<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Li L</submitter><funding>NIAID NIH HHS</funding><funding>NIH HHS</funding><pagination>63</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9113379</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>12(1)</volume><pubmed_abstract>&lt;h4>Background&lt;/h4>Neutralizing antibodies are approved drugs to treat coronavirus disease-2019 (COVID-19) patients, yet mutations in severe acute respiratory syndrome coronavirus (SARS-CoV-2) variants may reduce the antibody neutralizing activity. New monoclonal antibodies (mAbs) and antibody remolding strategies are recalled in the battle with COVID-19 epidemic.&lt;h4>Results&lt;/h4>We identified multiple mAbs from antibody phage display library made from COVID-19 patients and further characterized the R3P1-E4 clone, which effectively suppressed SARS-CoV-2 infection and rescued the lethal phenotype in mice infected with SARS-CoV-2. Crystal structural analysis not only explained why R3P1-E4 had selectively reduced binding and neutralizing activity to SARS-CoV-2 variants carrying K417 mutations,</pubmed_abstract><journal>Cell &amp; bioscience</journal><pubmed_title>Antibody engineering improves neutralization activity against K417 spike mutant SARS-CoV-2 variants.</pubmed_title><pmcid>PMC9113379</pmcid><funding_grant_id>AI158154</funding_grant_id><funding_grant_id>R01AI069120</funding_grant_id><funding_grant_id>AI140718</funding_grant_id><funding_grant_id>R01 AI140718</funding_grant_id><pubmed_authors>Deng YQ</pubmed_authors><pubmed_authors>Duan J</pubmed_authors><pubmed_authors>Yang H</pubmed_authors><pubmed_authors>Li J</pubmed_authors><pubmed_authors>Zu S</pubmed_authors><pubmed_authors>Guo Y</pubmed_authors><pubmed_authors>Jiao P</pubmed_authors><pubmed_authors>Rao Z</pubmed_authors><pubmed_authors>Aliyari SR</pubmed_authors><pubmed_authors>Li L</pubmed_authors><pubmed_authors>Shi Y</pubmed_authors><pubmed_authors>Gao M</pubmed_authors><pubmed_authors>Cao Y</pubmed_authors><pubmed_authors>Cheng G</pubmed_authors><pubmed_authors>Wan D</pubmed_authors><pubmed_authors>Qin CF</pubmed_authors></additional><is_claimable>false</is_claimable><name>Antibody engineering improves neutralization activity against K417 spike mutant SARS-CoV-2 variants.</name><description>&lt;h4>Background&lt;/h4>Neutralizing antibodies are approved drugs to treat coronavirus disease-2019 (COVID-19) patients, yet mutations in severe acute respiratory syndrome coronavirus (SARS-CoV-2) variants may reduce the antibody neutralizing activity. New monoclonal antibodies (mAbs) and antibody remolding strategies are recalled in the battle with COVID-19 epidemic.&lt;h4>Results&lt;/h4>We identified multiple mAbs from antibody phage display library made from COVID-19 patients and further characterized the R3P1-E4 clone, which effectively suppressed SARS-CoV-2 infection and rescued the lethal phenotype in mice infected with SARS-CoV-2. Crystal structural analysis not only explained why R3P1-E4 had selectively reduced binding and neutralizing activity to SARS-CoV-2 variants carrying K417 mutations,</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 May</publication><modification>2026-05-31T07:09:24.737Z</modification><creation>2025-02-19T05:05:31.65Z</creation></dates><accession>S-EPMC9113379</accession><cross_references><pubmed>35581593</pubmed><doi>10.1186/s13578-022-00794-7</doi></cross_references></HashMap>