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Kejian Wang - One of the best experts on this subject based on the ideXlab platform.
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An Ns1abp-like gene promotes white spot syndrome virus infection by interacting with the Viral Envelope Protein VP28 in red claw crayfish Cherax quadricarinatus.
Developmental and comparative immunology, 2018Co-Authors: Xiaolu Xie, Kejian Wang, Yan Gao, Ling-ke Liu, Xuejiao Chang, Man-jun Liu, Hai-peng LiuAbstract:Abstract Influenza A virus non-structural-1A binding Protein (named as Ns1abp) was originally identified as a host Protein from human that bound to the Viral NS-1 Protein. In our previous study, the expression of an Ns1abp-like gene (denoted as CqNs1abp-like gene) was found to be up-regulated in a transcriptome library from the haematopoietic tissue (Hpt) cells of red claw crayfish Cherax quadricarinatus post white spot syndrome virus (WSSV) infection. To elucidate the role of CqNs1abp-like gene involved in WSSV infection, we cloned the CqNs1abp-like gene in which the open reading frame was 2232 bp, encoding 743 amino acids with two typical domains of one BTB (Broad-Complex, Tramtrack and Bric a brac) domain at N-terminal and six Kelch domains at C-terminal. The gene expression profile showed that the mRNA transcript of CqNs1abp-like gene was widely expressed in all the tested tissues with highest expression in nerve, relatively high expression in Hpt and lowest expression in eyestalk. Importantly, both the WSSV entry and the Viral replication were significantly reduced in Hpt cells after gene silencing of CqNs1abp-like gene. By using Protein pull-down assay, we found that the recombinant BTB domain, six Kelch domains and CqNs1abp-like intact Protein were all bound to the WSSV Envelope Protein VP28, respectively, in which the BTB domain showed slightly less binding affinity than that of the six Kelch domains or the recombinant intact Protein. Besides, the WSSV entry into Hpt cells was clearly decreased when the virus was pre-incubated with the recombinant BTB domain, six Kelch domains, or the recombinant CqNs1abp-like intact Protein, respectively, suggesting that the CqNs1abp-like gene was likely to function as a putative recognition molecular towards WSSV infection in a crustacean C. quadricarinatus. Taken together, these data shed new light on the mechanism of WSSV infection and a putatively novel target on anti-WSSV infection in crustacean farming.
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a laminin receptor like Protein regulates white spot syndrome virus infection by binding to the Viral Envelope Protein vp28 in red claw crayfish cherax quadricarinatus
Developmental and Comparative Immunology, 2018Co-Authors: Weidong Li, Rongyuan Chen, Heng Hong, Kejian WangAbstract:Abstract White spot syndrome virus (WSSV) is a lethal pathogen of shrimp and many other crustaceans, which has been causing huge economic losses in global aquaculture. Laminin receptor (LR) is a cell surface receptor which participates in the interactions between cells as well as cells and extracellular matrix. Previously, we found that a CqLR-like gene was responsive to WSSV infection in the hematopoietic tissue (Hpt) cells from red claw crayfish Cherax quadricarinatus. To further reveal the role of CqLR-like gene involved in WSSV infection, the full-length cDNA of CqLR-like gene was cloned with 1000 bp, and the open reading frame encoded 308 amino acids with a conserved laminin-binding domain. Importantly, both the WSSV entry and Viral replication were strongly reduced in Hpt cells after loss-of-function of CqLR-like gene by gene silencing. Protein interaction assay demonstrated that the recombinant CqLR-like Protein could bind to WSSV virion in vitro by enzyme-linked immunosorbent assay and the binding affinity was in a dose-dependent manner. Furthermore, recombinant CqLR-like Protein was found to bind to WSSV envelop Protein VP28, but not other envelop Proteins tested including VP19, VP24, and VP26, by pull down assay in HEK293T cells. In regarding to that LR is mainly localized on many types of cells’ membrane, these data together suggested that CqLR-like Protein was likely to function as a putative recognition molecule towards WSSV and act in the Viral entry into a crustacean host cell, which may benefit the elucidation of the WSSV pathogenesis and further the pharmaceutical target for the possibly effective control of WSSV disease.
