{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Opuni KFM"],"funding":["Deutscher Akademischer Austauschdienst","European Union"],"pagination":["14987-14997"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7606685"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["295(44)"],"pubmed_abstract":["Rapid diagnostic tests are first-line assays for diagnosing infectious diseases, such as malaria. To minimize false positive and false negative test results in population-screening assays, high-quality reagents and well-characterized antigens and antibodies are needed. An important property of antigen-antibody binding is recognition specificity, which best can be estimated by mapping an antibody's epitope on the respective antigen. We have cloned a malarial antigen-containing fusion protein, MBP-<i>pf</i>MSP1<sub>19</sub>, in <i>Escherichia coli</i>, which then was structurally and functionally characterized before and after high pressure-assisted enzymatic digestion. We then used our previously developed method, intact transition epitope mapping-targeted high-energy rupture of extracted e"],"journal":["The Journal of biological chemistry"],"pubmed_title":["ITEM-THREE analysis of a monoclonal anti-malaria antibody reveals its assembled epitope on the <i>pf</i>MSP1<sub>19</sub> antigen."],"pmcid":["PMC7606685"],"funding_grant_id":["EFRE-UHROM 9","91566064","91548123"],"pubmed_authors":["Thiesen HJ","Alef A","Glocker MO","Russ M","Opuni KFM","Weresow M","Danquah BD","Reepmeyer M","Lorenz P","Koy C"],"additional_accession":[]},"is_claimable":false,"name":"ITEM-THREE analysis of a monoclonal anti-malaria antibody reveals its assembled epitope on the <i>pf</i>MSP1<sub>19</sub> antigen.","description":"Rapid diagnostic tests are first-line assays for diagnosing infectious diseases, such as malaria. To minimize false positive and false negative test results in population-screening assays, high-quality reagents and well-characterized antigens and antibodies are needed. An important property of antigen-antibody binding is recognition specificity, which best can be estimated by mapping an antibody's epitope on the respective antigen. We have cloned a malarial antigen-containing fusion protein, MBP-<i>pf</i>MSP1<sub>19</sub>, in <i>Escherichia coli</i>, which then was structurally and functionally characterized before and after high pressure-assisted enzymatic digestion. We then used our previously developed method, intact transition epitope mapping-targeted high-energy rupture of extracted e","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Oct","modification":"2026-05-09T01:45:28.343Z","creation":"2022-02-11T12:23:51.071Z"},"accession":"S-EPMC7606685","cross_references":{"pubmed":["32848020"],"doi":["10.1074/jbc.ra120.014802","10.1074/jbc.RA120.014802"]}}