Complement receptor 1 is the human erythrocyte receptor for Plasmodium vivax erythrocyte binding protein
The discovery that Africans were resistant to infection by ( ) led to the conclusion that invasion relied on the Duffy Binding Protein (PvDBP) interacting with the Duffy Antigen Receptor for Chemokines (DARC) expressed on erythrocytes. However, the recent reporting of infections in DARC-negative Afr...
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creator | Lee, Seong-Kyun Crosnier, Cécile Valenzuela-Leon, Paola Carolina Dizon, Brian L P Atkinson, John P Mu, Jianbing Wright, Gavin J Calvo, Eric Gunalan, Karthigayan Miller, Louis H |
description | The discovery that Africans were resistant to infection by
(
) led to the conclusion that
invasion relied on the
Duffy Binding Protein (PvDBP) interacting with the Duffy Antigen Receptor for Chemokines (DARC) expressed on erythrocytes. However, the recent reporting of
infections in DARC-negative Africans suggests that the parasite might use an alternate invasion pathway to infect DARC-negative reticulocytes. To identify the parasite ligands and erythrocyte receptors that enable
invasion of both DARC-positive and -negative erythrocytes, we expressed region II containing the Duffy Binding-Like (DBL) domain of
erythrocyte binding protein (PvEBP-RII) and verified that the DBL domain binds to both DARC-positive and -negative erythrocytes. Furthermore, an AVidity-based EXtracelluar Interaction Screening (AVEXIS) was used to identify the receptor for PvEBP among over 750 human cell surface receptor proteins, and this approach identified only Complement Receptor 1 (CR1, CD35, or C3b/C4b receptor) as a PvEBP receptor. CR1 is a well-known receptor for
Reticulocyte binding protein Homology 4 (PfRh4) and is present on the surfaces of both reticulocytes and normocytes, but its expression decreases as erythrocytes age. Indeed, PvEBP-RII bound to a subpopulation of both reticulocytes and normocytes, and this binding was blocked by the addition of soluble CR1 recombinant protein, indicating that CR1 is the receptor of PvEBP. In addition, we found that the Long Homology Repeat A (LHR-A) subdomain of CR1 is the only subdomain responsible for mediating the interaction with PvEBP-RII. |
doi_str_mv | 10.1073/pnas.2316304121 |
format | Article |
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(
) led to the conclusion that
invasion relied on the
Duffy Binding Protein (PvDBP) interacting with the Duffy Antigen Receptor for Chemokines (DARC) expressed on erythrocytes. However, the recent reporting of
infections in DARC-negative Africans suggests that the parasite might use an alternate invasion pathway to infect DARC-negative reticulocytes. To identify the parasite ligands and erythrocyte receptors that enable
invasion of both DARC-positive and -negative erythrocytes, we expressed region II containing the Duffy Binding-Like (DBL) domain of
erythrocyte binding protein (PvEBP-RII) and verified that the DBL domain binds to both DARC-positive and -negative erythrocytes. Furthermore, an AVidity-based EXtracelluar Interaction Screening (AVEXIS) was used to identify the receptor for PvEBP among over 750 human cell surface receptor proteins, and this approach identified only Complement Receptor 1 (CR1, CD35, or C3b/C4b receptor) as a PvEBP receptor. CR1 is a well-known receptor for
Reticulocyte binding protein Homology 4 (PfRh4) and is present on the surfaces of both reticulocytes and normocytes, but its expression decreases as erythrocytes age. Indeed, PvEBP-RII bound to a subpopulation of both reticulocytes and normocytes, and this binding was blocked by the addition of soluble CR1 recombinant protein, indicating that CR1 is the receptor of PvEBP. In addition, we found that the Long Homology Repeat A (LHR-A) subdomain of CR1 is the only subdomain responsible for mediating the interaction with PvEBP-RII.</description><identifier>ISSN: 0027-8424</identifier><identifier>ISSN: 1091-6490</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.2316304121</identifier><identifier>PMID: 38261617</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Avidity ; Biological Sciences ; CD2 Antigens ; Cell Adhesion Molecules ; Cell surface ; Cell surface receptors ; Chemokines ; Complement receptor 1 ; Duffy antigen ; Erythrocytes ; Homology ; Humans ; Malaria, Falciparum ; Parasites ; Plasmodium vivax ; Proteins ; Receptors ; Receptors, Cell Surface ; Reticulocytes</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2024-01, Vol.121 (5), p.e2316304121</ispartof><rights>Copyright National Academy of Sciences Jan 30, 2024</rights><rights>Copyright © 2024 the Author(s). Published by PNAS. 