{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T03:42:31Z","timestamp":1791085351341,"version":"4.1.0"},"reference-count":47,"publisher":"Portland Press Ltd.","issue":"8","license":[{"start":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T00:00:00Z","timestamp":1782864000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000925","name":"DHAC | National Health and Medical Research Council","doi-asserted-by":"publisher","award":["GNT2016908"],"award-info":[{"award-number":["GNT2016908"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"DHAC | National Health and Medical Research Council","doi-asserted-by":"publisher","award":["GNT2001385"],"award-info":[{"award-number":["GNT2001385"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"DHAC | National Health and Medical Research Council","doi-asserted-by":"publisher","award":["GNT2007996"],"award-info":[{"award-number":["GNT2007996"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,8,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Malaria is caused by Plasmodium parasites, and its clinical symptoms are a result of parasite invasion of red blood cells and the subsequent cycles of replication and proliferation. In human populations, Plasmodium vivax is responsible for the most widely distributed recurring malaria infections whereas Plasmodium falciparum inflicts the most mortality and morbidity. One well-characterized family of adhesins involved in red blood cell invasion is the reticulocyte-binding-like protein homolog family, known as the RBL superfamily that includes the PfRh family in P. falciparum and PvRBP family in P. vivax. Here we report a collection of nanobodies against three members of this adhesin family, PfRh5, PfRh4, and PvRBP2b. Nanobodies against these Plasmodium adhesins bind with high affinity across several epitopes and can block receptor engagement and inhibit parasite invasion of red blood cells. Using computational design, we generated stabilized PfRh4 variants that encompass the conserved scaffold present in the PfRh and PvRBP families of adhesins and show that several variants with improved expression retained binding to mouse monoclonal antibodies, nanobodies, and Complement Receptor 1, the human receptor for PfRh4. We also observed that most of the inhibitory nanobodies against the three antigens recognized the conserved structural scaffold that define this family of adhesins. These results demonstrate the potential of nanobodies to block malaria parasite invasion into red blood cells.<\/jats:p>","DOI":"10.1042\/bcj20260354","type":"journal-article","created":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T15:28:41Z","timestamp":1782919721000},"page":"1473-1488","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Nanobodies against\n                    <i>Plasmodium<\/i>\n                    adhesins that block receptor engagement and malaria parasite invasion"],"prefix":"10.1042","volume":"483","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4562-0241","authenticated-orcid":false,"given":"Jaison","family":"D\nSa","sequence":"first","affiliation":[{"name":"1The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia"},{"name":"2Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2724-0165","authenticated-orcid":false,"given":"Jill","family":"Chmielewski","sequence":"additional","affiliation":[{"name":"1The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia"},{"name":"2Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2952-7987","authenticated-orcid":false,"given":"Amy","family":"Adair","sequence":"additional","affiliation":[{"name":"1The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0606-4446","authenticated-orcid":false,"given":"Li\u00a0Lynn","family":"Tan","sequence":"additional","affiliation":[{"name":"1The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9439-3487","authenticated-orcid":false,"given":"Li-Jin","family":"Chan","sequence":"additional","affiliation":[{"name":"1The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia"},{"name":"2Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0241-6379","authenticated-orcid":false,"given":"Lucas","family":"Krauss","sequence":"additional","affiliation":[{"name":"3Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0608-229X","authenticated-orcid":false,"given":"Kathleen","family":"Zeglinski","sequence":"additional","affiliation":[{"name":"1The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia"},{"name":"2Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5142-7886","authenticated-orcid":false,"given":"Quentin","family":"Gouil","sequence":"additional","affiliation":[{"name":"1The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia"},{"name":"2Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia"},{"name":"4Olivia