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Basic Characteristics of Mutations
|
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Mutation Site
|
L351G |
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Mutation Site Sentence
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Together, these experiments show that mutation of either Y349 or LL350–351 disrupts BMRF-2 transport to the basolateral membranes of polarized oral epithelial cells. |
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Mutation Level
|
Amino acid level |
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Mutation Type
|
Nonsynonymous substitution |
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Gene/Protein/Region
|
BMRF2 |
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Standardized Encoding Gene
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BMRF2
|
|
Genotype/Subtype
|
- |
|
Viral Reference
|
-
|
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Functional Impact and Mechanisms
|
|
Disease
|
Cell line
|
|
Immune
|
- |
|
Target Gene
|
-
|
|
Clinical and Epidemiological Correlations
|
|
Clinical Information
|
- |
|
Treatment
|
- |
|
Location
|
- |
|
Literature Information
|
|
PMID
|
19394065
|
|
Title
|
EBV BMRF-2 facilitates cell-to-cell spread of virus within polarized oral epithelial cells
|
|
Author
|
Xiao J,Palefsky JM,Herrera R,Berline J,Tugizov SM
|
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Journal
|
Virology
|
|
Journal Info
|
2009 Jun 5;388(2):335-43
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Abstract
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We previously reported that the Epstein-Barr virus (EBV) BMRF-2 protein plays an important role in EBV infection of polarized oral epithelial cells by interacting with beta1 and alphav family integrins. Here we show that infection of polarized oral epithelial cells with B27-BMRF-2(low) recombinant virus, expressing a low level of BMRF-2, resulted in significantly smaller plaques compared with infection by parental B95-8 virus. BMRF-2 localized in the trans-Golgi network (TGN) and basolateral sorting vesicles and was transported to the basolateral membranes of polarized epithelial cells. Mutation of the tyrosine- and dileucine-containing basolateral sorting signal, YLLV, in the cytoplasmic domain of BMRF-2 led to the failure of its accumulation in the TGN and its basolateral transport. These data show that BMRF-2 may play an important role in promoting the spread of EBV progeny virions through lateral membranes of oral epithelial cells.
|
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Sequence Data
|
-
|