Terminal galactose residues and the antigenicity of Plasmodium falciparum glycoproteins
The presence of terminal α- d-galactosyl residues in the carbohydrate chains of glycoprotein antigens from the asexual blood stages of Plasmodium falciparum is demonstrated by (1) the α- d-galactosidase sensitivity of particular parasite antigens, (2) the use of specific glycosidases to cleave sugar...
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| Veröffentlicht in: | Molecular and biochemical parasitology 1986-05, Vol.19 (2), p.91-101 |
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| container_title | Molecular and biochemical parasitology |
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| creator | Ramasamy, Ranjan Reese, Robert T. |
| description | The presence of terminal α-
d-galactosyl residues in the carbohydrate chains of glycoprotein antigens from the asexual blood stages of
Plasmodium falciparum is demonstrated by (1) the α-
d-galactosidase sensitivity of particular parasite antigens, (2) the use of specific glycosidases to cleave sugars from parasite glycoproteins radiolabeled with [
3H]glucosamine, and (3) the ability of
Bandeirea simplicifolia lectin, which has a specificity for terminal α-galactosyl residues, to bind to the parasite. The carbohydrate side chains, and in particular the terminal α-galactosyl residues, are shown to have an important role in determining the binding of antibodies to parasite glycoproteins. |
| doi_str_mv | 10.1016/0166-6851(86)90113-1 |
| format | Article |
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d-galactosyl residues in the carbohydrate chains of glycoprotein antigens from the asexual blood stages of
Plasmodium falciparum is demonstrated by (1) the α-
d-galactosidase sensitivity of particular parasite antigens, (2) the use of specific glycosidases to cleave sugars from parasite glycoproteins radiolabeled with [
3H]glucosamine, and (3) the ability of
Bandeirea simplicifolia lectin, which has a specificity for terminal α-galactosyl residues, to bind to the parasite. The carbohydrate side chains, and in particular the terminal α-galactosyl residues, are shown to have an important role in determining the binding of antibodies to parasite glycoproteins.</description><identifier>ISSN: 0166-6851</identifier><identifier>EISSN: 1872-9428</identifier><identifier>DOI: 10.1016/0166-6851(86)90113-1</identifier><identifier>PMID: 3014331</identifier><identifier>CODEN: MBIPDP</identifier><language>eng</language><publisher>Shannon: Elsevier B.V</publisher><subject>alpha-Galactosidase ; Animals ; Antibodies, Monoclonal ; Antigenicity ; Antigens, Protozoan - immunology ; Aotus trivirgatus ; Biochemistry. Physiology. Immunology. Molecular biology ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Galactose - immunology ; Glycoproteins ; Glycoproteins - immunology ; Glycosidases ; Glycoside Hydrolases ; Human protozoal diseases ; Immune Sera ; Immunochemistry ; Infectious diseases ; Lectins - immunology ; Malaria ; Medical sciences ; Oligosaccharides ; Parasitic diseases ; Plant Lectins ; Plasmodium falciparum ; Plasmodium falciparum - immunology ; Protozoa ; Protozoal diseases ; Tropical medicine ; α- d-Galactose</subject><ispartof>Molecular and biochemical parasitology, 1986-05, Vol.19 (2), p.91-101</ispartof><rights>1986</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-4e3f7dfbd8103403f7b5a6be5f29c9fdfe8f06a71a14e75a2cd1462ee24b3fa93</citedby><cites>FETCH-LOGICAL-c417t-4e3f7dfbd8103403f7b5a6be5f29c9fdfe8f06a71a14e75a2cd1462ee24b3fa93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0166-6851(86)90113-1$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3549,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8682291$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3014331$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ramasamy, Ranjan</creatorcontrib><creatorcontrib>Reese, Robert T.</creatorcontrib><title>Terminal galactose residues and the antigenicity of Plasmodium falciparum glycoproteins</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>The presence of terminal α-
d-galactosyl residues in the carbohydrate chains of glycoprotein antigens from the asexual blood stages of
Plasmodium falciparum is demonstrated by (1) the α-
d-galactosidase sensitivity of particular parasite antigens, (2) the use of specific glycosidases to cleave sugars from parasite glycoproteins radiolabeled with [
3H]glucosamine, and (3) the ability of