Guang Hsiung Kou - One of the best experts on this subject based on the ideXlab platform.
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laminin receptor in shrimp is a cellular attachment receptor for white spot syndrome virus
PLOS ONE, 2016Co-Authors: Wang Jing Liu, Guang Hsiung KouAbstract:White spot syndrome virus (WSSV, genus Whispovirus, family Nimaviridae) is causing huge economic losses in global shrimp farming, but there is no effective control. Shrimp cell laminin receptor (Lamr) may have a role in WSSV infection. The objective was to characterize interactions between Penaeus monodon Lamr (PmLamr) and WSSV structural Proteins. In this study, PmLamr interacted with nine WSSV structural Proteins (based on yeast two-hybrid screening), of which one (VP31) was characterized. Protein pull-down assay confirmed the interaction between PmLamr and VP31; the latter was an Envelope Protein exposed outside the WSSV virion (based on membrane topology assays). Furthermore, similar to mammalian Lamr, there were two major Protein bands in shrimp cells. Cellular localization assay demonstrated VP31 co-localized with PmLamr on transfected cells. Enzyme-link immunosorbent assay (ELISA) and competitive ELISA demonstrated binding of VP31 on PmLamr was dose-dependent; however, addition of WSSV virion competed for binding affinity. Furthermore, based on an in vivo neutralization assay, both VP31 and PmLamr delayed mortality in shrimp challenged with WSSV. We concluded Lamr was an important receptor for WSSV infection and the Viral Envelope Protein VP31 may have a role in host cell recognition and binding. These data contributed to elucidating pathogenesis of WSSV infection and may help in controlling this disease.
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characterization of white spot syndrome virus Envelope Protein vp51a and its interaction with Viral tegument Protein vp26
Journal of Virology, 2008Co-Authors: Yunshiang Chang, Wang Jing Liu, Tsung Lu Chou, Yuan Ting Lee, Tailin Lee, Weitung Huang, Guang Hsiung KouAbstract:In this study, we characterize a novel white spot syndrome virus (WSSV) structural Protein, VP51A (WSSV-TW open reading frame 294), identified from a previous mass spectrometry study. Temporal-transcription analysis showed that vp51A is expressed in the late stage of WSSV infection. Gene structure analysis showed that the transcription initiation site of vp51A was 135 bp upstream of the translation start codon. The poly(A) addition signal overlapped with the translation stop codon, TAA, and the poly(A) tail was 23 bp downstream of the TAA. Western blot analysis of Viral Protein fractions and immunoelectron microscopy both suggested that VP51A is a Viral Envelope Protein. Western blotting of the total Proteins extracted from WSSV virions detected a band that was close to the predicted 51-kDa mass, but the strongest signal was around 72 kDa. We concluded that this 72-kDa band was in fact the full-length VP51A Protein. Membrane topology assays demonstrated that the VP51A 72-kDa Protein is a type II transmembrane Protein with a highly hydrophobic transmembrane domain on its N terminus and a C terminus that is exposed on the surface of the virion. Coimmunoprecipitation, colocalization, and yeast two-hybrid assays revealed that VP51A associated directly with VP26 and indirectly with VP28, with VP26 acting as a linker Protein in the formation of a VP51A-VP26-VP28 complex.
Hai-peng Liu - One of the best experts on this subject based on the ideXlab platform.
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An Ns1abp-like gene promotes white spot syndrome virus infection by interacting with the Viral Envelope Protein VP28 in red claw crayfish Cherax quadricarinatus.
