EBV Mutation Detail Information

Virus Mutation EBV Mutation Z214S


Basic Characteristics of Mutations
Mutation Site Z214S
Mutation Site Sentence As reported before, two Z proteins (Z214R/218R and Z214S/218S) containing mutations within the interface of Z214S/218S) containing mutations within the interface of the coiled-coil helix lost dimerization ability, as well as interaction with p65 (Fig. 1C, Z214R/218R data not shown) (Flemington and Speck, 1991; Gutschet al.,1994).
Mutation Level Amino acid level
Mutation Type Nonsynonymous substitution
Gene/Protein/Region BZLF1
Standardized Encoding Gene BZLF1  
Genotype/Subtype -
Viral Reference -
Functional Impact and Mechanisms
Disease Cell line    
Immune -
Target Gene NFKB1   
Clinical and Epidemiological Correlations
Clinical Information -
Treatment -
Location -
Literature Information
PMID 9123876
Title The bZip dimerization domain of the Epstein-Barr virus BZLF1 (Z) protein mediates lymphoid-specific negative regulation
Author Hong Y,Holley-Guthrie E,Kenney S
Journal Virology
Journal Info 1997 Mar 3;229(1):36-48
Abstract The Epstein-Barr virus (EBV) immediate-early (IE) protein, BZLF1 (Z), initiates the switch from latent to lytic infection, Z transactivation of an early viral promoter, BMRF1, is relatively inefficient in lymphoid cells (compared with epithelial cells), unless the other EBV IE protein, BRLF1, is also present. Cellular proteins, including the p65 component of NF-kappa B, have been shown to interact directly with Z in vitro through the bZip dimerization domain and inhibit Z-induced transactivation. Here we precisely define a residue within the bZip dimerization domain of Z (amino acid 200) which is required for interaction in vitro with the p65 component of NF-kappa B, but is not essential for Z homodimerization. In lymphoid cells, a Z mutant which has been altered at amino acid 200 (tyrosine to glutamic acid) transactivates both the early BMRF1 promoter and the immediate-early BZLF1 promoter (Zp) four- to fivefold better than wild-type Z. In contrast, mutation of amino acid 200 does not affect Z transactivator function in epithelial cells. The results suggest that Z function is specifically inhibited by a lymphoid-specific protein(s) through amino acid 200 in the bZip dimerization domain. Modulation of Z's activator function may help to regulate the stringency of viral latency in lymphocytes.
Sequence Data -
Mutation Information
Note
Basic Characteristics of Mutations
  • Mutation Site: The specific location in a gene or protein sequence where a change occurs.
  • Mutation Level: The level at which a mutation occurs, including the nucleotide or amino acid level.
  • Mutation Type: The nature of the mutation, such as missense mutation, nonsense mutation, synonymous mutation, etc.
  • Gene/Protein/Region: Refers to the specific region of the virus where the mutation occurs. Including viral genes, viral proteins, or a specific viral genome region. If the article does not specifically indicate the relationship between the mutation and its correspondence, the main
  • Gene/Protein/Region studied in the article is marked.
  • Genotype/Subtype: Refers to the viral genotype or subtype where the mutation occurs. If the article does not specifically indicate the relationship between the mutation and its correspondence, the main Genotype/Subtype studied in the article is marked.
  • Viral Reference: Refers to the standard virus strain used to compare and analyze viral sequences.
Functional Impact and Mechanisms
  • Disease: An abnormal physiological state with specific symptoms and signs caused by viral infection.
  • Immune: The article focuses on the study of mutations and immune.
  • Target Gene: Host genes that viral mutations may affect.
Clinical and Epidemiological Correlations
  • Clinical Information: The study is a clinical or epidemiological study and provides basic information about the population.
  • Treatment: The study mentioned a certain treatment method, such as drug resistance caused by mutations. If the study does not specifically indicate the relationship between mutations and their correspondence treatment, the main treatment studied in the article is marked.
  • Location: The source of the research data.
Literature Information
  • Sequence Data: The study provides the data accession number.