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Basic Characteristics of Mutations
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Mutation Site
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Y107A |
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Mutation Site Sentence
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The complex was absent when HLA class II was co-expressed with a previously described gp42 point mutant (Y107A), that does not bind HLA class II (Silva et al., 2004). |
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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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BZLF2 |
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Standardized Encoding Gene
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BZLF2
|
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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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Cell line
|
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Immune
|
- |
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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
|
21550622
|
|
Title
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Investigation of the function of the putative self-association site of Epstein-Barr virus (EBV) glycoprotein 42 (gp42)
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Author
|
Rowe CL,Matsuura H,Jardetzky TS,Longnecker R
|
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Journal
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Virology
|
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Journal Info
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2011 Jul 5;415(2):122-31
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Abstract
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The Epstein-Barr virus (EBV) glycoprotein 42 (gp42) is a type II membrane protein essential for entry into B cells but inhibits entry into epithelial cells. X-ray crystallography suggests that gp42 may form dimers when bound to human leukocyte antigen (HLA) class II receptor (Mullen et al., 2002) or multimerize when not bound to HLA class II (Kirschner et al., 2009). We investigated this self-association of gp42 using several different approaches. We generated soluble mutants of gp42 containing mutations within the self-association site and found that these mutants have a defect in fusion. The gp42 mutants bound to gH/gL and HLA class II, but were unable to bind wild-type gp42 or a cleavage mutant of gp42. Using purified gp42, gH/gL, and HLA, we found these proteins associate 1:1:1 by gel filtration suggesting that gp42 dimerization or multimerization does not occur or is a transient event undetectable by our methods.
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Sequence Data
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-
|