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Basic Characteristics of Mutations
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Mutation Site
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G282A |
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Mutation Site Sentence
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Moreover, a G282A substitution abolished the binding of E protein to LAMR1 and inhibited LAMR1-mediated E protein deubiquitination. |
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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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E |
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Standardized Encoding Gene
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envelope
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Genotype/Subtype
|
- |
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Viral Reference
|
KU955589.1
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Functional Impact and Mechanisms
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|
Disease
|
Cell line
|
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Immune
|
- |
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Target Gene
|
RPSA
|
|
Clinical and Epidemiological Correlations
|
|
Clinical Information
|
- |
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Treatment
|
- |
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Location
|
- |
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Literature Information
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|
PMID
|
34282707
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Title
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LAMR1 restricts Zika virus infection by attenuating the envelope protein ubiquitination
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Author
|
Hu D,Wang Y,Li A,Li Q,Wu C,Shereen MA,Huang S,Wu K,Zhu Y,Wang W,Wu J
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Journal
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Virulence
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Journal Info
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2021 Dec;12(1):1795-1807
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Abstract
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Zika virus (ZIKV) infection can cause severe neurological disorders, including Guillain-Barre syndrome and meningoencephalitis in adults and microcephaly in fetuses. Here, we reveal that laminin receptor 1 (LAMR1) is a novel host resistance factor against ZIKV infection. Mechanistically, we found that LAMR1 binds to ZIKV envelope (E) protein via its intracellular region and attenuates E protein ubiquitination through recruiting the deubiquitinase eukaryotic translation initiation factor 3 subunit 5 (EIF3S5). We further found that the conserved G282 residue of E protein is essential for its interaction with LAMR1. Moreover, a G282A substitution abolished the binding of E protein to LAMR1 and inhibited LAMR1-mediated E protein deubiquitination. Together, our results indicated that LAMR1 represses ZIKV infection through binding to E protein and attenuating its ubiquitination.
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Sequence Data
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-
|
|
|