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Basic Characteristics of Mutations
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Mutation Site
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G151R |
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Mutation Site Sentence
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Additionally, the 3L11 escape strains had G151R (Gly151 Arg151) and S152P (Ser152 Pro152) mutations within a conserved antigenic site A near the RBS that were not observed in field strains. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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HA |
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Standardized Encoding Gene
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HA
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Genotype/Subtype
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H7N9 |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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Influenza A
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Immune
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Y |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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China |
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Literature Information
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PMID
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31336147
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Title
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Rapid isolation of a potent human antibody against H7N9 influenza virus from an infected patient
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Author
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Li J,Yang Y,Wang M,Ren X,Yang Z,Liu L,Zhang G,Chen Q,Yang W,Chen YH,Wan X
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Journal
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Antiviral research
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Journal Info
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2019 Oct;170:104564
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Abstract
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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(151)-->Arg(151)) and S152P (Ser(152)-->Pro(152)) 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.
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Sequence Data
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-
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