@prefix : <http://semanticscholar.org/cv-research/> .
@prefix dc: <http://purl.org/dc/terms/> .
@prefix fhir_link: <http://hl7.org/fhir/link/> .
@prefix ncit: <http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#> .
@prefix rdf: <http://www.w3.org/1999/02/22-rdf-syntax-ns#> .
@prefix rdfs: <http://www.w3.org/2000/01/rdf-schema#> .
@prefix sso: <http://semanticscholar.org/cv-research/> .
@prefix whocv: <http://semanticscholar.org/cv-research/WHO#> .
@prefix xml: <http://www.w3.org/XML/1998/namespace> .
@prefix xsd: <http://www.w3.org/2001/XMLSchema#> .

<http://fhircat.org/cord-19/metadata/f779584a7b398e7e60721ce5cfe96fd2d0058a6b> dc:abstract "Since its first report in the Middle East in 2012, the Middle East respiratory syndrome-coronavirus (MERS-CoV) has become a global concern due to the high morbidity and mortality of individuals infected with the virus. Although the majority of MERS-CoV cases have been reported in Saudi Arabia, the overall risk in areas outside the Middle East remains significant as inside Saudi Arabia. Additional pandemics of MERS-CoV are expected, and thus novel tools and reagents for therapy and diagnosis are urgently needed. Here, we used phage display to develop novel monoclonal antibodies (mAbs) that target MERS-CoV. A human Fab phage display library was panned against the S2 subunit of the MERS-CoV spike protein (MERS-S2P), yielding three unique Fabs (S2A3, S2A6, and S2D5). The Fabs had moderate apparent affinities (Half maximal effective concentration (EC(50) = 123–421 nM) for MERS-S2P, showed no cross-reactivity to spike proteins from other CoVs, and were non-aggregating and thermostable (T(m) = 61.5–80.4 °C). Reformatting the Fabs into IgGs (Immunoglobulin Gs) greatly increased their apparent affinities (K(D) = 0.17–1.2 nM), presumably due to the effects of avidity. These apparent affinities were notably higher than that of a previously reported anti-MERS-CoV S2 reference mAb (K(D) = 8.7 nM). Furthermore, two of the three mAbs (S2A3 and S2D5) bound only MERS-CoV (Erasmus Medical Center (EMC)) and not other CoVs, reflecting their high binding specificity. However, the mAbs lacked MERS-CoV neutralizing activity. Given their high affinity, specificity, and desirable stabilities, we anticipate that these anti-MERS-CoV mAbs would be suitable reagents for developing antibody-based diagnostics in laboratory or hospital settings for point-of-care testing." ;
    dc:creator "['Kim, Yoonji', 'Lee, Hansaem', 'Park, Keunwan', 'Park, Sora', 'Lim, Ju-Hyeon', 'So, Min Kyung', 'Woo, Hye-Min', 'Ko, Hyemin', 'Lee, Jeong-Min', 'Lim, Sun Hee', 'Ko, Byoung Joon', 'Park, Yeon-Su', 'Choi, So-Young', 'Song, Du Hyun', 'Lee, Joo-Yeon', 'Kim, Sung Soon', 'Kim, Dae Young']" ;
    dc:identifier <http://dx.doi.org/10.3390/antib8030042>,
        <https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6783954>,
        <https://www.ncbi.nlm.nih.gov/pubmed/31544848> ;
    dc:issued "2019-01-01"^^xsd:date ;
    dc:license "CC BY" ;
    dc:title "Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning" ;
    sso:has_full_text "False" ;
    sso:journal "Antibodies (Basel)" ;
    sso:sha "f779584a7b398e7e60721ce5cfe96fd2d0058a6b" ;
    sso:source_x "PMC" .