Bandeirea simplicifolia lectin, which has a specificity for terminal α-galactosyl residues, to bind to the parasite. The carbohydrate side chains, and in particular the terminal α-galactosyl residues, are shown to have an important role in determining the binding of antibodies to parasite glycoproteins.</description><subject>alpha-Galactosidase</subject><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Antigenicity</subject><subject>Antigens, Protozoan - immunology</subject><subject>Aotus trivirgatus</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactose - immunology</subject><subject>Glycoproteins</subject><subject>Glycoproteins - immunology</subject><subject>Glycosidases</subject><subject>Glycoside Hydrolases</subject><subject>Human protozoal diseases</subject><subject>Immune Sera</subject><subject>Immunochemistry</subject><subject>Infectious diseases</subject><subject>Lectins - immunology</subject><subject>Malaria</subject><subject>Medical sciences</subject><subject>Oligosaccharides</subject><subject>Parasitic diseases</subject><subject>Plant Lectins</subject><subject>Plasmodium falciparum</subject><subject>Plasmodium falciparum - immunology</subject><subject>Protozoa</subject><subject>Protozoal diseases</subject><subject>Tropical medicine</subject><subject>α- d-Galactose</subject><issn>0166-6851</issn><issn>1872-9428</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE2LFDEQhoMo67j6DxT6IKKH1lSSTtIXQRa_YEEPKx5DdVIZI_0xJj3C_HszzjBHPYRKeJ-qFA9jT4G_Bg76TT261baDl1a_6jmAbOEe24A1ou2VsPfZ5oI8ZI9K-ck574zWV-xKclBSwoZ9v6M8pRnHZosj-nUp1GQqKeypNDiHZv1Bta5pS3PyaT00S2y-jlimJaT91EQcfdphrtftePDLLi8rpbk8Zg9qVOjJuV6zbx_e3918am-_fPx88-629QrM2iqS0YQ4BAtcKl4fQ4d6oC6K3vcxRLKRazSAoMh0KHwApQWRUIOM2Mtr9uI0t378q-68uikVT-OIMy374ozuwdhO_xcE1QlptamgOoE-L6Vkim6X04T54IC7o3h3tOqOVp3V7q94B7Xt2Xn-fpgoXJrOpmv-_Jxj8TjGjLNP5YJZbYXoj9jbE0ZV2u9E2RWfaPYUUia_urCkf-_xB46eoHY</recordid><startdate>19860501</startdate><enddate>19860501</enddate><creator>Ramasamy, Ranjan</creator><creator>Reese, Robert T.</creator><general>Elsevier B.V</general><general>Elsevier Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>19860501</creationdate><title>Terminal galactose residues and the antigenicity of Plasmodium falciparum glycoproteins</title><author>Ramasamy, Ranjan ; Reese, Robert T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-4e3f7dfbd8103403f7b5a6be5f29c9fdfe8f06a71a14e75a2cd1462ee24b3fa93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>alpha-Galactosidase</topic><topic>Animals</topic><topic>Antibodies, Monoclonal</topic><topic>Antigenicity</topic><topic>Antigens, Protozoan - immunology</topic><topic>Aotus trivirgatus</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactose - immunology</topic><topic>Glycoproteins</topic><topic>Glycoproteins - immunology</topic><topic>Glycosidases</topic><topic>Glycoside Hydrolases</topic><topic>Human protozoal diseases</topic><topic>Immune Sera</topic><topic>Immunochemistry</topic><topic>Infectious diseases</topic><topic>Lectins - immunology</topic><topic>Malaria</topic><topic>Medical sciences</topic><topic>Oligosaccharides</topic><topic>Parasitic diseases</topic><topic>Plant Lectins</topic><topic>Plasmodium falciparum</topic><topic>Plasmodium falciparum - immunology</topic><topic>Protozoa</topic><topic>Protozoal diseases</topic><topic>Tropical medicine</topic><topic>α- d-Galactose</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ramasamy, Ranjan</creatorcontrib><creatorcontrib>Reese, Robert T.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and biochemical parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ramasamy, Ranjan</au><au>Reese, Robert T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Terminal galactose residues and the antigenicity of Plasmodium falciparum glycoproteins</atitle><jtitle>Molecular and biochemical parasitology</jtitle><addtitle>Mol Biochem Parasitol</addtitle><date>1986-05-01</date><risdate>1986</risdate><volume>19</volume><issue>2</issue><spage>91</spage><epage>101</epage><pages>91-101</pages><issn>0166-6851</issn><eissn>1872-9428</eissn><coden>MBIPDP</coden><abstract>The presence of terminal α-
d-galactosyl residues in the carbohydrate chains of glycoprotein antigens from the asexual blood stages of
Plasmodium falciparum is demonstrated by (1) the α-
d-galactosidase sensitivity of particular parasite antigens, (2) the use of specific glycosidases to cleave sugars from parasite glycoproteins radiolabeled with [
3H]glucosamine, and (3) the ability of
Bandeirea simplicifolia lectin, which has a specificity for terminal α-galactosyl residues, to bind to the parasite. The carbohydrate side chains, and in particular the terminal α-galactosyl residues, are shown to have an important role in determining the binding of antibodies to parasite glycoproteins.</abstract><cop>Shannon</cop><pub>Elsevier B.V</pub><pmid>3014331</pmid><doi>10.1016/0166-6851(86)90113-1</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Molecular and biochemical parasitology, 1986-05, Vol.19 (2), p.91-101 |
| issn | 0166-6851 1872-9428 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | alpha-Galactosidase Animals Antibodies, Monoclonal Antigenicity Antigens, Protozoan - immunology Aotus trivirgatus Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences Fundamental and applied biological sciences. Psychology Galactose - immunology Glycoproteins Glycoproteins - immunology Glycosidases Glycoside Hydrolases Human protozoal diseases Immune Sera Immunochemistry Infectious diseases Lectins - immunology Malaria Medical sciences Oligosaccharides Parasitic diseases Plant Lectins Plasmodium falciparum Plasmodium falciparum - immunology Protozoa Protozoal diseases Tropical medicine α- d-Galactose |
| title | Terminal galactose residues and the antigenicity of Plasmodium falciparum glycoproteins |
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