Isolation of anti-SARS-CoV-2 neutralizing monoclonal antibodies cross effective to variants aiming at antibody therapy
We isolated five mAbs with potent neutralizing activities against SARS-CoV-2 from two convalescent COVID-19 patients infected with prototype virus. Among them, the 9-105 antibody that have a highest affinity for the receptor-binding domain (RBD), cross-neutralize variants, such as B.1.1.7 (alfa), mink cluster 5 variant, B.1.351 (beta), P.1 (gamma), C.37 (lambda), B.1.617.1 (kappa), B.1.617.2 (delta) and B.1.621 (mu). A single amino acid mutation at K417 of RBD decreased neutralization sensitivity of 9-105. A 9-105 homology model revealed that 9-105 light chain binds to RBD including K417 by the same angle as ACE2.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:71 |
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| Enthalten in: |
Uirusu - 71(2021), 2 vom: 28., Seite 163-168 |
| Sprache: |
Japanisch |
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| Links: |
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| Anmerkungen: |
Date Revised 28.05.2023 published: Print Citation Status PubMed-not-MEDLINE |
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| doi: |
10.2222/jsv.71.163 |
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| 520 | |a We isolated five mAbs with potent neutralizing activities against SARS-CoV-2 from two convalescent COVID-19 patients infected with prototype virus. Among them, the 9-105 antibody that have a highest affinity for the receptor-binding domain (RBD), cross-neutralize variants, such as B.1.1.7 (alfa), mink cluster 5 variant, B.1.351 (beta), P.1 (gamma), C.37 (lambda), B.1.617.1 (kappa), B.1.617.2 (delta) and B.1.621 (mu). A single amino acid mutation at K417 of RBD decreased neutralization sensitivity of 9-105. A 9-105 homology model revealed that 9-105 light chain binds to RBD including K417 by the same angle as ACE2 | ||
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