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Characterization of the Ordered Domain of an Epstein Barr Viral Tegument Protein
Author(s) -
Marlowe Megan E.,
Gorres Kelly
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.761.8
Subject(s) - viral tegument , lytic cycle , biology , virus , capsid , epstein–barr virus , gene , viral protein , viral life cycle , virology , herpes simplex virus , viral structural protein , protein domain , microbiology and biotechnology , viral entry , viral replication , genetics
Epstein Barr virus (EBV) is the first known human herpes virus to cause cancer. The virus also causes mononucleosis. Within the viral life cycle, the virus can switch between latent and lytic phases. In the latent phase, very few genes are expressed and new virions are not produced. During the lytic, or active, phase there is an increase in viral gene expression, proteins are produced, and infectious viral particles are released from the cell. The structure of Epstein‐Barr virus, like all herpesviruses, contains a tegument layer, which surrounds the genome‐containing capsid. The proteins in the tegument are delivered to the cell immediately upon infection. These proteins conduct a wide variety of functions in the viral life cycle. This project investigates an EBV tegument protein essential for virus production, but its role is unknown. Bioinformatics analysis identified homologs in other herpesviruses, but no similarity to any protein in any other organism. Amino acid sequences within a protein can exhibit order and disorder, relative to its three dimensional structure. A database called MobiDB was used to predict regions of order versus disorder from the amino acid sequence. The C‐terminal portion of the protein is calculated to be low complexity or disordered, whereas an N‐terminal domain is ordered. To express this structured part of the protein, an early stop codon was inserted into the gene. The protein with a His‐tag was overexpressed in E. coli and purified by nickel‐affinity chromatography. The objective of the experiments conducted is to study the function and characteristics of the structured domain of a tegument protein expressed in the lytic phase of the EBV infection. Support or Funding Information This work was supported by the UWL College of Science and Health and a UWL Faculty Research Grant to K.G.