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Basic Characteristics of Mutations
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Mutation Site
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K141E |
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Mutation Site Sentence
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Consistent with our previous report (Kwei et al., 2013), virion secretion was impaired by the T114R, T115A, K141E, and D144G immune escape mutations introduced into the 0.7mer construct (Fig. 1E & F). |
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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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Viral Reference
|
-
|
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Functional Impact and Mechanisms
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Disease
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Hepatitis B Virus Infection
|
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Immune
|
Y |
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Target Gene
|
-
|
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Clinical and Epidemiological Correlations
|
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Clinical Information
|
- |
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Treatment
|
- |
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Location
|
- |
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Literature Information
|
|
PMID
|
29604477
|
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Title
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Impact of immune escape mutations and N-linked glycosylation on the secretion of hepatitis B virus virions and subviral particles: Role of the small envelope protein
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Author
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Bi X,Tong S
|
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Journal
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Virology
|
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Journal Info
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2018 May;518:358-368
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Abstract
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Hepatitis B virus (HBV) expresses three co-terminal envelope proteins: large (L), middle (M), and small (S), with the S protein driving the secretion of both virions and subviral particles. Virion secretion requires N-linked glycosylation at N146 in the S domain but can be impaired by immune escape mutations. An M133T mutation creating a novel glycosylation site at N131could rescue virion secretion of N146Q mutant (loss of original glycosylation site) and immune escape mutants such as G145R. Here we demonstrate that other novel N-linked glycosylation sites could rescue virion secretion of the G145R and N146Q mutants to variable extents. Both G145R and N146Q mutations impaired virion secretion through the S protein. The M133T mutation restored virion secretion through the S protein, and could work in trans. Impaired virion secretion was not necessarily associated with a similar block in the secretion of subviral particles.
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Sequence Data
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-
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