{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T17:10:52Z","timestamp":1783617052971,"version":"3.55.0"},"reference-count":20,"publisher":"National Academy of Sciences","issue":"24","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1999,11,23]]},"abstract":"<jats:p>\n                    Invasion of erythrocytes by malaria parasites is mediated by specific molecular interactions. Whereas\n                    <jats:italic>Plasmodium vivax<\/jats:italic>\n                    and\n                    <jats:italic>Plasmodium knowlesi<\/jats:italic>\n                    use the Duffy blood group antigen,\n                    <jats:italic>Plasmodium falciparum<\/jats:italic>\n                    uses sialic acid residues of glycophorin A as receptors to invade human erythrocytes.\n                    <jats:italic>P. knowlesi<\/jats:italic>\n                    uses the Duffy antigen as well as other receptors to invade rhesus erythrocytes by multiple pathways. Parasite ligands that bind these receptors belong to a family of erythrocyte-binding proteins (EBP). The EBP family includes the\n                    <jats:italic>P. vivax<\/jats:italic>\n                    and\n                    <jats:italic>P. knowlesi<\/jats:italic>\n                    Duffy-binding proteins,\n                    <jats:italic>P. knowlesi<\/jats:italic>\n                    \u03b2 and \u03b3 proteins, which bind alternate receptors on rhesus erythrocytes, and\n                    <jats:italic>P. falciparum<\/jats:italic>\n                    erythrocyte-binding antigen (EBA-175), which binds sialic acid residues of human glycophorin A. Binding domains of each EBP lie in a conserved N-terminal cysteine-rich region, region II, which contains around 330 amino acids with 12 to 14 conserved cysteines. Regions containing binding residues have now been mapped within\n                    <jats:italic>P. vivax<\/jats:italic>\n                    and\n                    <jats:italic>P. knowlesi<\/jats:italic>\n                    \u03b2 region II. Chimeric domains containing\n                    <jats:italic>P. vivax<\/jats:italic>\n                    region II sequences fused to\n                    <jats:italic>P. knowlesi<\/jats:italic>\n                    \u03b2 region II sequences were expressed on the surface of COS cells and tested for binding to erythrocytes. Binding residues of\n                    <jats:italic>P. vivax<\/jats:italic>\n                    region II lie in a 170-aa stretch between cysteines 4 and 7, and binding residues of\n                    <jats:italic>P. knowlesi<\/jats:italic>\n                    \u03b2 region II lie in a 53-aa stretch between cysteines 4 and 5. Mapping regions responsible for receptor recognition is an important step toward understanding the structural basis for the interaction of these parasite ligands with host receptors.\n                  <\/jats:p>","DOI":"10.1073\/pnas.96.24.14067","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:41:48Z","timestamp":1027680108000},"page":"14067-14072","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":100,"title":["Mapping regions containing binding residues within functional domains of\n                    <i>Plasmodium vivax<\/i>\n                    and\n                    <i>Plasmodium knowlesi<\/i>\n                    erythrocyte-binding proteins"],"prefix":"10.1073","volume":"96","author":[{"given":"Akash","family":"Ranjan","sequence":"first","affiliation":[{"name":"International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chetan E.","family":"Chitnis","sequence":"additional","affiliation":[{"name":"International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1999,11,23]]},"reference":[{"key":"e_1_3_3_1_2","first-page":"249","volume-title":"Malaria: Molecular and Clinical Aspects","author":"Chitnis C E","year":"1999","unstructured":"C E Chitnis, P Sinnis, L H Miller Malaria: Molecular and Clinical Aspects, eds M Wahlgren, P Perlmann (Harwood, London), pp. 249\u2013285 (1999)."},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1145213"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM197608052950602"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.167.6.1873"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.146.1.277"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/297064a0"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.15.7085"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.180.2.497"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.111.5.1877"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.8009226"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(95)90054-3"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(95)90055-1"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(95)90056-X"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1038\/40888"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.187.1.15"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.62.6.1932-1940.1988"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.3901257"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.7689250"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.184.4.1531"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0166-6851(97)00113-8"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.96.24.14067","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T16:18:31Z","timestamp":1649866711000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.96.24.14067"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,11,23]]},"references-count":20,"journal-issue":{"issue":"24","published-print":{"date-parts":[[1999,11,23]]}},"alternative-id":["10.1073\/pnas.96.24.14067"],"URL":"https:\/\/doi.org\/10.1073\/pnas.96.24.14067","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1999,11,23]]},"assertion":[{"value":"1999-08-07","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"1999-09-30","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"1999-11-23","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}