basigin  (Sino Biological)


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    Name:
    Human CD147 EMMPRIN Basigin Protein His Tag
    Description:
    A DNA sequence encoding the extracellular domain Met 1 His 205 of human CD147 NP 940991 1 precursor was expressed with the fused polyhistidine tag at the C terminus
    Catalog Number:
    10186-H08H
    Price:
    None
    Category:
    recombinant protein
    Host:
    HEK293 Cells
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    Structured Review

    Sino Biological basigin
    Cyclophilin B interacts with <t>Basigin</t> (CD147/BSG), a critical merozoite invasion receptor on RBCs. a Co-localization of CypB and BSG on the surface of the RBC. RBCs were fixed and incubated with anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies. The cells were stained with fluorochrome-conjugated secondary antibodies against CypB (green) and BSG (red) followed by confocal microscopy. CypB and BSG co-localized on the RBC surface with a Pearson’s coefficient of 0.53. b Merozoites were incubated with 25 µM of BSG protein for 2 h and detection was carried out using anti-CD147 antibody (rabbit polyclonal) and secondary fluorochrome-conjugated (red), followed by confocal microscopy. c CypB and BSG bind together on the merozoite surface. Merozoites were incubated with CypB and BSG proteins (25 µM each) for 2 h and binding was detected using anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies followed by secondary antibodies and confocal microscopy. Supplementary Fig. 5 illustrates in vitro interaction assays between CypB and BSG. Scale bar = 5 µm
    A DNA sequence encoding the extracellular domain Met 1 His 205 of human CD147 NP 940991 1 precursor was expressed with the fused polyhistidine tag at the C terminus
    https://www.bioz.com/result/basigin/product/Sino Biological
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    basigin - by Bioz Stars, 2021-06
    90/100 stars

    Images

    1) Product Images from "Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum"

    Article Title: Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum

    Journal: Nature Communications

    doi: 10.1038/s41467-017-01638-6

    Cyclophilin B interacts with Basigin (CD147/BSG), a critical merozoite invasion receptor on RBCs. a Co-localization of CypB and BSG on the surface of the RBC. RBCs were fixed and incubated with anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies. The cells were stained with fluorochrome-conjugated secondary antibodies against CypB (green) and BSG (red) followed by confocal microscopy. CypB and BSG co-localized on the RBC surface with a Pearson’s coefficient of 0.53. b Merozoites were incubated with 25 µM of BSG protein for 2 h and detection was carried out using anti-CD147 antibody (rabbit polyclonal) and secondary fluorochrome-conjugated (red), followed by confocal microscopy. c CypB and BSG bind together on the merozoite surface. Merozoites were incubated with CypB and BSG proteins (25 µM each) for 2 h and binding was detected using anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies followed by secondary antibodies and confocal microscopy. Supplementary Fig. 5 illustrates in vitro interaction assays between CypB and BSG. Scale bar = 5 µm
    Figure Legend Snippet: Cyclophilin B interacts with Basigin (CD147/BSG), a critical merozoite invasion receptor on RBCs. a Co-localization of CypB and BSG on the surface of the RBC. RBCs were fixed and incubated with anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies. The cells were stained with fluorochrome-conjugated secondary antibodies against CypB (green) and BSG (red) followed by confocal microscopy. CypB and BSG co-localized on the RBC surface with a Pearson’s coefficient of 0.53. b Merozoites were incubated with 25 µM of BSG protein for 2 h and detection was carried out using anti-CD147 antibody (rabbit polyclonal) and secondary fluorochrome-conjugated (red), followed by confocal microscopy. c CypB and BSG bind together on the merozoite surface. Merozoites were incubated with CypB and BSG proteins (25 µM each) for 2 h and binding was detected using anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies followed by secondary antibodies and confocal microscopy. Supplementary Fig. 5 illustrates in vitro interaction assays between CypB and BSG. Scale bar = 5 µm

    Techniques Used: Incubation, Staining, Confocal Microscopy, Binding Assay, In Vitro

    2) Product Images from "Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum"

