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    Millipore aedes albopictus cells
    Aedes Albopictus Cells, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher aedes albopictus cells
    Aedes Albopictus Cells, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    China Center for Type Culture Collection aedes albopictus cells
    Aedes Albopictus Cells, supplied by China Center for Type Culture Collection, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher c636 aedes albopictus cells
    (A) Shannon conservation plot representing the degree of conservation (Y-axis) of DNMT2 orthologs present at every amino acid position (X-axis) across within DNMT2 orthologs from mosquitoes (Culicidae) and fruit flies (Drosophila). Colored boxes represent known DNMT2 functional motifs and domains involved in catalytic activity and target recognition (CFT). The mean conservation score (64%) across all amino acid positions is represented by the horizontal dotted line. Black arrows present on the top represent four major regions containing a majority of amino acid positions with evidence of positive selection and high posterior probability values (> 95%). These individual amino acids are also represented in the accompanying table to the right. (B, C) Spatial distribution of sites unique to each family are represented as yellow spheres on ribbon models of (B) Aedes <t>albopictus</t> (left, 9 sites) and (C) Drosophila melanogaster (right, 10 sites) DNMT2 structures visualized in PyMOL 2.4 (Schrödinger, LLC). The catalytically active cysteine residue (Cys, C) is represented in red. Predicted substrate i.e. S-adenosyl methionine (SAM) or S-adenosyl homocysteine (SAH) binding region is shown as a dashed oval. Functionally important active-site loop and target recognition domain are also indicated on each structure. The lower structures are rotated 180° relative to the upper ones.
    C636 Aedes Albopictus Cells, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    (A) Shannon conservation plot representing the degree of conservation (Y-axis) of DNMT2 orthologs present at every amino acid position (X-axis) across within DNMT2 orthologs from mosquitoes (Culicidae) and fruit flies (Drosophila). Colored boxes represent known DNMT2 functional motifs and domains involved in catalytic activity and target recognition (CFT). The mean conservation score (64%) across all amino acid positions is represented by the horizontal dotted line. Black arrows present on the top represent four major regions containing a majority of amino acid positions with evidence of positive selection and high posterior probability values (> 95%). These individual amino acids are also represented in the accompanying table to the right. (B, C) Spatial distribution of sites unique to each family are represented as yellow spheres on ribbon models of (B) Aedes albopictus (left, 9 sites) and (C) Drosophila melanogaster (right, 10 sites) DNMT2 structures visualized in PyMOL 2.4 (Schrödinger, LLC). The catalytically active cysteine residue (Cys, C) is represented in red. Predicted substrate i.e. S-adenosyl methionine (SAM) or S-adenosyl homocysteine (SAH) binding region is shown as a dashed oval. Functionally important active-site loop and target recognition domain are also indicated on each structure. The lower structures are rotated 180° relative to the upper ones.

    Journal: bioRxiv

    Article Title: Adaptive evolution in DNMT2 supports its role in the dipteran immune response

    doi: 10.1101/2020.09.15.297986

    Figure Lengend Snippet: (A) Shannon conservation plot representing the degree of conservation (Y-axis) of DNMT2 orthologs present at every amino acid position (X-axis) across within DNMT2 orthologs from mosquitoes (Culicidae) and fruit flies (Drosophila). Colored boxes represent known DNMT2 functional motifs and domains involved in catalytic activity and target recognition (CFT). The mean conservation score (64%) across all amino acid positions is represented by the horizontal dotted line. Black arrows present on the top represent four major regions containing a majority of amino acid positions with evidence of positive selection and high posterior probability values (> 95%). These individual amino acids are also represented in the accompanying table to the right. (B, C) Spatial distribution of sites unique to each family are represented as yellow spheres on ribbon models of (B) Aedes albopictus (left, 9 sites) and (C) Drosophila melanogaster (right, 10 sites) DNMT2 structures visualized in PyMOL 2.4 (Schrödinger, LLC). The catalytically active cysteine residue (Cys, C) is represented in red. Predicted substrate i.e. S-adenosyl methionine (SAM) or S-adenosyl homocysteine (SAH) binding region is shown as a dashed oval. Functionally important active-site loop and target recognition domain are also indicated on each structure. The lower structures are rotated 180° relative to the upper ones.

