Plasmodium falciparum: Pfalhesin and CD36 Form an Adhesin/Receptor Pair That Is Responsible for the pH-Dependent Portion of Cytoadherence/Sequestration
The cytoadherent behavior of two Plasmodium falciparum (human malaria) cell lines, FCR-3 and IT04 (a cell line with elevated ICAM-1 adherence), was studied using CHO cells transfected with CD36 or ICAM-1 receptors as target cells. ICAM-1-mediated adherence was found to be relatively pH insensitive,...
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| Veröffentlicht in: | Experimental parasitology 1994-03, Vol.78 (2), p.203-209 |
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| creator | Crandall, I. Land, K.M. Sherman, I.W. |
| description | The cytoadherent behavior of two Plasmodium falciparum (human malaria) cell lines, FCR-3 and IT04 (a cell line with elevated ICAM-1 adherence), was studied using CHO cells transfected with CD36 or ICAM-1 receptors as target cells. ICAM-1-mediated adherence was found to be relatively pH insensitive, whereas CD36-mediated adherence was pH sensitive and inhibited by monoclonal antibodies and peptides based on a region found in human band 3 protein and named pfalhesin. Immobilized pfalhesin was used as an affinity matrix to purify CD36 from extracts of C32 amelanotic melanoma cells, which have ICAM-1 as well as CD36 receptors, and bind both parasite cell lines. We conclude that pfalhesin and CD36-constitute an adhesin/receptor pair. |
| doi_str_mv | 10.1006/expr.1994.1020 |
| format | Article |
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ICAM-1-mediated adherence was found to be relatively pH insensitive, whereas CD36-mediated adherence was pH sensitive and inhibited by monoclonal antibodies and peptides based on a region found in human band 3 protein and named pfalhesin. Immobilized pfalhesin was used as an affinity matrix to purify CD36 from extracts of C32 amelanotic melanoma cells, which have ICAM-1 as well as CD36 receptors, and bind both parasite cell lines. 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ICAM-1-mediated adherence was found to be relatively pH insensitive, whereas CD36-mediated adherence was pH sensitive and inhibited by monoclonal antibodies and peptides based on a region found in human band 3 protein and named pfalhesin. Immobilized pfalhesin was used as an affinity matrix to purify CD36 from extracts of C32 amelanotic melanoma cells, which have ICAM-1 as well as CD36 receptors, and bind both parasite cell lines. We conclude that pfalhesin and CD36-constitute an adhesin/receptor pair.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anion Exchange Protein 1, Erythrocyte - physiology</subject><subject>Antigens, CD - physiology</subject><subject>Biological and medical sciences</subject><subject>CD36 Antigens</subject><subject>Cell Adhesion</subject><subject>Cell Adhesion Molecules - physiology</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Erythrocytes - parasitology</subject><subject>Experimental protozoal diseases and models</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Immunoblotting</subject><subject>Infectious diseases</subject><subject>Intercellular Adhesion Molecule-1</subject><subject>Medical sciences</subject><subject>Melanoma, Amelanotic</subject><subject>Molecular Sequence Data</subject><subject>Parasitic diseases</subject><subject>Plasmodium falciparum</subject><subject>Plasmodium falciparum - physiology</subject><subject>Protozoal diseases</subject><subject>Tumor Cells, Cultured</subject><issn>0014-4894</issn><issn>1090-2449</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFr3DAQhUVoSbdprrkVdCi9eVeyZVnqLWyaJhDokqZnIUsjVsG2XMkOzS_p362cXXIrPYnH-2Y0vIfQBSVrSgjfwO8xrqmULMuSnKAVJZIUJWPyDVoRQlnBhGTv0PuUHgkhgpbsFJ02NZFNzVfoz67TqQ_Wzz12ujN-1HHuv-BdFntIfsB6sHh7VXF8HWKfFb60L8bmHgyMU4h4p33ED3s94duE7yGNYUi-7QC7bE57wONNcQUjDBaGCe9CnHwYcHB4-zwFnbdFGAxsfsCvGdIU9WJ_QG_zBQnOj-8Z-nn99WF7U9x9_3a7vbwrTCXlVOiyEdRJITWrREsaQ7hmpRYMuHSGurYsK8aFoW1twdXWtrZtpCmZo9LWzFZn6PNh7xjDy_eq98lA1-kBwpxUwytRiob9F6ScM8rEAq4PoIkhpQhOjdH3Oj4rStRSmVoqU0tlaqksD3w8bp7bHuwrfuwo-5-Ovk5Gdy7qwfj0iuUcOGmqjIkDBjmuJw9RJeOXYK2PYCZlg__XBX8BXbm0GQ</recordid><startdate>19940301</startdate><enddate>19940301</enddate><creator>Crandall, I.