sialidase activity  (New England Biolabs)


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    Structured Review

    New England Biolabs sialidase activity
    Composition of substitution mutations with respect to consensus sequences. Percentages represent the mean across eight M. synoviae strains for nanI , nagA , nanA , nagC , nanE , and nagB genes of the <t>sialidase</t> locus, and three M. hyopneumoniae strains for housekeeping genes dnaA and ftsY .
    Sialidase Activity, supplied by New England Biolabs, 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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    Images

    1) Product Images from "Genetic Variation in Sialidase and Linkage to N-acetylneuraminate Catabolism in Mycoplasma synoviae"

    Article Title: Genetic Variation in Sialidase and Linkage to N-acetylneuraminate Catabolism in Mycoplasma synoviae

    Journal: Microbial pathogenesis

    doi: 10.1016/j.micpath.2008.02.002

    Composition of substitution mutations with respect to consensus sequences. Percentages represent the mean across eight M. synoviae strains for nanI , nagA , nanA , nagC , nanE , and nagB genes of the sialidase locus, and three M. hyopneumoniae strains for housekeeping genes dnaA and ftsY .
    Figure Legend Snippet: Composition of substitution mutations with respect to consensus sequences. Percentages represent the mean across eight M. synoviae strains for nanI , nagA , nanA , nagC , nanE , and nagB genes of the sialidase locus, and three M. hyopneumoniae strains for housekeeping genes dnaA and ftsY .

    Techniques Used:

    Related Articles

    Recombinant:

    Article Title: Cooperativity of catalytic and lectin-like domain of T. congolense trans-sialidase modulates its catalytic activity
    Article Snippet: .. Recombinant PNGaseF endoglycosidase was from New England Biolabs, United Kingdom. .. Pfu and Taq DNA polymerase, Eco105 I, Hind III, Nco I, Not I, Sal I and Spe I Fast Digest restriction enzymes, T4-DNA ligase, isopropyl-β-D-1-thiogalactopyranoside (IPTG), Dithiothreitol (DTT), Coomassie Brilliant Blue (Page Blue), protein molecular weight marker (PageRuler), GeneJET DNA Gel Extraction Kit, BCA Protein Assay Kit, enhanced chemiluminescence system (ECL-Kit), Luria Broth (LB) microbial growth medium, were from Thermo Scientific, Germany.

    Sequencing:

    Article Title: Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
    Article Snippet: Removal of excess label from the 2-AA fluorescently labeled glycan samples was performed using Speed Amide-2 cartridges (Applied Separations, Allentown, PA). .. Exoglycosidase Sequencing of N-Linked Glycans The 2-AA labeled glycans were sequentially digested using the following exoglycosidases according to the manufacturers’ instructions: α2-3,6,8 neuraminidase from Clostridium perfringens (New England Biolabs, Hertfordshire, UK), α2-3 neuraminidase from Streptococcus pneumoniae (New England BioLabs, Hertfordshire, UK), β1,4-galactosidase from Bacteroides fragilis (New England Biolabs, Hertfordshire, UK), and α-L-fucosidase from bovine kidney (Sigma-Aldrich, Dorset, UK), β-N -acetylglucosaminidase from Xanthomonas manihotis (New England Biolabs, Hertfordshire, UK), and α(1–2,3,6)-mannosidase from Jack bean (Sigma-Aldrich, Dorset, UK). .. Endoglycosidase H (endoH) from Streptomyces picatus (New England BioLabs, Hertfordshire, UK) was used for quantification of oligomannose structures.