    Article Snippet: Expression vectors containing Drosophila melanogaster and Aedes albopictus DNMT2 orthologs used here were designed in the following manner; Aedes albopictus AMt2 coding region was subcloned into PCR 2.1 TOPO vector (Invitrogen) by PCR amplification of cDNA generated using reverse transcribed from total cellular RNA isolated from C636 Aedes albopictus cells using Protoscript II RT (NEB) and oligo-dT primers (IDT).

    Techniques: Functional Assay, Activity Assay, Selection, Binding Assay

    Structures of DNMT2 orthologs from Drosophila melanogaster ( Dm DNMT2) and Aedes albopictus (AaDNMT2) were generated using homology modelling (Phyre 2). (A) Superimposed ribbon diagrams of DNMT2 orthologs from Drosophila melanogaster (DNMT2, in blue) and Aedes albopictus (AaDNMT2, in orange) outline key structural differences. Primary sequence alignment of the two orthologs (46% overall amino-acid sequence identity) indicate significant differences in the N-terminal end (indicated in pale red on the ribbon diagram and the sequence alignment below) and the Target Recognition Domain (TRD) (indicated in pale green on the ribbon diagram. The catalytic cysteine residue (Cys 78) present within the highly conserved PP C Q motif is represented as red spheres). (B) Electrostatic Potential Surface Visualization models of DNMT2 orthologs were generated through PyMOL 2.4 (Schrödinger, LLC.) using the in-built Adaptive Poisson-Boltzmann Solver (APBS) plug-in. Colored scale bars indicate the range of electrostatic potentials calculated based on amino-acid compositions of each DNMT2 ortholog. The rotation symbol reflects structural features viewed 180° apart along the vertical axis.

    Journal: bioRxiv

    Article Title: Adaptive evolution in DNMT2 supports its role in the dipteran immune response

    doi: 10.1101/2020.09.15.297986

    Figure Lengend Snippet: Structures of DNMT2 orthologs from Drosophila melanogaster ( Dm DNMT2) and Aedes albopictus (AaDNMT2) were generated using homology modelling (Phyre 2). (A) Superimposed ribbon diagrams of DNMT2 orthologs from Drosophila melanogaster (DNMT2, in blue) and Aedes albopictus (AaDNMT2, in orange) outline key structural differences. Primary sequence alignment of the two orthologs (46% overall amino-acid sequence identity) indicate significant differences in the N-terminal end (indicated in pale red on the ribbon diagram and the sequence alignment below) and the Target Recognition Domain (TRD) (indicated in pale green on the ribbon diagram. The catalytic cysteine residue (Cys 78) present within the highly conserved PP C Q motif is represented as red spheres). (B) Electrostatic Potential Surface Visualization models of DNMT2 orthologs were generated through PyMOL 2.4 (Schrödinger, LLC.) using the in-built Adaptive Poisson-Boltzmann Solver (APBS) plug-in. Colored scale bars indicate the range of electrostatic potentials calculated based on amino-acid compositions of each DNMT2 ortholog. The rotation symbol reflects structural features viewed 180° apart along the vertical axis.

    Article Snippet: Expression vectors containing Drosophila melanogaster and Aedes albopictus DNMT2 orthologs used here were designed in the following manner; Aedes albopictus AMt2 coding region was subcloned into PCR 2.1 TOPO vector (Invitrogen) by PCR amplification of cDNA generated using reverse transcribed from total cellular RNA isolated from C636 Aedes albopictus cells using Protoscript II RT (NEB) and oligo-dT primers (IDT).

