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Basic Characteristics of Mutations
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Mutation Site
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I152V |
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Mutation Site Sentence
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L and S protein expression was not affected in mutants that replaced Ile152 with Val or Phe (I152V or I152F), but the expression of L protein was impaired in those with Thr, Ser, or Asp (I152T, I152S, or I152N). |
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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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S |
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Standardized Encoding Gene
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S
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Genotype/Subtype
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D;B;A;C |
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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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Cell line
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Immune
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- |
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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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- |
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Literature Information
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PMID
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35084739
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Title
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Establishment of monoclonal antibodies broadly neutralize infection of hepatitis B virus
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Author
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Zhang H,Itoh Y,Suzuki T,Ihara KI,Tanaka T,Haga S,Enatsu H,Yumiya M,Kimura M,Takada A,Itoh D,Shibazaki Y,Nakao S,Yoshio S,Miyakawa K,Miyamoto Y,Sasaki H,Kajita T,Sugiyama M,Mizokami M,Tachibana T,Ryo A,Moriishi K,Miyoshi E,Kanto T,Okamoto T,Matsuura Y
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Journal
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Microbiology and immunology
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Journal Info
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2022 Apr;66(4):179-192
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Abstract
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Antibodies against hepatitis B virus S protein can protect against hepatitis B virus (HBV) infection. Therefore, hepatitis B immunoglobulin (HBIG), which contains HBsAb, is used clinically as a therapy for HBV infection. In this study, a series of monoclonal antibodies that recognize multiple HBV genotypes was obtained. All the antibodies recognized conformational epitopes of S protein, but not linear epitopes. Several antibodies neutralized HBV infection and exhibited strong affinities and neutralizing activities. Antigenic epitope analysis demonstrated that they recognized residue Ile152 of S protein, which is localized outside the ""a"" determinant. Ile152 is highly conserved, and a mutation in this residue resulted in reduced expression of large hepatitis B surface proteins (L protein), suggesting that the amino acid at this position is involved in the expression of L protein. In addition, the antibodies neutralized the infection of hepatitis D virus possessing a Gly145 mutation to Arg in S protein, which is a well-known escape mutation against HBIG treatment. Using mouse monoclonal antibodies, a humanized antibody possessing affinities and neutralizing activities similar to those of the original mouse antibody was successfully established. The antibodies generated in this study may have the potential for use in alternative antibody therapies for HBV infection.
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Sequence Data
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-
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