<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Opuni KFM</submitter><funding>Deutscher Akademischer Austauschdienst</funding><funding>European Union</funding><pagination>14987-14997</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7606685</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>295(44)</volume><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-&lt;i>pf&lt;/i>MSP1&lt;sub>19&lt;/sub>, in &lt;i>Escherichia coli&lt;/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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>ITEM-THREE analysis of a monoclonal anti-malaria antibody reveals its assembled epitope on the &lt;i>pf&lt;/i>MSP1&lt;sub>19&lt;/sub> antigen.</pubmed_title><pmcid>PMC7606685</pmcid><funding_grant_id>EFRE-UHROM 9</funding_grant_id><funding_grant_id>91566064</funding_grant_id><funding_grant_id>91548123</funding_grant_id><pubmed_authors>Thiesen HJ</pubmed_authors><pubmed_authors>Alef A</pubmed_authors><pubmed_authors>Glocker MO</pubmed_authors><pubmed_authors>Russ M</pubmed_authors><pubmed_authors>Opuni KFM</pubmed_authors><pubmed_authors>Weresow M</pubmed_authors><pubmed_authors>Danquah BD</pubmed_authors><pubmed_authors>Reepmeyer M</pubmed_authors><pubmed_authors>Lorenz P</pubmed_authors><pubmed_authors>Koy C</pubmed_authors></additional><is_claimable>false</is_claimable><name>ITEM-THREE analysis of a monoclonal anti-malaria antibody reveals its assembled epitope on the &lt;i>pf&lt;/i>MSP1&lt;sub>19&lt;/sub> antigen.</name><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-&lt;i>pf&lt;/i>MSP1&lt;sub>19&lt;/sub>, in &lt;i>Escherichia coli&lt;/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</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Oct</publication><modification>2026-05-09T01:45:28.343Z</modification><creation>2022-02-11T12:23:51.071Z</creation></dates><accession>S-EPMC7606685</accession><cross_references><pubmed>32848020</pubmed><doi>10.1074/jbc.ra120.014802</doi><doi>10.1074/jbc.RA120.014802</doi></cross_references></HashMap>