    Article Title: Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum

    Journal: Nature Communications

    doi: 10.1038/s41467-017-01638-6

    Cyclophilin B interacts with Basigin (CD147/BSG), a critical merozoite invasion receptor on RBCs. a Co-localization of CypB and BSG on the surface of the RBC. RBCs were fixed and incubated with anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies. The cells were stained with fluorochrome-conjugated secondary antibodies against CypB (green) and BSG (red) followed by confocal microscopy. CypB and BSG co-localized on the RBC surface with a Pearson’s coefficient of 0.53. b Merozoites were incubated with 25 µM of BSG protein for 2 h and detection was carried out using anti-CD147 antibody (rabbit polyclonal) and secondary fluorochrome-conjugated (red), followed by confocal microscopy. c CypB and BSG bind together on the merozoite surface. Merozoites were incubated with CypB and BSG proteins (25 µM each) for 2 h and binding was detected using anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies followed by secondary antibodies and confocal microscopy. Supplementary Fig. 5 illustrates in vitro interaction assays between CypB and BSG. Scale bar = 5 µm
    Figure Legend Snippet: Cyclophilin B interacts with Basigin (CD147/BSG), a critical merozoite invasion receptor on RBCs. a Co-localization of CypB and BSG on the surface of the RBC. RBCs were fixed and incubated with anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies. The cells were stained with fluorochrome-conjugated secondary antibodies against CypB (green) and BSG (red) followed by confocal microscopy. CypB and BSG co-localized on the RBC surface with a Pearson’s coefficient of 0.53. b Merozoites were incubated with 25 µM of BSG protein for 2 h and detection was carried out using anti-CD147 antibody (rabbit polyclonal) and secondary fluorochrome-conjugated (red), followed by confocal microscopy. c CypB and BSG bind together on the merozoite surface. Merozoites were incubated with CypB and BSG proteins (25 µM each) for 2 h and binding was detected using anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies followed by secondary antibodies and confocal microscopy. Supplementary Fig. 5 illustrates in vitro interaction assays between CypB and BSG. Scale bar = 5 µm

    Techniques Used: Incubation, Staining, Confocal Microscopy, Binding Assay, In Vitro

    Related Articles

    In Vitro:

    Article Title: Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum
    Article Snippet: Purified CDP3 was analyzed for the presence of Endotoxins using LAL (Limulus amebocyte lysate) gel clot assay kit provided by Charle’s River and it was found to be free of endotoxins. .. In vitro protein−protein interaction studiesRecombinant proteins Cyclophilin B (Catlog: 11004-H08H-100) and Basigin (BSG/CD147, Catlog: 10186-H08H-100) were obtained commercially from Sino Biological Inc., China (Supplementary Fig. ). .. To check the specificity of antibodies that have been used in present study, western blot analysis was performed to detect the native proteins (Supplementary Figs. , , Supplementary Table ).

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    Sino Biological basigin
    Cyclophilin B interacts with <t>Basigin</t> (CD147/BSG), a critical merozoite invasion receptor on RBCs. a Co-localization of CypB and BSG on the surface of the RBC. RBCs were fixed and incubated with anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies. The cells were stained with fluorochrome-conjugated secondary antibodies against CypB (green) and BSG (red) followed by confocal microscopy. CypB and BSG co-localized on the RBC surface with a Pearson’s coefficient of 0.53. b Merozoites were incubated with 25 µM of BSG protein for 2 h and detection was carried out using anti-CD147 antibody (rabbit polyclonal) and secondary fluorochrome-conjugated (red), followed by confocal microscopy. c CypB and BSG bind together on the merozoite surface. Merozoites were incubated with CypB and BSG proteins (25 µM each) for 2 h and binding was detected using anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies followed by secondary antibodies and confocal microscopy. Supplementary Fig. 5 illustrates in vitro interaction assays between CypB and BSG. Scale bar = 5 µm
    Basigin, supplied by Sino Biological, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/basigin/product/Sino Biological
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    basigin - by Bioz Stars, 2021-06
    90/100 stars
      Buy from Supplier