    Labeling:

    Article Title: Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
    Article Snippet: Removal of excess label from the 2-AA fluorescently labeled glycan samples was performed using Speed Amide-2 cartridges (Applied Separations, Allentown, PA). .. Exoglycosidase Sequencing of N-Linked Glycans The 2-AA labeled glycans were sequentially digested using the following exoglycosidases according to the manufacturers’ instructions: α2-3,6,8 neuraminidase from Clostridium perfringens (New England Biolabs, Hertfordshire, UK), α2-3 neuraminidase from Streptococcus pneumoniae (New England BioLabs, Hertfordshire, UK), β1,4-galactosidase from Bacteroides fragilis (New England Biolabs, Hertfordshire, UK), and α-L-fucosidase from bovine kidney (Sigma-Aldrich, Dorset, UK), β-N -acetylglucosaminidase from Xanthomonas manihotis (New England Biolabs, Hertfordshire, UK), and α(1–2,3,6)-mannosidase from Jack bean (Sigma-Aldrich, Dorset, UK). .. Endoglycosidase H (endoH) from Streptomyces picatus (New England BioLabs, Hertfordshire, UK) was used for quantification of oligomannose structures.

    Binding Assay:

    Article Title: Inhibition of SARS-CoV-2 viral entry upon blocking N- and O-glycan elaboration
    Article Snippet: In some cases, binding studies were also performed with stable 293T/ACE2 cells, in which case fluorescence gating was not necessary. .. In some assays, cells were treated with sialidase (200 U/mL Arthrobacter ureafaciens α2–3,6,8,9-Neuraminidase, New England BioLabs) for 1 hr at 37°C, and washed using HEPES buffer prior to the binding assay. .. Sialidase activity was verified based on SNA and ECL staining.

    Activity Assay:

    Article Title: Genetic Variation in Sialidase and Linkage to N-acetylneuraminate Catabolism in Mycoplasma synoviae
    Article Snippet: The amplicons were labeled with digoxygenin (DIG Hi prime, Roche Applied Sciences) according to the manufacturer’s instructions. .. Genomic DNA from the strains with the highest (WVU1853T ) and lowest (K4907A and K5395B) levels of sialidase activity was digested with endonuclease Vsp I (New England Biolabs, Ipswich, Massachusetts), then separated on a 0.6% agarose gel. ..

    Agarose Gel Electrophoresis:

    Article Title: Genetic Variation in Sialidase and Linkage to N-acetylneuraminate Catabolism in Mycoplasma synoviae
    Article Snippet: The amplicons were labeled with digoxygenin (DIG Hi prime, Roche Applied Sciences) according to the manufacturer’s instructions. .. Genomic DNA from the strains with the highest (WVU1853T ) and lowest (K4907A and K5395B) levels of sialidase activity was digested with endonuclease Vsp I (New England Biolabs, Ipswich, Massachusetts), then separated on a 0.6% agarose gel. ..