Newton-John Cancer Research Institute, Heidelberg, Victoria, Australia"},{"name":"5School of Cancer Medicine, La Trobe University, Bundoora, Victoria, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John\u00a0Z.","family":"Chen","sequence":"additional","affiliation":[{"name":"6Research School of Chemistry, The Australian National University, Canberra, Australian Capital Territory, Australia"},{"name":"7ARC Centre of Excellence in Synthetic Biology, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Colin\u00a0J.","family":"Jackson","sequence":"additional","affiliation":[{"name":"6Research School of Chemistry, The Australian National University, Canberra, Australian Capital Territory, Australia"},{"name":"7ARC Centre of Excellence in Synthetic Biology, Australia"},{"name":"8ARC Centre for Innovations in Peptide and Protein Science, Australia"},{"name":"9Research School of Biology, The Australian National University, Canberra, Australian Capital Territory, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christoph\u00a0Q.","family":"Schmidt","sequence":"additional","affiliation":[{"name":"10Institute of Experimental and Clinical Pharmacology, Toxicology and Pharmacology of Natural Products, University of Ulm Medical Center, Ulm, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3177-7560","authenticated-orcid":false,"given":"Sarel\u00a0J.","family":"Fleishman","sequence":"additional","affiliation":[{"name":"3Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2722-4621","authenticated-orcid":false,"given":"Phillip","family":"Pymm","sequence":"additional","affiliation":[{"name":"1The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia"},{"name":"2Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7950-8699","authenticated-orcid":false,"given":"Wai-Hong","family":"Tham","sequence":"additional","affiliation":[{"name":"1The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia"},{"name":"2Department of Medical Biology, The University of Melbourne, Parkville, Victoria, Australia"},{"name":"9Research School of Biology, The Australian National University, Canberra, Australian Capital Territory, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2026,7,9]]},"reference":[{"key":"2026071506163846000_B1","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1016\/j.ijpara.2008.09.007","article-title":"Morphology and kinetics of the three distinct phases of red blood cell invasion by Plasmodium falciparum merozoites","volume":"39","author":"Gilson","year":"2009","journal-title":"Int. J. Parasitol."},{"key":"2026071506163846000_B2","doi-asserted-by":"publisher","first-page":"748","DOI":"10.1126\/science.803712","article-title":"Invasion of erythrocytes by malaria merozoites","volume":"187","author":"Dvorak","year":"1975","journal-title":"Science"},{"key":"2026071506163846000_B3","doi-asserted-by":"publisher","first-page":"172","DOI":"10.1084\/jem.149.1.172","article-title":"Interaction between cytochalasin B-treated malarial parasites and erythrocytes. Attachment and junction formation","volume":"149","author":"Miller","year":"1979","journal-title":"J. Exp. Med."},{"key":"2026071506163846000_B4","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/j.chom.2010.12.003","article-title":"Super-resolution dissection of coordinated events during malaria parasite invasion of the human erythrocyte","volume":"9","author":"Riglar","year":"2011","journal-title":"Cell Host Microbe."},{"key":"2026071506163846000_B5","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1083\/jcb.77.1.72","article-title":"Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite","volume":"77","author":"Aikawa","year":"1978","journal-title":"J. Cell Biol."