    90
    Sino Biological human basigin cdna
    A, schematic diagram depicting the Label transfer method. The GST-tagged PvTRAg38 was incubated with biotin-labeled sulfo-SBED cross-linker. The labeled protein was incubated with erythrocyte membrane proteins, followed by exposure to UV light that photoactivates a photoreactive moiety (represented by orange triangle PR ) of trifunctional cross-linker, which will bind to the interacting protein. The Label transfer (represented by blue circle B ) was completed by cleaving the spacer arm to release the bait protein by reducing it with DTT. The protein-protein interaction between PvTRAg38 and erythrocyte membrane proteins was detected either by MuDPIT analysis from eluates or by probing eluates with streptavidin-HRP-based Western blot. B, identification of erythrocyte membrane proteins interacting with recombinant PvTRAg38 during Label transfer assay. Erythrocyte membrane proteins extracted with 1% C 12 E 8 were incubated with recombinant GST-tagged PvTRAg38 (labeled with trifunctional Sulfo-SBED cross-linker), washed and resolved on 15% SDS-PAGE, and transferred to nitrocellulose membrane. The blot was probed with streptavidin-HRP. Lane M, molecular weight marker. Lane 1, recombinant GST-tagged PvTRAg38 (labeled with biotin-labeled cross-linker). Lane 2, erythrocyte membrane extract incubated with labeled GST-tagged PvTRAg38. Label transferred to erythrocyte proteins in lane 2 are named on right-hand side. SCFP1 , solute-carrier family protein 1. C, detection of <t>basigin</t> in eluates by Western blotting analysis. Eluate was from the Label transfer assay where labeled GST-tagged PvTRAg38 was incubated with reticulocyte-enriched RBCs; membrane lysate was resolved on 15% SDS-PAGE, and protein bands were transferred to nitrocellulose membrane. The blot was probed with anti-basigin antibody ( lane 1 ). Lane M, molecular weight marker lane. Sizes of marker proteins are shown on right-hand side .
    Human Basigin Cdna, supplied by Sino Biological, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human basigin cdna/product/Sino Biological
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    human basigin cdna - by Bioz Stars, 2021-06
    90/100 stars
      Buy from Supplier

    N/A
    The mature form of human CD147 NP 940991 1 extracellular domain Met 1 His 205 with quinary aa peptide DDDDK at the C terminus was expressed and purified
      Buy from Supplier

    N/A
    This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified recombinant Human CD147 EMMPRIN Basigin
      Buy from Supplier

    Image Search Results


    Cyclophilin B interacts with Basigin (CD147/BSG), a critical merozoite invasion receptor on RBCs. a Co-localization of CypB and BSG on the surface of the RBC. RBCs were fixed and incubated with anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies. The cells were stained with fluorochrome-conjugated secondary antibodies against CypB (green) and BSG (red) followed by confocal microscopy. CypB and BSG co-localized on the RBC surface with a Pearson’s coefficient of 0.53. b Merozoites were incubated with 25 µM of BSG protein for 2 h and detection was carried out using anti-CD147 antibody (rabbit polyclonal) and secondary fluorochrome-conjugated (red), followed by confocal microscopy. c CypB and BSG bind together on the merozoite surface. Merozoites were incubated with CypB and BSG proteins (25 µM each) for 2 h and binding was detected using anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies followed by secondary antibodies and confocal microscopy. Supplementary Fig. 5 illustrates in vitro interaction assays between CypB and BSG. Scale bar = 5 µm

    Journal: Nature Communications

    Article Title: Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum

    doi: 10.1038/s41467-017-01638-6

    Figure Lengend Snippet: Cyclophilin B interacts with Basigin (CD147/BSG), a critical merozoite invasion receptor on RBCs. a Co-localization of CypB and BSG on the surface of the RBC. RBCs were fixed and incubated with anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies. The cells were stained with fluorochrome-conjugated secondary antibodies against CypB (green) and BSG (red) followed by confocal microscopy. CypB and BSG co-localized on the RBC surface with a Pearson’s coefficient of 0.53. b Merozoites were incubated with 25 µM of BSG protein for 2 h and detection was carried out using anti-CD147 antibody (rabbit polyclonal) and secondary fluorochrome-conjugated (red), followed by confocal microscopy. c CypB and BSG bind together on the merozoite surface. Merozoites were incubated with CypB and BSG proteins (25 µM each) for 2 h and binding was detected using anti-CypB (mouse monoclonal) and anti-BSG (rabbit polyclonal) antibodies followed by secondary antibodies and confocal microscopy. Supplementary Fig. 5 illustrates in vitro interaction assays between CypB and BSG. Scale bar = 5 µm

    Article Snippet: In vitro protein−protein interaction studies Recombinant proteins Cyclophilin B (Catlog: 11004-H08H-100) and Basigin (BSG/CD147, Catlog: 10186-H08H-100) were obtained commercially from Sino Biological Inc., China (Supplementary Fig. ).