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    New England Biolabs sialidase activity
    Composition of substitution mutations with respect to consensus sequences. Percentages represent the mean across eight M. synoviae strains for nanI , nagA , nanA , nagC , nanE , and nagB genes of the <t>sialidase</t> locus, and three M. hyopneumoniae strains for housekeeping genes dnaA and ftsY .
    Sialidase Activity, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sialidase activity/product/New England Biolabs
    Average 86 stars, based on 1 article reviews
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    New England Biolabs sialidase
    Altered O -glycosylation on CSRP3 in the LV of DS hypertensive rats. (A) ACA lectin blot analysis and SYPRO Ruby staining of fractions from <t>sialidase-treated</t> LV extracts. Arrow indicates the ACA-positive band, which is observed strongly in fraction 3 of HS ( H ) but weakly in that of the LS ( L ) group. (B) Two-dimensional PAGE images of sialidase-treated LV fraction 3. Proteins transferred to membranes were subjected to SYPRO Ruby staining, and then to ACA lectin blotting. Insets show magnified images of two spots used for protein identification. (C) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of recombinant human CSRP3. Recombinant proteins expressed in E . coli (unglycosylated negative control) and in HEK293 cells (potentially glycosylated reference) were analyzed after treatment with sialidase and O -glycosidase. (D) Relative expression levels of Csrp3 in the LV tissues. qPCR data were normalized to Tbp expression levels. The numbers of examined rats were n = 12 and n = 15 for HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (E) Protein levels of CSRP3 in LV extracts. Densitometry analysis data of western blotting are shown (n = 6). (D,E) The data are presented as the fold change compared with LS rats at 12 weeks. (F) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of CSRP3 from LV extracts of DS rats. CSRP3 in LV extracts was immunoprecipitated, denatured, separated by SDS-PAGE, and analyzed. Recombinant human CSRP3 was used as an experimental control of immunoprecipitation with anti-CSRP3 antibody (+) or normal IgG (-). Lower panel shows densitometry analysis data; the intensity of each band in LB was normalized to that in WB (n = 6). (G) Effects of glycosidases on CSRP3 dimerization. LV extracts from three HS ( H ) or LS ( L ) rats at 16 weeks were treated with three glycosidases as indicated and then analyzed by western blotting for CSRP3. Arrows indicate the bands corresponding to monomers and dimers. Lower panels show densitometry analysis from five experiments; dimer/monomer ratios are presented as the fold change compared with LS rats without glycosidase treatment. (D-G) *, p
    Sialidase, supplied by New England Biolabs, 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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    New England Biolabs α2 3 neuraminidase
    Impact of Fc Glycosylation (A) Impact of Fc glycosylation on neutralizing activity. Comparison of the neutralizing activities of wild-type IgG1, wild-type IgA1, and IgA1 in which the glycosylation consensus sequences at position 263 or 459 have been removed. (B) Comparison of the complex glycoforms of IgG1 and IgA1 and the oligomannose-type glycoform of IgA1 expressed in 293S cells (IgA S). (C) Impact of neuraminidase treatment on the neutralization of rg-A/Chicken/Vietnam/C58/2004 (H5N3). The neutralizing activity of the indicated antibodies incubated either with <t>α2–3</t> neuraminidase from Salmonella typhimurium LT2 (NA S) or α2–3,6,8,9 neuraminidase A from Arthrobacter ureafaciens (NA A) was compared to that of the mock-treated IgA1 and IgG1 molecules. (D) Impact of Fc glycosylation on hemagglutination inhibition. A constant amount of the indicated virus was incubated with titrated amounts of the indicated antibodies and added to chicken erythrocytes that were then allowed to sediment at room temperature. (E) Impact of prolonged incubation with virus. Virus and titrated amounts of the indicated isotype of mAb 3.1 were incubated for either 1 hr or overnight before residual infectivity was determined.
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    New England Biolabs neuraminidase a
    Impact of Fc Glycosylation (A) Impact of Fc glycosylation on neutralizing activity. Comparison of the neutralizing activities of wild-type IgG1, wild-type IgA1, and IgA1 in which the glycosylation consensus sequences at position 263 or 459 have been removed. (B) Comparison of the complex glycoforms of IgG1 and IgA1 and the oligomannose-type glycoform of IgA1 expressed in 293S cells (IgA S). (C) Impact of neuraminidase treatment on the neutralization of rg-A/Chicken/Vietnam/C58/2004 (H5N3). The neutralizing activity of the indicated antibodies incubated either with α2–3 neuraminidase from Salmonella typhimurium LT2 (NA S) or α2–3,6,8,9 <t>neuraminidase</t> A from Arthrobacter ureafaciens (NA A) was compared to that of the mock-treated IgA1 and IgG1 molecules. (D) Impact of Fc glycosylation on hemagglutination inhibition. A constant amount of the indicated virus was incubated with titrated amounts of the indicated antibodies and added to chicken erythrocytes that were then allowed to sediment at room temperature. (E) Impact of prolonged incubation with virus. Virus and titrated amounts of the indicated isotype of mAb 3.1 were incubated for either 1 hr or overnight before residual infectivity was determined.
    Neuraminidase A, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Composition of substitution mutations with respect to consensus sequences. Percentages represent the mean across eight M. synoviae strains for nanI , nagA , nanA , nagC , nanE , and nagB genes of the sialidase locus, and three M. hyopneumoniae strains for housekeeping genes dnaA and ftsY .