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-cca5901c0356c47ea4bdbdefecb3a9b5573cbca92739684427a68b61ac8c54433</citedby><cites>FETCH-LOGICAL-c422t-cca5901c0356c47ea4bdbdefecb3a9b5573cbca92739684427a68b61ac8c54433</cites><orcidid>0000-0002-5740-5178 ; 0000-0001-7880-2730 ; 0000-0002-2514-3441</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10835065/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10835065/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38261617$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Seong-Kyun</creatorcontrib><creatorcontrib>Crosnier, Cécile</creatorcontrib><creatorcontrib>Valenzuela-Leon, Paola Carolina</creatorcontrib><creatorcontrib>Dizon, Brian L P</creatorcontrib><creatorcontrib>Atkinson, John P</creatorcontrib><creatorcontrib>Mu, Jianbing</creatorcontrib><creatorcontrib>Wright, Gavin J</creatorcontrib><creatorcontrib>Calvo, Eric</creatorcontrib><creatorcontrib>Gunalan, Karthigayan</creatorcontrib><creatorcontrib>Miller, Louis H</creatorcontrib><title>Complement receptor 1 is the human erythrocyte receptor for Plasmodium vivax erythrocyte binding protein</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The discovery that Africans were resistant to infection by
(
) led to the conclusion that
invasion relied on the
Duffy Binding Protein (PvDBP) interacting with the Duffy Antigen Receptor for Chemokines (DARC) expressed on erythrocytes. However, the recent reporting of
infections in DARC-negative Africans suggests that the parasite might use an alternate invasion pathway to infect DARC-negative reticulocytes. To identify the parasite ligands and erythrocyte receptors that enable
invasion of both DARC-positive and -negative erythrocytes, we expressed region II containing the Duffy Binding-Like (DBL) domain of
erythrocyte binding protein (PvEBP-RII) and verified that the DBL domain binds to both DARC-positive and -negative erythrocytes. Furthermore, an AVidity-based EXtracelluar Interaction Screening (AVEXIS) was used to identify the receptor for PvEBP among over 750 human cell surface receptor proteins, and this approach identified only Complement Receptor 1 (CR1, CD35, or C3b/C4b receptor) as a PvEBP receptor. CR1 is a well-known receptor for
Reticulocyte binding protein Homology 4 (PfRh4) and is present on the surfaces of both reticulocytes and normocytes, but its expression decreases as erythrocytes age. Indeed, PvEBP-RII bound to a subpopulation of both reticulocytes and normocytes, and this binding was blocked by the addition of soluble CR1 recombinant protein, indicating that CR1 is the receptor of PvEBP. In addition, we found that the Long Homology Repeat A (LHR-A) subdomain of CR1 is the only subdomain responsible for mediating the interaction with PvEBP-RII.</description><subject>Avidity</subject><subject>Biological Sciences</subject><subject>CD2 Antigens</subject><subject>Cell Adhesion Molecules</subject><subject>Cell surface</subject><subject>Cell surface receptors</subject><subject>Chemokines</subject><subject>Complement receptor 1</subject><subject>Duffy antigen</subject><subject>Erythrocytes</subject><subject>Homology</subject><subject>Humans</subject><subject>Malaria, Falciparum</subject><subject>Parasites</subject><subject>Plasmodium vivax</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Receptors, Cell Surface</subject><subject>Reticulocytes</subject><issn>0027-8424</issn><issn>1091-6490</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkU1v1DAQhi0EokvhzA1F4sIlrcdfsU8IrfiSKpVDe7YcZ7ZxldjBTlbsvyerlpb2YM3Bz7yaVw8h74GeAW34-RRdOWMcFKcCGLwgG6AGaiUMfUk2lLKm1oKJE_KmlFtKqZGaviYnXDMFCpoN6bdpnAYcMc5VRo_TnHIFVSjV3GPVL6OLFebD3OfkDzM-Mrv1_RpcGVMXlrHah73784RsQ-xCvKmmnGYM8S15tXNDwXf385Rcf_t6tf1RX1x-_7n9clF7wdhce--koeApl8qLBp1ou7bDHfqWO9NK2XDfemdYw43SQrDGKd0qcF57KQTnp-TzXe60tCN2fi2W3WCnHEaXDza5YJ_-xNDbm7S3QDWXVMk14dN9Qk6_FyyzHUPxOAwuYlqKZQY0GN1IsaIfn6G3aclx7bdSDMAoIY7U-R3lcyol4-7hGqD2qNEeNdpHjevGh_9LPPD_vPG_BbicAQ</recordid><startdate>20240130</startdate><enddate>20240130</enddate><creator>Lee, Seong-Kyun</creator><creator>Crosnier, Cécile</creator><creator>Valenzuela-Leon, Paola Carolina</creator><creator>Dizon, Brian L P</creator><creator>Atkinson, John P</creator><creator>Mu, Jianbing</creator><creator>Wright, Gavin J</creator><creator>Calvo, Eric</creator><creator>Gunalan, Karthigayan</creator><creator>Miller, Louis H</creator><general>National Academy of Sciences</general><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-5740-5178</orcidid><orcidid>https://orcid.org/0000-0001-7880-2730</orcidid><orcidid>https://orcid.org/0000-0002-2514-3441</orcidid></search><sort><creationdate>20240130</creationdate><title>Complement