tetano
Editor, Senior Moderator
Antiviral Res. 2019 Jul 20;170:104564. doi: 10.1016/j.antiviral.2019.104564. [Epub ahead of print]
[h=1]Rapid isolation of a potent human antibody against H7N9 influenza virus from an infected patient.[/h] Li J[SUP]1[/SUP], Yang Y[SUP]2[/SUP], Wang M[SUP]3[/SUP], Ren X[SUP]4[/SUP], Yang Z[SUP]5[/SUP], Liu L[SUP]6[/SUP], Zhang G[SUP]6[/SUP], Chen Q[SUP]1[/SUP], Yang W[SUP]7[/SUP], Chen YH[SUP]8[/SUP], Wan X[SUP]9[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza virus A H7N9 remains a serious threat to public health due to the lack of effective vaccines and drugs. In this study, a neutralizing human antibody named 3L11 was rapidly isolated from the switched memory B cells of a patient infected with H7N9. The antibody 3L11 was encoded by the heavy-chain VH1-8 gene and the light-chain VL2-13 gene that had undergone somatic mutations, and conferred high affinity binding to H7N9 hemagglutinins (HAs). It promoted killing of infected cells by antibody-dependent cell-mediated cytotoxicity (ADCC). Epitope mapping by mass spectroscopy (MS) indicated that 3L11 bound to the peptide 149-175 of HAs that contained the 150-loop of the receptor-binding site (RBS). Additionally, the 3L11 escape strains had G151R (Gly[SUP]151[/SUP]→Arg[SUP]151[/SUP]) and S152P (Ser[SUP]152[/SUP]→Pro[SUP]152[/SUP]) mutations within a conserved antigenic site A near the RBS that were not observed in field strains. Importantly, 3L11 fully protected mice against a lethal H7N9 virus challenge, in both pre- and postexposure administration regimens. Altogether, this work demonstrates the feasibility of rapid isolation of neutralizing H7N9 antibodies from infected patients and provides a potential prophylactic and therapeutic agent against H7N9 viruses.
Copyright ? 2019 Elsevier B.V. All rights reserved.
[h=4]KEYWORDS:[/h] ADCC; Antigenic site A; H7N9; Human monoclonal antibody; Mass spectroscopy; Switched memory B cells
PMID: 31336147 DOI: 10.1016/j.antiviral.2019.104564
[h=1]Rapid isolation of a potent human antibody against H7N9 influenza virus from an infected patient.[/h] Li J[SUP]1[/SUP], Yang Y[SUP]2[/SUP], Wang M[SUP]3[/SUP], Ren X[SUP]4[/SUP], Yang Z[SUP]5[/SUP], Liu L[SUP]6[/SUP], Zhang G[SUP]6[/SUP], Chen Q[SUP]1[/SUP], Yang W[SUP]7[/SUP], Chen YH[SUP]8[/SUP], Wan X[SUP]9[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza virus A H7N9 remains a serious threat to public health due to the lack of effective vaccines and drugs. In this study, a neutralizing human antibody named 3L11 was rapidly isolated from the switched memory B cells of a patient infected with H7N9. The antibody 3L11 was encoded by the heavy-chain VH1-8 gene and the light-chain VL2-13 gene that had undergone somatic mutations, and conferred high affinity binding to H7N9 hemagglutinins (HAs). It promoted killing of infected cells by antibody-dependent cell-mediated cytotoxicity (ADCC). Epitope mapping by mass spectroscopy (MS) indicated that 3L11 bound to the peptide 149-175 of HAs that contained the 150-loop of the receptor-binding site (RBS). Additionally, the 3L11 escape strains had G151R (Gly[SUP]151[/SUP]→Arg[SUP]151[/SUP]) and S152P (Ser[SUP]152[/SUP]→Pro[SUP]152[/SUP]) mutations within a conserved antigenic site A near the RBS that were not observed in field strains. Importantly, 3L11 fully protected mice against a lethal H7N9 virus challenge, in both pre- and postexposure administration regimens. Altogether, this work demonstrates the feasibility of rapid isolation of neutralizing H7N9 antibodies from infected patients and provides a potential prophylactic and therapeutic agent against H7N9 viruses.
Copyright ? 2019 Elsevier B.V. All rights reserved.
[h=4]KEYWORDS:[/h] ADCC; Antigenic site A; H7N9; Human monoclonal antibody; Mass spectroscopy; Switched memory B cells
PMID: 31336147 DOI: 10.1016/j.antiviral.2019.104564