    Journal: Microbial pathogenesis

    Article Title: Genetic Variation in Sialidase and Linkage to N-acetylneuraminate Catabolism in Mycoplasma synoviae

    doi: 10.1016/j.micpath.2008.02.002

    Figure Lengend Snippet: Composition of substitution mutations with respect to consensus sequences. Percentages represent the mean across eight M. synoviae strains for nanI , nagA , nanA , nagC , nanE , and nagB genes of the sialidase locus, and three M. hyopneumoniae strains for housekeeping genes dnaA and ftsY .

    Article Snippet: Genomic DNA from the strains with the highest (WVU1853T ) and lowest (K4907A and K5395B) levels of sialidase activity was digested with endonuclease Vsp I (New England Biolabs, Ipswich, Massachusetts), then separated on a 0.6% agarose gel.

    Techniques:

    Altered O -glycosylation on CSRP3 in the LV of DS hypertensive rats. (A) ACA lectin blot analysis and SYPRO Ruby staining of fractions from sialidase-treated LV extracts. Arrow indicates the ACA-positive band, which is observed strongly in fraction 3 of HS ( H ) but weakly in that of the LS ( L ) group. (B) Two-dimensional PAGE images of sialidase-treated LV fraction 3. Proteins transferred to membranes were subjected to SYPRO Ruby staining, and then to ACA lectin blotting. Insets show magnified images of two spots used for protein identification. (C) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of recombinant human CSRP3. Recombinant proteins expressed in E . coli (unglycosylated negative control) and in HEK293 cells (potentially glycosylated reference) were analyzed after treatment with sialidase and O -glycosidase. (D) Relative expression levels of Csrp3 in the LV tissues. qPCR data were normalized to Tbp expression levels. The numbers of examined rats were n = 12 and n = 15 for HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (E) Protein levels of CSRP3 in LV extracts. Densitometry analysis data of western blotting are shown (n = 6). (D,E) The data are presented as the fold change compared with LS rats at 12 weeks. (F) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of CSRP3 from LV extracts of DS rats. CSRP3 in LV extracts was immunoprecipitated, denatured, separated by SDS-PAGE, and analyzed. Recombinant human CSRP3 was used as an experimental control of immunoprecipitation with anti-CSRP3 antibody (+) or normal IgG (-). Lower panel shows densitometry analysis data; the intensity of each band in LB was normalized to that in WB (n = 6). (G) Effects of glycosidases on CSRP3 dimerization. LV extracts from three HS ( H ) or LS ( L ) rats at 16 weeks were treated with three glycosidases as indicated and then analyzed by western blotting for CSRP3. Arrows indicate the bands corresponding to monomers and dimers. Lower panels show densitometry analysis from five experiments; dimer/monomer ratios are presented as the fold change compared with LS rats without glycosidase treatment. (D-G) *, p

    Journal: PLoS ONE

    Article Title: Aberrant Glycosylation in the Left Ventricle and Plasma of Rats with Cardiac Hypertrophy and Heart Failure

