Host shutoff during productive Epstein-Barr virus infection is mediated by BGLF5 and may contribute to immune evasion

Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3366-71. doi: 10.1073/pnas.0611128104. Epub 2007 Feb 21.

Abstract

Relatively little is known about immune evasion during the productive phase of infection by the gamma(1)-herpesvirus Epstein-Barr virus (EBV). The use of a unique system to isolate cells in lytic cycle allowed us to identify a host shutoff function operating in productively EBV-infected B cells. This impairment of protein synthesis results from mRNA degradation induced upon expression of the early lytic-cycle gene product BGLF5. Recently, a gamma(2)-herpesvirus, Kaposi sarcoma herpesvirus, has also been shown to encode a host shutoff function, indicating that host shutoff appears to be a general feature of gamma-herpesviruses. One of the consequences of host shutoff is a block in the synthesis of HLA class I and II molecules, reflected by reduced levels of these antigen-presenting complexes at the surface of cells in EBV lytic cycle. This effect could lead to escape from T cell recognition and elimination of EBV-producing cells, thereby allowing generation of viral progeny in the face of memory T cell responses.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigen Presentation
  • B-Lymphocytes / cytology
  • B-Lymphocytes / immunology*
  • Cell Line, Tumor
  • Deoxyribonucleases / immunology*
  • Epstein-Barr Virus Infections / immunology*
  • Gene Expression Regulation / immunology*
  • Histocompatibility Antigens Class I / biosynthesis
  • Histocompatibility Antigens Class I / metabolism*
  • Histocompatibility Antigens Class II / biosynthesis
  • Histocompatibility Antigens Class II / metabolism*
  • Humans
  • Microscopy, Fluorescence
  • Protein Biosynthesis / immunology*
  • Viral Proteins / immunology*

Substances

  • Histocompatibility Antigens Class I
  • Histocompatibility Antigens Class II
  • Viral Proteins
  • Deoxyribonucleases
  • deoxyribonuclease, Epstein-Barr virus