    Techniques: Generated, Sequencing

    (A) Drosophila melanogaster derived JW18 cells (without Wolbachia ) were transfected with plasmid constructs expressing epitope (FLAG) tagged versions of either the native fly ( Dm DNMT2, depicted in orange) or the non-native mosquito ( Aa DNMT2, depicted in blue) orthologs. Empty vector carrying only the FLAG-tag was used as a negative control (depicted in black). Protein expression was assessed 72 hours post transfection via Western Blot using antibodies against the FLAG-epitope. Cellular β-actin protein expression, probed using anti-β-actin antibody, was used as loading control. (B) 72 hours post transfection, JW18 cells expressing either the empty vector, the native DNMT2 ( Dm DNMT2) or the non-native DNMT2 ( Aa DNMT2) were challenged with SINV at MOI of 10 particles/cell. Cell supernatants were collected 48 hours post infection and infectious virus production was assessed via standard plaque assays on mammalian fibroblast BHK-21 cells. One-way ANOVA with Tukey’s post hoc test for multiple comparisons: Empty Vector vs Dm DNMT2: p = 0.0016, Empty Vector vs Aa DNMT2: p = 0.0017, Dm DNMT2 vs Aa DNMT2: p = 0.9971. Error bars represent standard error of the mean of 3 independent experiments. (C) Specific infectivity ratios of progeny SINV derived from JW18 cells either the empty vector, the native DNMT2 ( Dm DNMT2) or the non-native DNMT2 ( Aa DNMT2) was calculated as the ratio of infectious virus titer (infectious particles) and total viral genome copies (total virus particles) present in supernatants collected 72 hours post infection. One-way ANOVA with Tukey’s post hoc test for multiple comparisons: Empty Vector vs Dm DNMT2: p = 0.0030, Empty Vector vs Aa DNMT2: p = 0.0066, Dm DNMT2 vs Aa DNMT2: p = 0.6951. Error bars represent standard error of the mean of 3 independent experiments. (D) Aedes albopictus derived C636 cells (without Wolbachia ) were transfected with plasmid constructs expressing epitope (FLAG) tagged versions of either the native fly ( Dm DNMT2, depicted in orange) or the non-native mosquito ( Aa DNMT2, depicted in blue) orthologs. Empty vector carrying only the FLAG-tag was used as a negative control (depicted in black). Protein expression was assessed 72 hours post transfection via Western Blot using antibodies against the FLAG-epitope. Cellular β-actin protein expression, probed using anti-β-actin antibody, was used as loading control. (E) 72 hours post transfection, Aedes albopictus derived C710 cells (colonized with w Stri Wolbachia strain) expressing either the empty vector, the native DNMT2 ( Dm DNMT2) or the non-native DNMT2 ( Aa DNMT2) were challenged with SINV at MOI of 10 particles/cell. Cell supernatants were collected 48 hours post infection and infectious virus production was assessed via standard plaque assays on mammalian fibroblast BHK-21 cells. One-way ANOVA with Tukey’s post hoc test for multiple comparisons: Empty Vector vs Dm DNMT2: p = 0.0937, Empty Vector vs Aa DNMT2: p < 0.0001, Dm DNMT2 vs Aa DNMT2: p = 0.0001. Error bars represent standard error of the mean of 3 independent experiments. (F) Specific infectivity ratios of progeny SINV derived from JW18 cells either the empty vector, the native DNMT2 ( Dm DNMT2) or the non-native DNMT2 ( Aa DNMT2) was calculated as the ratio of infectious virus titer (infectious particles) and total viral genome copies (total virus particles) present in supernatants collected 72 hours post infection. One-way ANOVA with Tukey’s post hoc test for multiple comparisons: Empty Vector vs Dm DNMT2: p = 0.8969, Empty Vector vs Aa DNMT2: p = 0.0060, Dm DNMT2 vs Aa DNMT2: p = 0.0095. Error bars represent standard error of mean of 3 independent experiments. ****p < 0.0001, ***p < 0.001, **p < 0.01, ns = not-significant.

    Journal: bioRxiv

    Article Title: Adaptive evolution in DNMT2 supports its role in the dipteran immune response