    doi: 10.1371/journal.pone.0150210

    Figure Lengend Snippet: Altered O -glycosylation on CSRP3 in the LV of DS hypertensive rats. (A) ACA lectin blot analysis and SYPRO Ruby staining of fractions from sialidase-treated LV extracts. Arrow indicates the ACA-positive band, which is observed strongly in fraction 3 of HS ( H ) but weakly in that of the LS ( L ) group. (B) Two-dimensional PAGE images of sialidase-treated LV fraction 3. Proteins transferred to membranes were subjected to SYPRO Ruby staining, and then to ACA lectin blotting. Insets show magnified images of two spots used for protein identification. (C) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of recombinant human CSRP3. Recombinant proteins expressed in E . coli (unglycosylated negative control) and in HEK293 cells (potentially glycosylated reference) were analyzed after treatment with sialidase and O -glycosidase. (D) Relative expression levels of Csrp3 in the LV tissues. qPCR data were normalized to Tbp expression levels. The numbers of examined rats were n = 12 and n = 15 for HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (E) Protein levels of CSRP3 in LV extracts. Densitometry analysis data of western blotting are shown (n = 6). (D,E) The data are presented as the fold change compared with LS rats at 12 weeks. (F) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of CSRP3 from LV extracts of DS rats. CSRP3 in LV extracts was immunoprecipitated, denatured, separated by SDS-PAGE, and analyzed. Recombinant human CSRP3 was used as an experimental control of immunoprecipitation with anti-CSRP3 antibody (+) or normal IgG (-). Lower panel shows densitometry analysis data; the intensity of each band in LB was normalized to that in WB (n = 6). (G) Effects of glycosidases on CSRP3 dimerization. LV extracts from three HS ( H ) or LS ( L ) rats at 16 weeks were treated with three glycosidases as indicated and then analyzed by western blotting for CSRP3. Arrows indicate the bands corresponding to monomers and dimers. Lower panels show densitometry analysis from five experiments; dimer/monomer ratios are presented as the fold change compared with LS rats without glycosidase treatment. (D-G) *, p

    Article Snippet: Protein deglycosylation LV extracts prepared for western blot and lectin blot analyses and recombinant proteins were treated with glycosidases, including sialidase, O -glycosidase, and PNGase F, which were all obtained from New England Biolabs (Beverly, MA).

    Techniques: Staining, Polyacrylamide Gel Electrophoresis, Western Blot, Recombinant, Negative Control, Expressing, Real-time Polymerase Chain Reaction, Immunoprecipitation, SDS Page

    Altered mucin-type O -glycosylation in the LV of DS hypertensive rats. (A) T-synthase activity in LV extracts. Data were normalized to protein content. (B) Correlation of T-synthase activity with ANP gene expression. ANP gene expression level was quantified by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (C) Correlation of T-synthase activity with ejection fraction. (D) Relative expression levels of glycogenes involved in the early stage of mucin-type O -glycosylation in the LV tissues of DS rats were analyzed by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (E) Schematic summary of gene expression analysis data shown in (D). Examined glycosyltransferases in the mucin-type O -glycosylation pathway are shown in red (upregulated), blue (downregulated), or black (no change) letters. Relatively rare core structures (core 5, 6, 7, and 8) synthesized from Tn are omitted. The biosynthetic pathway of disialyl-T is upregulated, as indicated with bold arrows. GalNAc, N -acetylgalactosamine; GlcNAc, N -acetylglucosamine; Gal, galactose; NeuAc, N -acetylneuraminic acid. (F) Lectin blot analysis of sialidase-treated LV extracts using ACA. Representative images demonstrate ACA-reactive glycoproteins and SYPRO Ruby-stained total proteins of three individual rats in each group. Lower panel shows densitometry analysis; intensity of each band was normalized to total protein amount. Data are presented as the fold change (n = 6) compared with sialidase-untreated LV extracts of HS rats at 12 weeks. (A,D) The numbers of examined rats were n = 12 and n = 15 for the HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (A,D,F) *, p

    Journal: PLoS ONE

    Article Title: Aberrant Glycosylation in the Left Ventricle and Plasma of Rats with Cardiac Hypertrophy and Heart Failure