    Techniques: Incubation, Staining, Confocal Microscopy, Binding Assay, In Vitro

    A, schematic diagram depicting the Label transfer method. The GST-tagged PvTRAg38 was incubated with biotin-labeled sulfo-SBED cross-linker. The labeled protein was incubated with erythrocyte membrane proteins, followed by exposure to UV light that photoactivates a photoreactive moiety (represented by orange triangle PR ) of trifunctional cross-linker, which will bind to the interacting protein. The Label transfer (represented by blue circle B ) was completed by cleaving the spacer arm to release the bait protein by reducing it with DTT. The protein-protein interaction between PvTRAg38 and erythrocyte membrane proteins was detected either by MuDPIT analysis from eluates or by probing eluates with streptavidin-HRP-based Western blot. B, identification of erythrocyte membrane proteins interacting with recombinant PvTRAg38 during Label transfer assay. Erythrocyte membrane proteins extracted with 1% C 12 E 8 were incubated with recombinant GST-tagged PvTRAg38 (labeled with trifunctional Sulfo-SBED cross-linker), washed and resolved on 15% SDS-PAGE, and transferred to nitrocellulose membrane. The blot was probed with streptavidin-HRP. Lane M, molecular weight marker. Lane 1, recombinant GST-tagged PvTRAg38 (labeled with biotin-labeled cross-linker). Lane 2, erythrocyte membrane extract incubated with labeled GST-tagged PvTRAg38. Label transferred to erythrocyte proteins in lane 2 are named on right-hand side. SCFP1 , solute-carrier family protein 1. C, detection of basigin in eluates by Western blotting analysis. Eluate was from the Label transfer assay where labeled GST-tagged PvTRAg38 was incubated with reticulocyte-enriched RBCs; membrane lysate was resolved on 15% SDS-PAGE, and protein bands were transferred to nitrocellulose membrane. The blot was probed with anti-basigin antibody ( lane 1 ). Lane M, molecular weight marker lane. Sizes of marker proteins are shown on right-hand side .

    Journal: The Journal of Biological Chemistry

    Article Title: Basigin Interacts with Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 as a Second Erythrocyte Receptor to Promote Parasite Growth *

    doi: 10.1074/jbc.M116.744367

    Figure Lengend Snippet: A, schematic diagram depicting the Label transfer method. The GST-tagged PvTRAg38 was incubated with biotin-labeled sulfo-SBED cross-linker. The labeled protein was incubated with erythrocyte membrane proteins, followed by exposure to UV light that photoactivates a photoreactive moiety (represented by orange triangle PR ) of trifunctional cross-linker, which will bind to the interacting protein. The Label transfer (represented by blue circle B ) was completed by cleaving the spacer arm to release the bait protein by reducing it with DTT. The protein-protein interaction between PvTRAg38 and erythrocyte membrane proteins was detected either by MuDPIT analysis from eluates or by probing eluates with streptavidin-HRP-based Western blot. B, identification of erythrocyte membrane proteins interacting with recombinant PvTRAg38 during Label transfer assay. Erythrocyte membrane proteins extracted with 1% C 12 E 8 were incubated with recombinant GST-tagged PvTRAg38 (labeled with trifunctional Sulfo-SBED cross-linker), washed and resolved on 15% SDS-PAGE, and transferred to nitrocellulose membrane. The blot was probed with streptavidin-HRP. Lane M, molecular weight marker. Lane 1, recombinant GST-tagged PvTRAg38 (labeled with biotin-labeled cross-linker). Lane 2, erythrocyte membrane extract incubated with labeled GST-tagged PvTRAg38. Label transferred to erythrocyte proteins in lane 2 are named on right-hand side. SCFP1 , solute-carrier family protein 1. C, detection of basigin in eluates by Western blotting analysis. Eluate was from the Label transfer assay where labeled GST-tagged PvTRAg38 was incubated with reticulocyte-enriched RBCs; membrane lysate was resolved on 15% SDS-PAGE, and protein bands were transferred to nitrocellulose membrane. The blot was probed with anti-basigin antibody ( lane 1 ). Lane M, molecular weight marker lane. Sizes of marker proteins are shown on right-hand side .

