{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T06:23:47Z","timestamp":1790663027358,"version":"4.1.0"},"reference-count":23,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2025,6,30]],"date-time":"2025-06-30T00:00:00Z","timestamp":1751241600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Cell. Infect. Microbiol."],"abstract":"<jats:p>Molecular mechanisms of red cell invasion by the <jats:italic>Plasmodium vivax<\/jats:italic> parasite remain obscure since information on receptor\u2013ligand interaction is scarce. Several proteins of the <jats:italic>P. vivax<\/jats:italic> Pvfam \u201ca\u201d family are known to bind with host erythrocytes. Some of them share their erythrocyte receptors with each other and <jats:italic>vice versa<\/jats:italic>, but the identification of these receptors is awaited with the exception of PvTRAg38. Here, we demonstrate by using solid-phase binding assay and surface plasmon resonance that majority (7 out of 10) of these erythrocyte binding proteins (PvTRAg, PvTRAg33.5, PvTRAg35.2, PvTRAg34, PvTRAg36, PvTRAg38, and PvTRAg69.4) interact with the erythrocyte receptor Basigin. These interactions seem to be important for the parasite\u2019s survival since each of these proteins interfered with the parasite\u2019s growth in a heterologous culture system. Furthermore, a higher parasite growth inhibition rate was observed with the combination of these proteins, suggesting the significance of multiple parasite ligand\u2019s interaction with the same erythrocyte receptor during the invasion process. These results will be helpful in understanding <jats:italic>P. vivax<\/jats:italic> biology and developing the therapeutics for vivax malaria.<\/jats:p>","DOI":"10.3389\/fcimb.2025.1592281","type":"journal-article","created":{"date-parts":[[2025,6,30]],"date-time":"2025-06-30T05:26:21Z","timestamp":1751261181000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":4,"title":["Majority of the erythrocyte binding proteins of the Pvfam \u201ca\u201d family of Plasmodium vivax interact with Basigin to assist parasite entry into the host cell"],"prefix":"10.3389","volume":"15","author":[{"given":"Manish","family":"Tripathi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meghna","family":"Santoshi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yagya D.","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sumit","family":"Rathore","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2025,6,30]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"3787","DOI":"10.1016\/j.vaccine.2008.05.059","article-title":"High immunogenecity and erythrocyte-binding activity in the tryptophan-rich domain (TRD) of the 74-kDa Plasmodium vivax alanine-tryptophan-rich antigen (PvATRAg74)","volume":"26","author":"Alam","year":"2008","journal-title":"Vaccine"},{"key":"B2","doi-asserted-by":"publisher","first-page":"20257","DOI":"10.1074\/jbc.M115.644906","article-title":"Interaction of plasmodium vivax tryptophan-rich antigen pvTRAg38 with band 3 on human erythrocyte surface facilitates parasite growth","volume":"290","author":"Alam","year":"2015","journal-title":"J. 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