},{"key":"2026071506163846000_B6","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1038\/415673a","article-title":"The pathogenic basis of malaria","volume":"415","author":"Miller","year":"2002","journal-title":"Nature"},{"key":"2026071506163846000_B7","doi-asserted-by":"publisher","first-page":"232","DOI":"10.1016\/j.chom.2017.07.003","article-title":"The molecular basis of erythrocyte invasion by malaria parasites","volume":"22","author":"Cowman","year":"2017","journal-title":"Cell Host Microbe."},{"key":"2026071506163846000_B8","doi-asserted-by":"publisher","first-page":"e13110","DOI":"10.1111\/cmi.13110","article-title":"Plasmodium vivax reticulocyte binding proteins for invasion into reticulocytes","volume":"22","author":"Chan","year":"2020","journal-title":"Cell. Microbiol."},{"key":"2026071506163846000_B9","doi-asserted-by":"publisher","first-page":"e2569","DOI":"10.1371\/journal.pntd.0002569","article-title":"De novo assembly of a field isolate genome reveals novel Plasmodium vivax erythrocyte invasion genes","volume":"7","author":"Hester","year":"2013","journal-title":"PLoS Negl. Trop. Dis."},{"key":"2026071506163846000_B10","doi-asserted-by":"publisher","first-page":"757","DOI":"10.1038\/nature07327","article-title":"Comparative genomics of the neglected human malaria parasite Plasmodium vivax","volume":"455","author":"Carlton","year":"2008","journal-title":"Nature"},{"key":"2026071506163846000_B11","doi-asserted-by":"publisher","first-page":"677","DOI":"10.1128\/IAI.01117-15","article-title":"Gene models, expression repertoire, and immune response of Plasmodium vivax reticulocyte binding proteins","volume":"84","author":"Hietanen","year":"2015","journal-title":"Infect. Immun."},{"key":"2026071506163846000_B12","doi-asserted-by":"publisher","first-page":"534","DOI":"10.1038\/nature10606","article-title":"Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum","volume":"480","author":"Crosnier","year":"2011","journal-title":"Nature"},{"key":"2026071506163846000_B13","doi-asserted-by":"publisher","first-page":"17327","DOI":"10.1073\/pnas.1008151107","article-title":"Complement receptor 1 is the host erythrocyte receptor for Plasmodium falciparum PfRh4 invasion ligand","volume":"107","author":"Tham","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026071506163846000_B14","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1126\/science.aan1078","article-title":"Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax","volume":"359","author":"Gruszczyk","year":"2018","journal-title":"Science"},{"key":"2026071506163846000_B15","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1038\/s41586-018-0249-1","article-title":"Cryo-EM structure of an essential Plasmodium vivax invasion complex","volume":"559","author":"Gruszczyk","year":"2018","journal-title":"Nature"},{"key":"2026071506163846000_B16","doi-asserted-by":"publisher","first-page":"991","DOI":"10.1038\/s41564-021-00939-3","article-title":"Plasmodium vivax binds host CD98hc (SLC3A2) to enter immature red blood cells","volume":"6","author":"Malleret","year":"2021","journal-title":"Nat. Microbiol."},{"key":"2026071506163846000_B17","doi-asserted-by":"publisher","first-page":"427","DOI":"10.1038\/nature13715","article-title":"Structure of malaria invasion protein RH5 with erythrocyte basigin and blocking antibodies","volume":"515","author":"Wright","year":"2014","journal-title":"Nature"},{"key":"2026071506163846000_B18","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.04187","article-title":"Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes","volume":"3","author":"Chen","year":"2014","journal-title":"Elife"},{"key":"2026071506163846000_B19","doi-asserted-by":"publisher","first-page":"E191","DOI":"10.1073\/pnas.1516512113","article-title":"Structurally conserved erythrocyte-binding domain in Plasmodium provides a versatile scaffold for alternate receptor engagement","volume":"113","author":"Gruszczyk","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026071506163846000_B20","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1016\/j.ijpara.2008.10.006","article-title":"Reticulocyte-binding protein homologue 5\u2014an essential adhesin involved in invasion of human erythrocytes by Plasmodium falciparum","volume":"39","author":"Baum","year":"2009","journal-title":"Int. J. Parasitol."