    Article Snippet: The following were commercially obtained: human basigin cDNA clone, mammalian expressed recombinant histidine-tagged CD59 (Sino Biological, Beijing, China); human erythrocyte 55-kDa membrane protein (GeneCopoeia, Rockville, MD); Alexa Fluor 488-conjugated goat anti-mouse and anti-rabbit IgG, proofreading Pfx polymerase enzyme (Invitrogen Life Technologies, Inc.); sulfo-SBED-biotin Label transfer cross-linker (sulfosuccinimidyl-2-[6-(biotin amide)-2-( p -azidobenzamido)hexanoamido] ethyl-1,3′-dithiopropionate) (Thermo Scientific, Rockford, IL); GeneJET gel extraction kit (Thermo Scientific, Waltham, MA); HEK-293 cells (American Type Culture Collection (ATCC), Manassas, VA); RPMI 1640 medium, hypoxanthine, penicillin/streptomycin, fetal calf serum, glutamine, glutaraldehyde, poly- l -lysine, monoclonal antibodies against basigin (Clone MEM-M6); His6 and GST (Sigma); Lipofectamine® 2000, synthetic peptides (Thermo Fisher Scientific, GmbH, Germany); mouse monoclonal antibodies DL6 (Santa Cruz Biotechnology, Dallas, TX); HBS-EP buffer (degassed and ready to use 0.01 m HEPES, pH 7.4, 0.15 m NaCl, 3 m m EDTA, 0.005% v/v surfactant P20); protein marker standards for GPC (GE Healthcare); Matchmaker Gold Systems (Clontech); and trypsin (Promega Corp., Madison, WI).

    Techniques: Incubation, Labeling, Western Blot, Recombinant, SDS Page, Molecular Weight, Marker

    Expression, purification, and biophysical characterization of recombinant basigin. A, SDS-PAGE analysis of the purified histidine-tagged recombinant basigin. The purified recombinant protein was resolved on 12% SDS-PAGE. Lane 1, purified histidine-tagged basigin. Lane M, molecular weight markers. B, circular dichroism spectra of purified histidine-tagged recombinant basigin. C, gel permeation chromatography profile of purified histidine-tagged basigin. Elution profile of molecular weight markers and purified histidine-tagged basigin are represented by gray and black lines , respectively.

    Journal: The Journal of Biological Chemistry

    Article Title: Basigin Interacts with Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 as a Second Erythrocyte Receptor to Promote Parasite Growth *

    doi: 10.1074/jbc.M116.744367

    Figure Lengend Snippet: Expression, purification, and biophysical characterization of recombinant basigin. A, SDS-PAGE analysis of the purified histidine-tagged recombinant basigin. The purified recombinant protein was resolved on 12% SDS-PAGE. Lane 1, purified histidine-tagged basigin. Lane M, molecular weight markers. B, circular dichroism spectra of purified histidine-tagged recombinant basigin. C, gel permeation chromatography profile of purified histidine-tagged basigin. Elution profile of molecular weight markers and purified histidine-tagged basigin are represented by gray and black lines , respectively.

