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Neutralization or enhancement of SARS-CoV-2 infection by a monoclonal antibody targeting a specific epitope in the spike receptor-binding domain.
Lai, Guan-Chun; Chao, Tai-Ling; Lin, Shiau-Yu; Kao, Han-Chieh; Tsai, Ya-Min; Lu, De-Chao; Chiang, Yi-Wei; Chang, Sui-Yuan; Chang, Shih-Chung.
  • Lai GC; Department of Biochemical Science and Technology, College of Life Science, National Taiwan University, Taipei, 106, Taiwan.
  • Chao TL; Department of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan University, Taipei, 106, Taiwan; Genomics Research Center, Academia Sinica, Taipei, 115, Taiwan.
  • Lin SY; Department of Biochemical Science and Technology, College of Life Science, National Taiwan University, Taipei, 106, Taiwan.
  • Kao HC; Department of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan University, Taipei, 106, Taiwan.
  • Tsai YM; Department of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan University, Taipei, 106, Taiwan.
  • Lu DC; Department of Biochemical Science and Technology, College of Life Science, National Taiwan University, Taipei, 106, Taiwan.
  • Chiang YW; Department of Biochemical Science and Technology, College of Life Science, National Taiwan University, Taipei, 106, Taiwan.
  • Chang SY; Department of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan University, Taipei, 106, Taiwan; Department of Laboratory Medicine, National Taiwan University Hospital, College of Medicine, National Taiwan University, Taipei, 106, Taiwan. Electronic address
  • Chang SC; Department of Biochemical Science and Technology, College of Life Science, National Taiwan University, Taipei, 106, Taiwan; Center of Biotechnology, National Taiwan University, Taipei, 106, Taiwan. Electronic address: shihchung@ntu.edu.tw.
Antiviral Res ; 200: 105290, 2022 04.
Article in English | MEDLINE | ID: covidwho-1734185
ABSTRACT
Neutralizing antibodies (NAbs) are believed to be promising prophylactic and therapeutic treatment against the coronavirus disease 2019 (COVID-19), which is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Here, we reported two mouse monoclonal antibodies 7 Eb-4G and 1Ba-3H that specifically recognized the receptor-binding domain (RBD) of SARS-CoV-2 spike (S) protein without exhibiting cross-reactivity with the S proteins of SARS-CoV and MERS-CoV. The binding epitopes of 7 Eb-4G and 1Ba-3H were respectively located in the regions of residues 457-476 and 477-496 in the S protein. Only 1Ba-3H exhibited the neutralizing activity for preventing the pseudotyped lentivirus from binding to the angiotensin-converting enzyme 2 (ACE2)-transfected HEK293T cells. The competitive ELISA further showed that 1Ba-3H interfered with the binding between RBD and ACE2. Epitope mapping experiments demonstrated that a single alanine replacement at residues 480, 482, 484, 485, and 488-491 in the RBD abrogated 1Ba-3H binding. 1Ba-3H exhibited the neutralizing activity against the wild-type, Alpha, Delta, and Epsilon variants of SARS-CoV-2, but lost the neutralizing activity against Gamma variant in the plaque reduction assay. On the contrary, 1Ba-3H enhanced the cellular infection of Gamma variant in a dose-dependent manner. Our findings suggest that the antibody-dependent enhancement of infection mediated by the RBD-specific antibody for different SARS-CoV-2 variants must be considered while developing the NAb.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Type of study: Randomized controlled trials Topics: Variants Limits: Animals / Humans Language: English Journal: Antiviral Res Year: 2022 Document Type: Article Affiliation country: J.antiviral.2022.105290

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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Type of study: Randomized controlled trials Topics: Variants Limits: Animals / Humans Language: English Journal: Antiviral Res Year: 2022 Document Type: Article Affiliation country: J.antiviral.2022.105290