},{"key":"2026071506163846000_B21","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.chom.2008.06.001","article-title":"Erythrocyte binding protein PfRH5 polymorphisms determine species-specific pathways of Plasmodium falciparum invasion","volume":"4","author":"Hayton","year":"2008","journal-title":"Cell Host Microbe."},{"key":"2026071506163846000_B22","doi-asserted-by":"publisher","first-page":"4964.e21","DOI":"10.1016\/j.cell.2024.06.015","article-title":"Analysis of the diverse antigenic landscape of the malaria protein RH5 identifies a potent vaccine-induced human public antibody clonotype","volume":"187","author":"Barrett","year":"2024","journal-title":"Cell"},{"key":"2026071506163846000_B23","doi-asserted-by":"publisher","first-page":"4981.e14","DOI":"10.1016\/j.cell.2024.06.037","article-title":"Natural malaria infection elicits rare but potent neutralizing antibodies to the blood-stage antigen RH5","volume":"187","author":"Wang","year":"2024","journal-title":"Cell"},{"key":"2026071506163846000_B24","doi-asserted-by":"publisher","first-page":"e1000968","DOI":"10.1371\/journal.ppat.1000968","article-title":"Complement receptor 1 is a sialic acid-independent erythrocyte receptor of Plasmodium falciparum","volume":"6","author":"Spadafora","year":"2010","journal-title":"PLoS Pathog."},{"key":"2026071506163846000_B25","doi-asserted-by":"publisher","first-page":"1384","DOI":"10.1126\/science.1115257","article-title":"Molecular mechanism for switching of P. falciparum invasion pathways into human erythrocytes","volume":"309","author":"Stubbs","year":"2005","journal-title":"Science"},{"key":"2026071506163846000_B26","doi-asserted-by":"publisher","first-page":"25307","DOI":"10.1074\/jbc.M115.657171","article-title":"Characterization of inhibitors and monoclonal antibodies that modulate the interaction between Plasmodium falciparum adhesin PfRh4 with its erythrocyte receptor complement receptor 1","volume":"290","author":"Lim","year":"2015","journal-title":"J. Biol. Chem."},{"key":"2026071506163846000_B27","doi-asserted-by":"publisher","first-page":"1538","DOI":"10.1038\/s41467-021-21811-2","article-title":"Naturally acquired blocking human monoclonal antibodies to Plasmodium vivax reticulocyte binding protein 2b","volume":"12","author":"Chan","year":"2021","journal-title":"Nat. Commun."},{"key":"2026071506163846000_B28","doi-asserted-by":"publisher","first-page":"2623326","DOI":"10.1080\/19420862.2026.2623326","article-title":"Alpseq: an open-source workflow to turbocharge nanobody discovery with high-throughput sequencing","volume":"18","author":"Zeglinski","year":"2026","journal-title":"MAbs"},{"key":"2026071506163846000_B29","doi-asserted-by":"publisher","first-page":"e2101918118","DOI":"10.1073\/pnas.2101918118","article-title":"Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice","volume":"118","author":"Pymm","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026071506163846000_B30","doi-asserted-by":"publisher","first-page":"2427","DOI":"10.1128\/IAI.00048-09","article-title":"Antibodies to reticulocyte binding protein-like homologue 4 inhibit invasion of Plasmodium falciparum into human erythrocytes","volume":"77","author":"Tham","year":"2009","journal-title":"Infect. Immun."},{"key":"2026071506163846000_B31","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1186\/1475-2875-9-152","article-title":"Development of fluorescent Plasmodium falciparum for in vitro growth inhibition assays","volume":"9","author":"Wilson","year":"2010","journal-title":"Malar. J."},{"key":"2026071506163846000_B32","doi-asserted-by":"crossref","first-page":"108290","DOI":"10.1016\/j.jbc.2025.108290","article-title":"Stabilized designs of the malaria adhesin protein PvRBP2b for use as a potential diagnostic for Plasmodium vivax","volume":"301","author":"Sa","year":"2025","journal-title":"J. Biol. Chem."