    Article Snippet: The following were commercially obtained: human basigin cDNA clone, mammalian expressed recombinant histidine-tagged CD59 (Sino Biological, Beijing, China); human erythrocyte 55-kDa membrane protein (GeneCopoeia, Rockville, MD); Alexa Fluor 488-conjugated goat anti-mouse and anti-rabbit IgG, proofreading Pfx polymerase enzyme (Invitrogen Life Technologies, Inc.); sulfo-SBED-biotin Label transfer cross-linker (sulfosuccinimidyl-2-[6-(biotin amide)-2-( p -azidobenzamido)hexanoamido] ethyl-1,3′-dithiopropionate) (Thermo Scientific, Rockford, IL); GeneJET gel extraction kit (Thermo Scientific, Waltham, MA); HEK-293 cells (American Type Culture Collection (ATCC), Manassas, VA); RPMI 1640 medium, hypoxanthine, penicillin/streptomycin, fetal calf serum, glutamine, glutaraldehyde, poly- l -lysine, monoclonal antibodies against basigin (Clone MEM-M6); His6 and GST (Sigma); Lipofectamine® 2000, synthetic peptides (Thermo Fisher Scientific, GmbH, Germany); mouse monoclonal antibodies DL6 (Santa Cruz Biotechnology, Dallas, TX); HBS-EP buffer (degassed and ready to use 0.01 m HEPES, pH 7.4, 0.15 m NaCl, 3 m m EDTA, 0.005% v/v surfactant P20); protein marker standards for GPC (GE Healthcare); Matchmaker Gold Systems (Clontech); and trypsin (Promega Corp., Madison, WI).

    Techniques: Expressing, Purification, Recombinant, SDS Page, Molecular Weight, GPC Assay

    Assessment of basigin and PvTRAg38 interaction by mammalian expression system. The pRE4-basigin transfected HEK-293 cells expressing basigin on the surface ( upper panel ) or HEK-293 cells transfected with pRE4 vector alone ( lower panel ) were incubated with GST-tagged PvTRAg38 and then co-localized with anti-GST monoclonal and anti-basigin polyclonal antibodies. Secondary antibodies used were Alexa Fluor 488-tagged anti-mouse and Alexa Fluor 594-tagged anti-rabbit. Smears were mounted in DAPI anti-fade and sealed.

    Journal: The Journal of Biological Chemistry

    Article Title: Basigin Interacts with Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 as a Second Erythrocyte Receptor to Promote Parasite Growth *

    doi: 10.1074/jbc.M116.744367

    Figure Lengend Snippet: Assessment of basigin and PvTRAg38 interaction by mammalian expression system. The pRE4-basigin transfected HEK-293 cells expressing basigin on the surface ( upper panel ) or HEK-293 cells transfected with pRE4 vector alone ( lower panel ) were incubated with GST-tagged PvTRAg38 and then co-localized with anti-GST monoclonal and anti-basigin polyclonal antibodies. Secondary antibodies used were Alexa Fluor 488-tagged anti-mouse and Alexa Fluor 594-tagged anti-rabbit. Smears were mounted in DAPI anti-fade and sealed.

    Article Snippet: The following were commercially obtained: human basigin cDNA clone, mammalian expressed recombinant histidine-tagged CD59 (Sino Biological, Beijing, China); human erythrocyte 55-kDa membrane protein (GeneCopoeia, Rockville, MD); Alexa Fluor 488-conjugated goat anti-mouse and anti-rabbit IgG, proofreading Pfx polymerase enzyme (Invitrogen Life Technologies, Inc.); sulfo-SBED-biotin Label transfer cross-linker (sulfosuccinimidyl-2-[6-(biotin amide)-2-( p -azidobenzamido)hexanoamido] ethyl-1,3′-dithiopropionate) (Thermo Scientific, Rockford, IL); GeneJET gel extraction kit (Thermo Scientific, Waltham, MA); HEK-293 cells (American Type Culture Collection (ATCC), Manassas, VA); RPMI 1640 medium, hypoxanthine, penicillin/streptomycin, fetal calf serum, glutamine, glutaraldehyde, poly- l -lysine, monoclonal antibodies against basigin (Clone MEM-M6); His6 and GST (Sigma); Lipofectamine® 2000, synthetic peptides (Thermo Fisher Scientific, GmbH, Germany); mouse monoclonal antibodies DL6 (Santa Cruz Biotechnology, Dallas, TX); HBS-EP buffer (degassed and ready to use 0.01 m HEPES, pH 7.4, 0.15 m NaCl, 3 m m EDTA, 0.005% v/v surfactant P20); protein marker standards for GPC (GE Healthcare); Matchmaker Gold Systems (Clontech); and trypsin (Promega Corp., Madison, WI).