Developmental and comparative immunology, 2018Co-Authors: Xiaolu Xie, Kejian Wang, Yan Gao, Ling-ke Liu, Xuejiao Chang, Man-jun Liu, Hai-peng LiuAbstract:Abstract Influenza A virus non-structural-1A binding Protein (named as Ns1abp) was originally identified as a host Protein from human that bound to the Viral NS-1 Protein. In our previous study, the expression of an Ns1abp-like gene (denoted as CqNs1abp-like gene) was found to be up-regulated in a transcriptome library from the haematopoietic tissue (Hpt) cells of red claw crayfish Cherax quadricarinatus post white spot syndrome virus (WSSV) infection. To elucidate the role of CqNs1abp-like gene involved in WSSV infection, we cloned the CqNs1abp-like gene in which the open reading frame was 2232 bp, encoding 743 amino acids with two typical domains of one BTB (Broad-Complex, Tramtrack and Bric a brac) domain at N-terminal and six Kelch domains at C-terminal. The gene expression profile showed that the mRNA transcript of CqNs1abp-like gene was widely expressed in all the tested tissues with highest expression in nerve, relatively high expression in Hpt and lowest expression in eyestalk. Importantly, both the WSSV entry and the Viral replication were significantly reduced in Hpt cells after gene silencing of CqNs1abp-like gene. By using Protein pull-down assay, we found that the recombinant BTB domain, six Kelch domains and CqNs1abp-like intact Protein were all bound to the WSSV Envelope Protein VP28, respectively, in which the BTB domain showed slightly less binding affinity than that of the six Kelch domains or the recombinant intact Protein. Besides, the WSSV entry into Hpt cells was clearly decreased when the virus was pre-incubated with the recombinant BTB domain, six Kelch domains, or the recombinant CqNs1abp-like intact Protein, respectively, suggesting that the CqNs1abp-like gene was likely to function as a putative recognition molecular towards WSSV infection in a crustacean C. quadricarinatus. Taken together, these data shed new light on the mechanism of WSSV infection and a putatively novel target on anti-WSSV infection in crustacean farming.
Joshua M Farber - One of the best experts on this subject based on the ideXlab platform.
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macrophage tropic hiv and siv Envelope Proteins induce a signal through the ccr5 chemokine receptor
Nature, 1997Co-Authors: Drew Weissman, Mark Dybul, Andrea Rubbert, Ruth Swofford, Joshua M Farber, James Arthos, Sundararajan Venkatesan, Robert L Rabin, Anthony S FauciAbstract:Human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) enter target cells by forming a complex between the Viral Envelope Protein and two cell-surface membrane receptors: CD4 and a 7-span transmembrane chemokine receptor. Isolates of HIV that differ in cellular tropism use different subsets of chemokine receptors as entry cofactors: macrophage-tropic HIVs primarily use CCR5, whereas T-cell-tropic and dual-tropic isolates use CXCR4 receptors. HIV-mediated signal transduction through CCR5 is not required for efficient fusion and entry of HIV in vitro. Here we show that recombinant Envelope Proteins from macrophage-tropic HIV and SIV induce a signal through CCR5 on CD4+ T cells and that Envelope-mediated signal transduction through CCR5 induces chemotaxis of T cells. This chemotactic response may contribute to the pathogenesis of HIV in vivo by chemo-attracting activated CD4+ cells to sites of Viral replication. HIV-mediated signalling through CCR5 may also enhance Viral replication in vivo by increasing the activation state of target cells. Alternatively, Envelope-mediated CCR5 signal transduction may influence Viral-associated cytopathicity or apoptosis.
