{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T08:03:46Z","timestamp":1789545826115,"version":"build-2803163510"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2003,8,15]]},"abstract":"<jats:p>Plasmodium vivax and P. knowlesi use the Duffy antigen as a receptor to invade human erythrocytes. Duffy-binding ligands belong to a family of erythrocyte-binding proteins that bind erythrocyte receptors to mediate invasion. Receptor-binding domains in erythrocyte-binding proteins lie in conserved cysteine-rich regions called Duffy-binding-like domains. In the present study, we report an analysis of the overall three-dimensional architecture of P. vivax and P. knowlesi Duffy-binding domains based on mild proteolysis and supportive-functional assays. Our proteolysis experiments indicate that these domains are built of two distinct subdomains. The N-terminal region from Cys-1\u20134 (C1\u2013C4) forms a stable non-functional subdomain. The region spanning C5\u2013C12 forms another subdomain, which is capable of binding Duffy antigen. These subdomains are joined by a protease-sensitive linker. Results from deletion constructs, designed for expression of truncated proteins on COS cell surface, show that regions containing C5\u2013C8 of the Duffy-binding domains are sufficient for the binding receptor. Therefore the central region of Duffy-binding domains, which is flanked by two non-functional regions, is responsible for receptor recognition. Moreover, the minimal Duffy-binding region identified here is capable of folding into a functionally competent module. These studies pave the way for understanding the architecture of Duffy-binding domains and their interactions with host receptors.<\/jats:p>","DOI":"10.1042\/bj20030622","type":"journal-article","created":{"date-parts":[[2003,8,18]],"date-time":"2003-08-18T10:49:53Z","timestamp":1061203793000},"page":"193-198","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":54,"title":["Definition of structural elements in Plasmodium vivax and P. knowlesi Duffy-binding domains necessary for erythrocyte invasion"],"prefix":"10.1042","volume":"374","author":[{"given":"Saurabh K.","family":"SINGH","sequence":"first","affiliation":[{"name":"Malaria Research Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Agam P.","family":"SINGH","sequence":"additional","affiliation":[{"name":"Malaria Research Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sunita","family":"PANDEY","sequence":"additional","affiliation":[{"name":"Malaria Research Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Syed S.","family":"YAZDANI","sequence":"additional","affiliation":[{"name":"Malaria Research Group, 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":"Malaria Research Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amit","family":"SHARMA","sequence":"additional","affiliation":[{"name":"Malaria Research Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/374\/1\/193\/711889\/bj3740193.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/374\/1\/193\/711889\/bj3740193.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T14:19:31Z","timestamp":1637590771000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/374\/1\/193\/43666\/Definition-of-structural-elements-in-Plasmodium"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,8,15]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2003,8,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20030622","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2003,8,15]]}}}