    doi: 10.1101/2020.09.15.297986

    Figure Lengend Snippet: (A) Drosophila melanogaster derived JW18 cells (without Wolbachia ) were transfected with plasmid constructs expressing epitope (FLAG) tagged versions of either the native fly ( Dm DNMT2, depicted in orange) or the non-native mosquito ( Aa DNMT2, depicted in blue) orthologs. Empty vector carrying only the FLAG-tag was used as a negative control (depicted in black). Protein expression was assessed 72 hours post transfection via Western Blot using antibodies against the FLAG-epitope. Cellular β-actin protein expression, probed using anti-β-actin antibody, was used as loading control. (B) 72 hours post transfection, JW18 cells expressing either the empty vector, the native DNMT2 ( Dm DNMT2) or the non-native DNMT2 ( Aa DNMT2) were challenged with SINV at MOI of 10 particles/cell. Cell supernatants were collected 48 hours post infection and infectious virus production was assessed via standard plaque assays on mammalian fibroblast BHK-21 cells. One-way ANOVA with Tukey’s post hoc test for multiple comparisons: Empty Vector vs Dm DNMT2: p = 0.0016, Empty Vector vs Aa DNMT2: p = 0.0017, Dm DNMT2 vs Aa DNMT2: p = 0.9971. Error bars represent standard error of the mean of 3 independent experiments. (C) Specific infectivity ratios of progeny SINV derived from JW18 cells either the empty vector, the native DNMT2 ( Dm DNMT2) or the non-native DNMT2 ( Aa DNMT2) was calculated as the ratio of infectious virus titer (infectious particles) and total viral genome copies (total virus particles) present in supernatants collected 72 hours post infection. One-way ANOVA with Tukey’s post hoc test for multiple comparisons: Empty Vector vs Dm DNMT2: p = 0.0030, Empty Vector vs Aa DNMT2: p = 0.0066, Dm DNMT2 vs Aa DNMT2: p = 0.6951. Error bars represent standard error of the mean of 3 independent experiments. (D) Aedes albopictus derived C636 cells (without Wolbachia ) were transfected with plasmid constructs expressing epitope (FLAG) tagged versions of either the native fly ( Dm DNMT2, depicted in orange) or the non-native mosquito ( Aa DNMT2, depicted in blue) orthologs. Empty vector carrying only the FLAG-tag was used as a negative control (depicted in black). Protein expression was assessed 72 hours post transfection via Western Blot using antibodies against the FLAG-epitope. Cellular β-actin protein expression, probed using anti-β-actin antibody, was used as loading control. (E) 72 hours post transfection, Aedes albopictus derived C710 cells (colonized with w Stri Wolbachia strain) expressing either the empty vector, the native DNMT2 ( Dm DNMT2) or the non-native DNMT2 ( Aa DNMT2) were challenged with SINV at MOI of 10 particles/cell. Cell supernatants were collected 48 hours post infection and infectious virus production was assessed via standard plaque assays on mammalian fibroblast BHK-21 cells. One-way ANOVA with Tukey’s post hoc test for multiple comparisons: Empty Vector vs Dm DNMT2: p = 0.0937, Empty Vector vs Aa DNMT2: p < 0.0001, Dm DNMT2 vs Aa DNMT2: p = 0.0001. Error bars represent standard error of the mean of 3 independent experiments. (F) Specific infectivity ratios of progeny SINV derived from JW18 cells either the empty vector, the native DNMT2 ( Dm DNMT2) or the non-native DNMT2 ( Aa DNMT2) was calculated as the ratio of infectious virus titer (infectious particles) and total viral genome copies (total virus particles) present in supernatants collected 72 hours post infection. One-way ANOVA with Tukey’s post hoc test for multiple comparisons: Empty Vector vs Dm DNMT2: p = 0.8969, Empty Vector vs Aa DNMT2: p = 0.0060, Dm DNMT2 vs Aa DNMT2: p = 0.0095. Error bars represent standard error of mean of 3 independent experiments. ****p < 0.0001, ***p < 0.001, **p < 0.01, ns = not-significant.

    Article Snippet: Expression vectors containing Drosophila melanogaster and Aedes albopictus DNMT2 orthologs used here were designed in the following manner; Aedes albopictus AMt2 coding region was subcloned into PCR 2.1 TOPO vector (Invitrogen) by PCR amplification of cDNA generated using reverse transcribed from total cellular RNA isolated from C636 Aedes albopictus cells using Protoscript II RT (NEB) and oligo-dT primers (IDT).

    Techniques: Derivative Assay, Transfection, Plasmid Preparation, Construct, Expressing, FLAG-tag, Negative Control, Western Blot, Infection

    Heterologous expression of either Dm DNMT2 or Aa DNMT2 in Drosophila melanogaster derived JW18 cells leads to virus inhibition, likely as a consequence of hypermethylation of a viral and/or host target. In this case, Dm DNMT2 function is potentially aided by the presence of an unidentified co-factor. Heterologous expression of Aa DNMT2 in Wolbachia- colonized Aedes albopictus cells leads to the rescue of virus inhibition, likely due to hypermethylation of a viral and/or host target. In contrast, Dm DNMT2 expression in these cells has no observable effect on virus replication suggesting either a loss in MTase activity or potential off-target effects. This result could be due to the absence of Dm DNMT2’s cognate interaction partner(s) or co-factor(s) that are unique to Drosophila and are thus absent in Aedes albopictus cells.

