools in research and may also be utilized in clinical settings. Like their parental virions, they are known to depend on the cellular machinery for successful gene delivery and integration. While most of the studies on cellular proteomic and transcriptomic changes have focused on the late phase of the transduction, studies of those changes in early time-points, especially in the case of HIV-2 based vectors, are widely lacking. Using second generation HIV-1 and 2 vesicular stomatitis virus G protein (VSV-G) pseudotyped lentiviral vectors, we transduced HEK-293T human embryonic kidney cells and carried out transcriptomic profiling at 0 and 2 h time points, with accompanying proteomic analysis at 2 h following transduction. Significant variations were observed in gene expression profile between HIV-1 and HIV-2 transduced samples. Thrombospondin 1 (THBS1), collagens (COL1A2, COL3A1), and eukaryotic translation factors (EIF3CL) in addition to various genes coding for long non-coding RNA (lncRNA) were significantly upregulated 2 h after HIV-2 transduction compared to HIV-1. Label-free quantification mass spectrometry (MS) indicated that seven proteins involved in RNA binding, mRNA transport, and chaperoning were significantly downregulated. The identification of cellular protein targets of lentiviral vectors and their effect on the cellular transcriptome will undoubtedly shed more light on their complex life cycle and may be utilized against infection by their parental lentiviruses. Furthermore, characterizing the early phase of HIV-2 infection may aid in the understanding of its pathomechanism and long incubation period.

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“…This was performed as previously described (20). HSE maintained in the growth medium, was augmented with GM3 or GTlb (100pM/ml) and the cells were incubated for 24 h. At the end of incubation, the cells were harvested by means of trypsin treatment (0.1% WjV), suspended in serum-free RPMI 1640 and seeded at a concentration of 2 x 104/100 pl per well in 96 wellplates (Costar Cambridge, Mass.)…”

Section: Cell Adhesion Assaymentioning

confidence: 99%