    doi: 10.1371/journal.pone.0150210

    Figure Lengend Snippet: Altered mucin-type O -glycosylation in the LV of DS hypertensive rats. (A) T-synthase activity in LV extracts. Data were normalized to protein content. (B) Correlation of T-synthase activity with ANP gene expression. ANP gene expression level was quantified by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (C) Correlation of T-synthase activity with ejection fraction. (D) Relative expression levels of glycogenes involved in the early stage of mucin-type O -glycosylation in the LV tissues of DS rats were analyzed by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (E) Schematic summary of gene expression analysis data shown in (D). Examined glycosyltransferases in the mucin-type O -glycosylation pathway are shown in red (upregulated), blue (downregulated), or black (no change) letters. Relatively rare core structures (core 5, 6, 7, and 8) synthesized from Tn are omitted. The biosynthetic pathway of disialyl-T is upregulated, as indicated with bold arrows. GalNAc, N -acetylgalactosamine; GlcNAc, N -acetylglucosamine; Gal, galactose; NeuAc, N -acetylneuraminic acid. (F) Lectin blot analysis of sialidase-treated LV extracts using ACA. Representative images demonstrate ACA-reactive glycoproteins and SYPRO Ruby-stained total proteins of three individual rats in each group. Lower panel shows densitometry analysis; intensity of each band was normalized to total protein amount. Data are presented as the fold change (n = 6) compared with sialidase-untreated LV extracts of HS rats at 12 weeks. (A,D) The numbers of examined rats were n = 12 and n = 15 for the HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (A,D,F) *, p

    Article Snippet: Protein deglycosylation LV extracts prepared for western blot and lectin blot analyses and recombinant proteins were treated with glycosidases, including sialidase, O -glycosidase, and PNGase F, which were all obtained from New England Biolabs (Beverly, MA).

    Techniques: Activity Assay, Aqueous Normal-phase Chromatography, Expressing, Real-time Polymerase Chain Reaction, Synthesized, Staining

    Impact of Fc Glycosylation (A) Impact of Fc glycosylation on neutralizing activity. Comparison of the neutralizing activities of wild-type IgG1, wild-type IgA1, and IgA1 in which the glycosylation consensus sequences at position 263 or 459 have been removed. (B) Comparison of the complex glycoforms of IgG1 and IgA1 and the oligomannose-type glycoform of IgA1 expressed in 293S cells (IgA S). (C) Impact of neuraminidase treatment on the neutralization of rg-A/Chicken/Vietnam/C58/2004 (H5N3). The neutralizing activity of the indicated antibodies incubated either with α2–3 neuraminidase from Salmonella typhimurium LT2 (NA S) or α2–3,6,8,9 neuraminidase A from Arthrobacter ureafaciens (NA A) was compared to that of the mock-treated IgA1 and IgG1 molecules. (D) Impact of Fc glycosylation on hemagglutination inhibition. A constant amount of the indicated virus was incubated with titrated amounts of the indicated antibodies and added to chicken erythrocytes that were then allowed to sediment at room temperature. (E) Impact of prolonged incubation with virus. Virus and titrated amounts of the indicated isotype of mAb 3.1 were incubated for either 1 hr or overnight before residual infectivity was determined.

    Journal: Cell Reports

    Article Title: Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses

    doi: 10.1016/j.celrep.2018.03.027

    Figure Lengend Snippet: Impact of Fc Glycosylation (A) Impact of Fc glycosylation on neutralizing activity. Comparison of the neutralizing activities of wild-type IgG1, wild-type IgA1, and IgA1 in which the glycosylation consensus sequences at position 263 or 459 have been removed. (B) Comparison of the complex glycoforms of IgG1 and IgA1 and the oligomannose-type glycoform of IgA1 expressed in 293S cells (IgA S). (C) Impact of neuraminidase treatment on the neutralization of rg-A/Chicken/Vietnam/C58/2004 (H5N3). The neutralizing activity of the indicated antibodies incubated either with α2–3 neuraminidase from Salmonella typhimurium LT2 (NA S) or α2–3,6,8,9 neuraminidase A from Arthrobacter ureafaciens (NA A) was compared to that of the mock-treated IgA1 and IgG1 molecules. (D) Impact of Fc glycosylation on hemagglutination inhibition. A constant amount of the indicated virus was incubated with titrated amounts of the indicated antibodies and added to chicken erythrocytes that were then allowed to sediment at room temperature. (E) Impact of prolonged incubation with virus. Virus and titrated amounts of the indicated isotype of mAb 3.1 were incubated for either 1 hr or overnight before residual infectivity was determined.