    Journal: bioRxiv

    Article Title: Adaptive evolution in DNMT2 supports its role in the dipteran immune response

    doi: 10.1101/2020.09.15.297986

    Figure Lengend Snippet: Heterologous expression of either Dm DNMT2 or Aa DNMT2 in Drosophila melanogaster derived JW18 cells leads to virus inhibition, likely as a consequence of hypermethylation of a viral and/or host target. In this case, Dm DNMT2 function is potentially aided by the presence of an unidentified co-factor. Heterologous expression of Aa DNMT2 in Wolbachia- colonized Aedes albopictus cells leads to the rescue of virus inhibition, likely due to hypermethylation of a viral and/or host target. In contrast, Dm DNMT2 expression in these cells has no observable effect on virus replication suggesting either a loss in MTase activity or potential off-target effects. This result could be due to the absence of Dm DNMT2’s cognate interaction partner(s) or co-factor(s) that are unique to Drosophila and are thus absent in Aedes albopictus cells.

    Article Snippet: Expression vectors containing Drosophila melanogaster and Aedes albopictus DNMT2 orthologs used here were designed in the following manner; Aedes albopictus AMt2 coding region was subcloned into PCR 2.1 TOPO vector (Invitrogen) by PCR amplification of cDNA generated using reverse transcribed from total cellular RNA isolated from C636 Aedes albopictus cells using Protoscript II RT (NEB) and oligo-dT primers (IDT).

    Techniques: Expressing, Derivative Assay, Inhibition, Activity Assay

    72 hours post transfection, Aedes albopictus derived C710 cells (colonized with w Stri Wolbachia strain) expressing either the empty vector, the native DNMT2 ( Dm DNMT2) or the non-native DNMT2 ( Aa DNMT2) were challenged with SINV at MOI of 10 particles/cell. Cell lysates were collected 48 hours post infection and levels of (A) virus and (B) Wolbachia RNA levels were assessed using qRT-PCR on total extracted RNA. One-way ANOVA with Tukey’s post hoc test for multiple comparisons: SINV RNA, Empty Vector vs Dm DNMT2: p = 0.7875, Empty Vector vs Aa DNMT2: p < 0.05, Dm DNMT2 vs Aa DNMT2: p < 0.05, Wolbachia , Empty Vector vs Dm DNMT2: p = 0.4121, Empty Vector vs Aa DNMT2: p = 0.5639, Dm DNMT2 vs Aa DNMT2: p = 0.9523. Error bars represent standard error of mean of 3 independent experiments. *p < 0.05, ns = not-significant.

    Journal: bioRxiv

    Article Title: Adaptive evolution in DNMT2 supports its role in the dipteran immune response

    doi: 10.1101/2020.09.15.297986

    Figure Lengend Snippet: 72 hours post transfection, Aedes albopictus derived C710 cells (colonized with w Stri Wolbachia strain) expressing either the empty vector, the native DNMT2 ( Dm DNMT2) or the non-native DNMT2 ( Aa DNMT2) were challenged with SINV at MOI of 10 particles/cell. Cell lysates were collected 48 hours post infection and levels of (A) virus and (B) Wolbachia RNA levels were assessed using qRT-PCR on total extracted RNA. One-way ANOVA with Tukey’s post hoc test for multiple comparisons: SINV RNA, Empty Vector vs Dm DNMT2: p = 0.7875, Empty Vector vs Aa DNMT2: p < 0.05, Dm DNMT2 vs Aa DNMT2: p < 0.05, Wolbachia , Empty Vector vs Dm DNMT2: p = 0.4121, Empty Vector vs Aa DNMT2: p = 0.5639, Dm DNMT2 vs Aa DNMT2: p = 0.9523. Error bars represent standard error of mean of 3 independent experiments. *p < 0.05, ns = not-significant.

    Article Snippet: Expression vectors containing Drosophila melanogaster and Aedes albopictus DNMT2 orthologs used here were designed in the following manner; Aedes albopictus AMt2 coding region was subcloned into PCR 2.1 TOPO vector (Invitrogen) by PCR amplification of cDNA generated using reverse transcribed from total cellular RNA isolated from C636 Aedes albopictus cells using Protoscript II RT (NEB) and oligo-dT primers (IDT).

    Techniques: Transfection, Derivative Assay, Expressing, Plasmid Preparation, Infection, Quantitative RT-PCR