Literature DB >> 15003866

The Epstein-Barr virus BFRF1 and BFLF2 proteins interact and coexpression alters their cellular localization.

Cathleen M Lake1, Lindsey M Hutt-Fletcher.   

Abstract

The BFRF1 protein of Epstein-Barr virus (EBV) is a recently identified membrane protein that is the homolog of the alphaherpesvirus UL34 gene product. We report here that a yeast two-hybrid screen identified the BFLF2 gene product, a homolog of alphaherpesvirus UL31, as a protein that interacts with BFRF1. Expression of BFLF2 in mammalian cells revealed a protein of approximately 28 kDa that associated with BFRF1 in a noncovalently linked complex. When expressed alone, the BFRF1 protein was found in the cytoplasm and perinuclear region. BFLF2 was found diffusely in the nucleus in the absence of BFRF1, but coexpression of BFRF1 and BFLF2 resulted in colocalization of the two proteins at the nuclear rim. These data recapitulate the behavior of the alphaherpesvirus homologs of BFRF1 and BFLF2 and suggest that functional as well as structural and positional homology may be conserved.

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Year:  2004        PMID: 15003866     DOI: 10.1016/j.virol.2003.11.018

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  47 in total

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9.  Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins.

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