},{"key":"2026071506163846000_B33","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1016\/j.molcel.2016.06.012","article-title":"Automated structure- and sequence-based design of proteins for high bacterial expression and stability","volume":"63","author":"Goldenzweig","year":"2016","journal-title":"Mol. Cell"},{"key":"2026071506163846000_B34","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1126\/science.add2187","article-title":"Robust deep learning-based protein sequence design using ProteinMPNN","volume":"378","author":"Dauparas","year":"2022","journal-title":"Science"},{"key":"2026071506163846000_B35","doi-asserted-by":"publisher","first-page":"661","DOI":"10.1186\/s12951-024-02900-y","article-title":"Discovery of nanobodies: a comprehensive review of their applications and potential over the past five years","volume":"22","author":"Alexander","year":"2024","journal-title":"J. Nanobiotechnol."},{"key":"2026071506163846000_B36","doi-asserted-by":"publisher","first-page":"105259","DOI":"10.1016\/j.isci.2022.105259","article-title":"Biparatopic nanobodies targeting the receptor binding domain efficiently neutralize SARS-CoV-2","volume":"25","author":"Pymm","year":"2022","journal-title":"iScience"},{"key":"2026071506163846000_B37","doi-asserted-by":"publisher","first-page":"674","DOI":"10.1038\/nprot.2014.039","article-title":"A general protocol for the generation of nanobodies for structural biology","volume":"9","author":"Pardon","year":"2014","journal-title":"Nat. Protoc."},{"key":"2026071506163846000_B38","doi-asserted-by":"publisher","first-page":"579","DOI":"10.1042\/BCJ20200415","article-title":"Nanobody generation and structural characterization of Plasmodium falciparum 6-cysteine protein Pf12p","volume":"478","author":"Dietrich","year":"2021","journal-title":"Biochem. J."},{"key":"2026071506163846000_B39","doi-asserted-by":"publisher","first-page":"xtac005","DOI":"10.1093\/femsmc\/xtac005","article-title":"Structure of the Pf12 and Pf41 heterodimeric complex of Plasmodium falciparum 6-cysteine proteins","volume":"3","author":"Dietrich","year":"2022","journal-title":"FEMS Microbes."},{"key":"2026071506163846000_B40","doi-asserted-by":"publisher","first-page":"2529","DOI":"10.1042\/BCJ20220554","article-title":"Nanobodies against Pfs230 block Plasmodium falciparum transmission","volume":"479","author":"Dietrich","year":"2022","journal-title":"Biochem. J."},{"key":"2026071506163846000_B41","doi-asserted-by":"publisher","first-page":"eady0241","DOI":"10.1126\/science.ady0241","article-title":"Cryo-EM structure of endogenous Plasmodium falciparum Pfs230 and Pfs48\/45 fertilization complex","volume":"389","author":"Dietrich","year":"2025","journal-title":"Science"},{"key":"2026071506163846000_B42","first-page":"406","article-title":"The neighbor-joining method: a new method for reconstructing phylogenetic trees","volume":"4","author":"Saitou","year":"1987","journal-title":"Mol. Biol. Evol."},{"key":"2026071506163846000_B43","doi-asserted-by":"publisher","first-page":"592","DOI":"10.1093\/bioinformatics\/btq706","article-title":"phangorn: phylogenetic analysis in R","volume":"27","author":"Schliep","year":"2011","journal-title":"Bioinformatics"},{"key":"2026071506163846000_B44","doi-asserted-by":"publisher","first-page":"3041","DOI":"10.1093\/molbev\/msy194","article-title":"Two methods for mapping and visualizing associated data on phylogeny using Ggtree","volume":"35","author":"Yu","year":"2018","journal-title":"Mol. Biol. Evol."},{"key":"2026071506163846000_B45","article-title":"R: a language and environment for statistical computing","author":"R Core Team","year":"2020"},{"key":"2026071506163846000_B46","doi-asserted-by":"publisher","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2026071506163846000_B47","doi-asserted-by":"publisher","first-page":"e80635","DOI":"10.1371\/journal.pone.0080635","article-title":"Maximum allowed solvent accessibilites of residues in proteins","volume":"8","author":"Tien","year":"2013","journal-title":"PloS ONE"}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/483\/8\/1473\/989940\/bcj-2026-0354.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/483\/8\/1473\/989940\/bcj-2026-0354.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T10:16:45Z","timestamp":1784110605000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/483\/8\/1473\/237794\/Nanobodies-against-Plasmodium-adhesins-that-block"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,9]]},"references-count":47,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2026,8,5]]}},"URL":"https:\/\/doi.org\/10.1042\/bcj20260354","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2026,8]]},"published":{"date-parts":[[2026,7,9]]}}}