    Techniques: Expressing, Transfection, Plasmid Preparation, Incubation

    Putative binding sites of PvTRAg38 peptide P 2 on human basigin by molecular docking. A, depicted surface model represents P 2 peptide ( gray ) that was docked into the human basigin by computer simulation using Z-DOCK software. Ribbon representation of the human basigin ( pink ) and stick representation of the peptide P 2 ( yellow, with transparent electrostatic surface) are shown in zoomed image. B, schematic diagram showing details of interactions of peptide P 2 residues with neighboring residues of human basigin. Hydrogen bonds between Gln-12 (corresponding to Gln-178 of PvTRAg38)–Asp-77(basigin), Gly-5 (corresponding to Gly-171 of PvTRAg38)–Trp-82 (basigin), Lys-7 (corresponding to Lys-173 of PvTRAg38)–Asp79 (basigin), and Leu-9 (corresponding to Leu-175 of PvTRAg38)–Pro-104 (basigin) are shown ( green dashed lines ). Hydrophobic interactions are also depicted with dark red semi-circles . Most of the pictured hydrogen bonds are lost in alanine substitution. The figure was created using LIGPLOT.

    Journal: The Journal of Biological Chemistry

    Article Title: Basigin Interacts with Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 as a Second Erythrocyte Receptor to Promote Parasite Growth *

    doi: 10.1074/jbc.M116.744367

    Figure Lengend Snippet: Putative binding sites of PvTRAg38 peptide P 2 on human basigin by molecular docking. A, depicted surface model represents P 2 peptide ( gray ) that was docked into the human basigin by computer simulation using Z-DOCK software. Ribbon representation of the human basigin ( pink ) and stick representation of the peptide P 2 ( yellow, with transparent electrostatic surface) are shown in zoomed image. B, schematic diagram showing details of interactions of peptide P 2 residues with neighboring residues of human basigin. Hydrogen bonds between Gln-12 (corresponding to Gln-178 of PvTRAg38)–Asp-77(basigin), Gly-5 (corresponding to Gly-171 of PvTRAg38)–Trp-82 (basigin), Lys-7 (corresponding to Lys-173 of PvTRAg38)–Asp79 (basigin), and Leu-9 (corresponding to Leu-175 of PvTRAg38)–Pro-104 (basigin) are shown ( green dashed lines ). Hydrophobic interactions are also depicted with dark red semi-circles . Most of the pictured hydrogen bonds are lost in alanine substitution. The figure was created using LIGPLOT.

    Article Snippet: The following were commercially obtained: human basigin cDNA clone, mammalian expressed recombinant histidine-tagged CD59 (Sino Biological, Beijing, China); human erythrocyte 55-kDa membrane protein (GeneCopoeia, Rockville, MD); Alexa Fluor 488-conjugated goat anti-mouse and anti-rabbit IgG, proofreading Pfx polymerase enzyme (Invitrogen Life Technologies, Inc.); sulfo-SBED-biotin Label transfer cross-linker (sulfosuccinimidyl-2-[6-(biotin amide)-2-( p -azidobenzamido)hexanoamido] ethyl-1,3′-dithiopropionate) (Thermo Scientific, Rockford, IL); GeneJET gel extraction kit (Thermo Scientific, Waltham, MA); HEK-293 cells (American Type Culture Collection (ATCC), Manassas, VA); RPMI 1640 medium, hypoxanthine, penicillin/streptomycin, fetal calf serum, glutamine, glutaraldehyde, poly- l -lysine, monoclonal antibodies against basigin (Clone MEM-M6); His6 and GST (Sigma); Lipofectamine® 2000, synthetic peptides (Thermo Fisher Scientific, GmbH, Germany); mouse monoclonal antibodies DL6 (Santa Cruz Biotechnology, Dallas, TX); HBS-EP buffer (degassed and ready to use 0.01 m HEPES, pH 7.4, 0.15 m NaCl, 3 m m EDTA, 0.005% v/v surfactant P20); protein marker standards for GPC (GE Healthcare); Matchmaker Gold Systems (Clontech); and trypsin (Promega Corp., Madison, WI).

    Techniques: Binding Assay, Software