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Basic Characteristics of Mutations
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Mutation Site
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G102S |
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Mutation Site Sentence
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Out of the 23 isolates, 15 (65%) exhibited single or multiple substitutions, which resulted to specific amino acid changes as follows: Tyrosine (Y) to Cysteine (C) at position 100, Glutamine (Q) to Lysine (K) at position 101, Glycine (G) to Serine (S) at position 102, Methionine (M) to Isoleucine (I) at position 103, Leucine (L) to Proline (P) at position 109, Isoleucine (I) to Leucine (L) at position 110, Leucine (L) to Isoleucine (I) at position 110, Threonine (T) to Serine (S) at position 113, Threonine (T) to Asparagine (N) at position 116, Serine (S) to Arginine (R) at position 117, Isoluecine (I) to Threonine (T) at position 126, Isoleucine (I) to Serine (S) at position 126, Proline (P) to Threonine (T) at position 127, Glycine (G) to Serine (S) at position 130, Methionine (M) to Threonine (T) at position 133, Phenylalanine (F) to Isoleucine (I) at position 134, Serine (S) to Leucine (L) at position 136, and Aspartic acid (D) to Alanine (A) at position 144 as shown in Figures 1-3. |
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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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- |
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Viral Reference
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Fig.1;Fig.2;Fig.3
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Functional Impact and Mechanisms
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Disease
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Hepatitis B, Chronic
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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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24009186
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Title
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Unique surface gene variants of hepatitis B virus isolated from patients in the Philippines
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Author
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Baclig MO,Alvarez MR,Gopez-Cervantes J,Natividad FF
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Journal
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Journal of medical virology
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Journal Info
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2014 Feb;86(2):209-16
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Abstract
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Point mutations and multiple variants across the ""a"" determinant can destroy the antigenicity and immunogenicity of hepatitis B virus (HBV) leading to false negative assay and vaccine escape. In this study, the presence of surface gene variants of HBV was investigated among patients clinically diagnosed with chronic hepatitis B and positive for HBV DNA from 2002 to 2009. Sequence analysis of the surface gene of HBV showed that 23 (43%) of the 53 isolates had variations. Out of the 23 isolates, 15 (65%) exhibited single or multiple substitutions, which resulted to specific amino acid changes. The remaining 8 (35%) isolates had silent mutations. The amino acid substitution M133T which was associated with failure of HBsAg detection was found in one isolate (7%, 1/15), while the amino acid substitution D144A which was associated with vaccine escape was observed in one isolate (7%, 1/15). No G145R mutation was observed. Of the 15 isolates with identified single or multiple substitutions, 6 (40%) were found to have unique sequences which caused changes in the hydrophobicity profile in the protein. Unique sequence variants at amino acid positions M103I, L109P, S117R, F134I, and S136L found in this study have not yet been reported. These data should be taken into account when developing next generation HBV assays to detect both common and unique variants, and when new HBV vaccines will be designed.
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Sequence Data
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HM371272-HM371323;AEI70508-AEI70555
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