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macrophage tropic hiv and siv Envelope Proteins induce a signal through the ccr5 chemokine receptor
Nature, 1997Co-Authors: Drew Weissman, Mark Dybul, Andrea Rubbert, Ruth Swofford, James Arthos, Sundararajan Venkatesan, Robert L Rabin, Joshua M FarberAbstract:Human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) enter target cells by forming a complex between the Viral Envelope Protein and two cell-surface membrane receptors: CD4 and a 7-span transmembrane chemokine receptor (reviewed in refs 1,2,3). Isolates of HIV that differ in cellular tropism use different subsets of chemokine receptors as entry cofactors: macrophage-tropic HIVs primarily use CCR5, whereas T-cell-tropic and dual-tropic isolates use CXCR4 (refs 1,2,3) receptors. HIV-mediated signal transduction through CCR5 is not required for efficient fusion and entry of HIV in vitro4,5. Here we show that recombinant Envelope Proteins from macrophage-tropic HIV and SIV induce a signal through CCR5 on CD4+ T cells and that Envelope-mediated signal transduction through CCR5 induces chemotaxis of T cells. This chemotactic response may contribute to the pathogenesis of HIV in vivo by chemo-attracting activated CD4+ cells to sites of Viral replication1,2. HIV-mediated signalling through CCR5 may also enhance Viral replication invivo by increasing the activation state of target cells. Alternatively, Envelope-mediated CCR5 signal transduction may influence Viral-associated cytopathicity or apoptosis.
Drew Weissman - One of the best experts on this subject based on the ideXlab platform.
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macrophage tropic hiv and siv Envelope Proteins induce a signal through the ccr5 chemokine receptor
Nature, 1997Co-Authors: Drew Weissman, Mark Dybul, Andrea Rubbert, Ruth Swofford, Joshua M Farber, James Arthos, Sundararajan Venkatesan, Robert L Rabin, Anthony S FauciAbstract:Human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) enter target cells by forming a complex between the Viral Envelope Protein and two cell-surface membrane receptors: CD4 and a 7-span transmembrane chemokine receptor. Isolates of HIV that differ in cellular tropism use different subsets of chemokine receptors as entry cofactors: macrophage-tropic HIVs primarily use CCR5, whereas T-cell-tropic and dual-tropic isolates use CXCR4 receptors. HIV-mediated signal transduction through CCR5 is not required for efficient fusion and entry of HIV in vitro. Here we show that recombinant Envelope Proteins from macrophage-tropic HIV and SIV induce a signal through CCR5 on CD4+ T cells and that Envelope-mediated signal transduction through CCR5 induces chemotaxis of T cells. This chemotactic response may contribute to the pathogenesis of HIV in vivo by chemo-attracting activated CD4+ cells to sites of Viral replication. HIV-mediated signalling through CCR5 may also enhance Viral replication in vivo by increasing the activation state of target cells. Alternatively, Envelope-mediated CCR5 signal transduction may influence Viral-associated cytopathicity or apoptosis.
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macrophage tropic hiv and siv Envelope Proteins induce a signal through the ccr5 chemokine receptor
Nature, 1997Co-Authors: Drew Weissman, Mark Dybul, Andrea Rubbert, Ruth Swofford, James Arthos, Sundararajan Venkatesan, Robert L Rabin, Joshua M FarberAbstract:Human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) enter target cells by forming a complex between the Viral Envelope Protein and two cell-surface membrane receptors: CD4 and a 7-span transmembrane chemokine receptor (reviewed in refs 1,2,3). Isolates of HIV that differ in cellular tropism use different subsets of chemokine receptors as entry cofactors: macrophage-tropic HIVs primarily use CCR5, whereas T-cell-tropic and dual-tropic isolates use CXCR4 (refs 1,2,3) receptors. HIV-mediated signal transduction through CCR5 is not required for efficient fusion and entry of HIV in vitro4,5. Here we show that recombinant Envelope Proteins from macrophage-tropic HIV and SIV induce a signal through CCR5 on CD4+ T cells and that Envelope-mediated signal transduction through CCR5 induces chemotaxis of T cells. This chemotactic response may contribute to the pathogenesis of HIV in vivo by chemo-attracting activated CD4+ cells to sites of Viral replication1,2. HIV-mediated signalling through CCR5 may also enhance Viral replication invivo by increasing the activation state of target cells. Alternatively, Envelope-mediated CCR5 signal transduction may influence Viral-associated cytopathicity or apoptosis.