</creator><creator>Land, K.M.</creator><creator>Sherman, I.W.</creator><general>Elsevier Inc</general><general>Elsevier</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>M7N</scope><scope>7X8</scope></search><sort><creationdate>19940301</creationdate><title>Plasmodium falciparum: Pfalhesin and CD36 Form an Adhesin/Receptor Pair That Is Responsible for the pH-Dependent Portion of Cytoadherence/Sequestration</title><author>Crandall, I. ; Land, K.M. ; Sherman, I.W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-a2781f989a438b07c06a42a84e69fc1fb223468c1b5def5ddbdb79c24f19d54d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Anion Exchange Protein 1, Erythrocyte - physiology</topic><topic>Antigens, CD - physiology</topic><topic>Biological and medical sciences</topic><topic>CD36 Antigens</topic><topic>Cell Adhesion</topic><topic>Cell Adhesion Molecules - physiology</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Erythrocytes - parasitology</topic><topic>Experimental protozoal diseases and models</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Immunoblotting</topic><topic>Infectious diseases</topic><topic>Intercellular Adhesion Molecule-1</topic><topic>Medical sciences</topic><topic>Melanoma, Amelanotic</topic><topic>Molecular Sequence Data</topic><topic>Parasitic diseases</topic><topic>Plasmodium falciparum</topic><topic>Plasmodium falciparum - physiology</topic><topic>Protozoal diseases</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Crandall, I.</creatorcontrib><creatorcontrib>Land, K.M.</creatorcontrib><creatorcontrib>Sherman, I.W.</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Experimental parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Crandall, I.</au><au>Land, K.M.</au><au>Sherman, I.W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Plasmodium falciparum: Pfalhesin and CD36 Form an Adhesin/Receptor Pair That Is Responsible for the pH-Dependent Portion of Cytoadherence/Sequestration</atitle><jtitle>Experimental parasitology</jtitle><addtitle>Exp Parasitol</addtitle><date>1994-03-01</date><risdate>1994</risdate><volume>78</volume><issue>2</issue><spage>203</spage><epage>209</epage><pages>203-209</pages><issn>0014-4894</issn><eissn>1090-2449</eissn><coden>EXPAAA</coden><abstract>The cytoadherent behavior of two Plasmodium falciparum (human malaria) cell lines, FCR-3 and IT04 (a cell line with elevated ICAM-1 adherence), was studied using CHO cells transfected with CD36 or ICAM-1 receptors as target cells. ICAM-1-mediated adherence was found to be relatively pH insensitive, whereas CD36-mediated adherence was pH sensitive and inhibited by monoclonal antibodies and peptides based on a region found in human band 3 protein and named pfalhesin. Immobilized pfalhesin was used as an affinity matrix to purify CD36 from extracts of C32 amelanotic melanoma cells, which have ICAM-1 as well as CD36 receptors, and bind both parasite cell lines. We conclude that pfalhesin and CD36-constitute an adhesin/receptor pair.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>7509756</pmid><doi>10.1006/expr.1994.1020</doi><tpages>7</tpages></addata></record> |
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| ispartof | Experimental parasitology, 1994-03, Vol.78 (2), p.203-209 |
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| subjects | Amino Acid Sequence Animals Anion Exchange Protein 1, Erythrocyte - physiology Antigens, CD - physiology Biological and medical sciences CD36 Antigens Cell Adhesion Cell Adhesion Molecules - physiology CHO Cells Cricetinae Erythrocytes - parasitology Experimental protozoal diseases and models Humans Hydrogen-Ion Concentration Immunoblotting Infectious diseases Intercellular Adhesion Molecule-1 Medical sciences Melanoma, Amelanotic Molecular Sequence Data Parasitic diseases Plasmodium falciparum Plasmodium falciparum - physiology Protozoal diseases Tumor Cells, Cultured |
| title | Plasmodium falciparum: Pfalhesin and CD36 Form an Adhesin/Receptor Pair That Is Responsible for the pH-Dependent Portion of Cytoadherence/Sequestration |
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