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Article

Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning

1
New Drug Development Center, Osong Medical Innovation Foundation, Cheongju-si, Chungcheongbuk-do 28160, Korea
2
Korea Center for Disease Control, Osong Health Technology Administration Complex, Cheongju-si, Chungcheongbuk-do 28159, Korea
3
Plexense, Inc., Yongin-si, Gyeonggi-do 441-813, Korea
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Current address: Korea Institute of Science and Technology, Gangneung-si, Gangwon-do 25451, Korea.
Antibodies 2019, 8(3), 42; https://doi.org/10.3390/antib8030042
Received: 3 June 2019 / Revised: 1 July 2019 / Accepted: 7 July 2019 / Published: 31 July 2019
(This article belongs to the Special Issue Antibody Phage Display)
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 (EC50 = 123–421 nM) for MERS-S2P, showed no cross-reactivity to spike proteins from other CoVs, and were non-aggregating and thermostable (Tm = 61.5–80.4 °C). Reformatting the Fabs into IgGs (Immunoglobulin Gs) greatly increased their apparent affinities (KD = 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 (KD = 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. View Full-Text
Keywords: MERS-CoV; spike protein; S2 subunit; phage display; monoclonal antibody MERS-CoV; spike protein; S2 subunit; phage display; monoclonal antibody
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MDPI and ACS Style

Kim, Y.; Lee, H.; Park, K.; Park, S.; Lim, J.-H.; So, M.K.; Woo, H.-M.; Ko, H.; Lee, J.-M.; Lim, S.H.; Ko, B.J.; Park, Y.-S.; Choi, S.-Y.; Song, D.H.; Lee, J.-Y.; Kim, S.S.; Kim, D.Y. Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning. Antibodies 2019, 8, 42. https://doi.org/10.3390/antib8030042

AMA Style

Kim Y, Lee H, Park K, Park S, Lim J-H, So MK, Woo H-M, Ko H, Lee J-M, Lim SH, Ko BJ, Park Y-S, Choi S-Y, Song DH, Lee J-Y, Kim SS, Kim DY. Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning. Antibodies. 2019; 8(3):42. https://doi.org/10.3390/antib8030042

Chicago/Turabian Style

Kim, Yoonji, Hansaem Lee, Keunwan Park, Sora Park, Ju-Hyeon Lim, Min K. So, Hye-Min Woo, Hyemin Ko, Jeong-Min Lee, Sun H. Lim, Byoung J. Ko, Yeon-Su Park, So-Young Choi, Du H. Song, Joo-Yeon Lee, Sung S. Kim, and Dae Y. Kim 2019. "Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning" Antibodies 8, no. 3: 42. https://doi.org/10.3390/antib8030042

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