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10.1080/19420862.2020.1778435

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suck abstract from ncbi


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pmid32544372      MAbs 2020 ; 12 (1): 1778435
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  • Potent neutralization of SARS-CoV-2 by human antibody heavy-chain variable domains isolated from a large library with a new stable scaffold #MMPMID32544372
  • Sun Z; Chen C; Li W; Martinez DR; Drelich A; Baek DS; Liu X; Mellors JW; Tseng CT; Baric RS; Dimitrov DS
  • MAbs 2020[Jan]; 12 (1): 1778435 PMID32544372show ga
  • Effective therapies are urgently needed for COVID-19. Here we describe the identification of a new stable human immunoglobulin G1 heavy-chain variable (VH) domain scaffold that was used for the construction of a large library, lCAT6, of engineered human VHs. This library was panned against the receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) glycoprotein. Two VH domains (VH ab6 and VH m397) were selected and fused to Fc for increased half-life in circulation. The VH-Fc ab6 and m397 specifically neutralized SARS-CoV-2 with high potencies (50% neutralization at 0.35 microg/ml and 1.5 microg/ml, respectively) as measured by two independent replication-competent virus neutralization assays. Ab6 and m397 competed with ACE2 for binding to RBD, suggesting a competitive mechanism of virus neutralization. These VH domains may have potential applications for prophylaxis and therapy of COVID-19 alone or in combination, as well as for diagnosis and as tools for research.
  • |*Coronavirus Infections[MESH]
  • |*Pandemics[MESH]
  • |*Pneumonia, Viral[MESH]
  • |Antibodies, Monoclonal[MESH]
  • |Antibodies, Neutralizing/*immunology[MESH]
  • |Antibodies, Viral/*immunology[MESH]
  • |Betacoronavirus/*immunology[MESH]
  • |COVID-19[MESH]
  • |Humans[MESH]
  • |Immunoglobulin Heavy Chains/immunology[MESH]
  • |Peptide Library[MESH]
  • |SARS-CoV-2[MESH]


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