receptor 1 is the human erythrocyte receptor for Plasmodium vivax erythrocyte binding protein</title><author>Lee, Seong-Kyun ; Crosnier, Cécile ; Valenzuela-Leon, Paola Carolina ; Dizon, Brian L P ; Atkinson, John P ; Mu, Jianbing ; Wright, Gavin J ; Calvo, Eric ; Gunalan, Karthigayan ; Miller, Louis H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c422t-cca5901c0356c47ea4bdbdefecb3a9b5573cbca92739684427a68b61ac8c54433</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Avidity</topic><topic>Biological Sciences</topic><topic>CD2 Antigens</topic><topic>Cell Adhesion Molecules</topic><topic>Cell surface</topic><topic>Cell surface receptors</topic><topic>Chemokines</topic><topic>Complement receptor 1</topic><topic>Duffy antigen</topic><topic>Erythrocytes</topic><topic>Homology</topic><topic>Humans</topic><topic>Malaria, Falciparum</topic><topic>Parasites</topic><topic>Plasmodium vivax</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Receptors, Cell Surface</topic><topic>Reticulocytes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Seong-Kyun</creatorcontrib><creatorcontrib>Crosnier, Cécile</creatorcontrib><creatorcontrib>Valenzuela-Leon, Paola Carolina</creatorcontrib><creatorcontrib>Dizon, Brian L P</creatorcontrib><creatorcontrib>Atkinson, John P</creatorcontrib><creatorcontrib>Mu, Jianbing</creatorcontrib><creatorcontrib>Wright, Gavin J</creatorcontrib><creatorcontrib>Calvo, Eric</creatorcontrib><creatorcontrib>Gunalan, Karthigayan</creatorcontrib><creatorcontrib>Miller, Louis H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Seong-Kyun</au><au>Crosnier, Cécile</au><au>Valenzuela-Leon, Paola Carolina</au><au>Dizon, Brian L P</au><au>Atkinson, John P</au><au>Mu, Jianbing</au><au>Wright, Gavin J</au><au>Calvo, Eric</au><au>Gunalan, Karthigayan</au><au>Miller, Louis H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complement receptor 1 is the human erythrocyte receptor for Plasmodium vivax erythrocyte binding protein</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2024-01-30</date><risdate>2024</risdate><volume>121</volume><issue>5</issue><spage>e2316304121</spage><pages>e2316304121-</pages><issn>0027-8424</issn><issn>1091-6490</issn><eissn>1091-6490</eissn><abstract>The discovery that Africans were resistant to infection by
(
) led to the conclusion that
invasion relied on the
Duffy Binding Protein (PvDBP) interacting with the Duffy Antigen Receptor for Chemokines (DARC) expressed on erythrocytes. However, the recent reporting of
infections in DARC-negative Africans suggests that the parasite might use an alternate invasion pathway to infect DARC-negative reticulocytes. To identify the parasite ligands and erythrocyte receptors that enable
invasion of both DARC-positive and -negative erythrocytes, we expressed region II containing the Duffy Binding-Like (DBL) domain of
erythrocyte binding protein (PvEBP-RII) and verified that the DBL domain binds to both DARC-positive and -negative erythrocytes. Furthermore, an AVidity-based EXtracelluar Interaction Screening (AVEXIS) was used to identify the receptor for PvEBP among over 750 human cell surface receptor proteins, and this approach identified only Complement Receptor 1 (CR1, CD35, or C3b/C4b receptor) as a PvEBP receptor. CR1 is a well-known receptor for
Reticulocyte binding protein Homology 4 (PfRh4) and is present on the surfaces of both reticulocytes and normocytes, but its expression decreases as erythrocytes age. Indeed, PvEBP-RII bound to a subpopulation of both reticulocytes and normocytes, and this binding was blocked by the addition of soluble CR1 recombinant protein, indicating that CR1 is the receptor of PvEBP. In addition, we found that the Long Homology Repeat A (LHR-A) subdomain of CR1 is the only subdomain responsible for mediating the interaction with PvEBP-RII.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>38261617</pmid><doi>10.1073/pnas.2316304121</doi><orcidid>https://orcid.org/0000-0002-5740-5178</orcidid><orcidid>https://orcid.org/0000-0001-7880-2730</orcidid><orcidid>https://orcid.org/0000-0002-2514-3441</orcidid><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
subjects | Avidity Biological Sciences CD2 Antigens Cell Adhesion Molecules Cell surface Cell surface receptors Chemokines Complement receptor 1 Duffy antigen Erythrocytes Homology Humans Malaria, Falciparum Parasites Plasmodium vivax Proteins Receptors Receptors, Cell Surface Reticulocytes |
title | Complement receptor 1 is the human erythrocyte receptor for Plasmodium vivax erythrocyte binding protein |
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