    Article Snippet: Exoglycosidase Sequencing of N-Linked Glycans The 2-AA labeled glycans were sequentially digested using the following exoglycosidases according to the manufacturers’ instructions: α2-3,6,8 neuraminidase from Clostridium perfringens (New England Biolabs, Hertfordshire, UK), α2-3 neuraminidase from Streptococcus pneumoniae (New England BioLabs, Hertfordshire, UK), β1,4-galactosidase from Bacteroides fragilis (New England Biolabs, Hertfordshire, UK), and α-L-fucosidase from bovine kidney (Sigma-Aldrich, Dorset, UK), β-N -acetylglucosaminidase from Xanthomonas manihotis (New England Biolabs, Hertfordshire, UK), and α(1–2,3,6)-mannosidase from Jack bean (Sigma-Aldrich, Dorset, UK).

    Techniques: Activity Assay, Neutralization, Incubation, HI Assay, Infection

    Impact of Fc Glycosylation (A) Impact of Fc glycosylation on neutralizing activity. Comparison of the neutralizing activities of wild-type IgG1, wild-type IgA1, and IgA1 in which the glycosylation consensus sequences at position 263 or 459 have been removed. (B) Comparison of the complex glycoforms of IgG1 and IgA1 and the oligomannose-type glycoform of IgA1 expressed in 293S cells (IgA S). (C) Impact of neuraminidase treatment on the neutralization of rg-A/Chicken/Vietnam/C58/2004 (H5N3). The neutralizing activity of the indicated antibodies incubated either with α2–3 neuraminidase from Salmonella typhimurium LT2 (NA S) or α2–3,6,8,9 neuraminidase A from Arthrobacter ureafaciens (NA A) was compared to that of the mock-treated IgA1 and IgG1 molecules. (D) Impact of Fc glycosylation on hemagglutination inhibition. A constant amount of the indicated virus was incubated with titrated amounts of the indicated antibodies and added to chicken erythrocytes that were then allowed to sediment at room temperature. (E) Impact of prolonged incubation with virus. Virus and titrated amounts of the indicated isotype of mAb 3.1 were incubated for either 1 hr or overnight before residual infectivity was determined.

    Journal: Cell Reports

    Article Title: Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses

    doi: 10.1016/j.celrep.2018.03.027

    Figure Lengend Snippet: Impact of Fc Glycosylation (A) Impact of Fc glycosylation on neutralizing activity. Comparison of the neutralizing activities of wild-type IgG1, wild-type IgA1, and IgA1 in which the glycosylation consensus sequences at position 263 or 459 have been removed. (B) Comparison of the complex glycoforms of IgG1 and IgA1 and the oligomannose-type glycoform of IgA1 expressed in 293S cells (IgA S). (C) Impact of neuraminidase treatment on the neutralization of rg-A/Chicken/Vietnam/C58/2004 (H5N3). The neutralizing activity of the indicated antibodies incubated either with α2–3 neuraminidase from Salmonella typhimurium LT2 (NA S) or α2–3,6,8,9 neuraminidase A from Arthrobacter ureafaciens (NA A) was compared to that of the mock-treated IgA1 and IgG1 molecules. (D) Impact of Fc glycosylation on hemagglutination inhibition. A constant amount of the indicated virus was incubated with titrated amounts of the indicated antibodies and added to chicken erythrocytes that were then allowed to sediment at room temperature. (E) Impact of prolonged incubation with virus. Virus and titrated amounts of the indicated isotype of mAb 3.1 were incubated for either 1 hr or overnight before residual infectivity was determined.

    Article Snippet: Neuraminidase Treatment Neuraminidase S (α2-3: New England Biolabs, Ipswich, MA, USA) and neuraminidase A (α2-3,6,8,9: New England Biolabs, Ipswich, MA, USA) were used to desialylate IgA1.

    Techniques: Activity Assay, Neutralization, Incubation, HI Assay, Infection