Chaperone functions common to nonhomologous Epstein-Barr virus gL and Varicella-Zoster virus gL proteins.
Herpesviruses encode the complex-forming, essential glycoproteins gH and gL. Maturation and transport of gH are dependent on coexpression of its chaperone, gL. The gL proteins of alpha herpesviruses and gamma herpesviruses do not have a significant percentage of amino acid sequence homology. Yet, as we report herein, the diverse gL glycoproteins of Epstein-Barr virus (EBV) and varicella-zoster virus (VZV) were functionally interchangeable, although membrane expression and maturation of gH were separate functions for these viruses. In VZV both functions were performed by a single protein. EBV required two separate glycoproteins, one of which can be replaced by its homologous protein from VZV, a distant relative of EBV. Collectively, these results suggested that VZV gL is a simpler form of the gL chaperone protein than EBV gL.
Li
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Q
School of Biological Sciences, University of Missouri-Kansas City, 64110, USA.
Buranathai
C
C
Grose
C
C
Hutt-Fletcher
L M
LM
D014645:Herpesvirus 3, Human / Q000235:genetics*; D004854:Herpesvirus 4, Human / Q000235:genetics*; D008562:Membrane Glycoproteins / Q000235:genetics*; D018832:Molecular Chaperones / Q000235:genetics*; D014764:Viral Proteins / Q000235:genetics*
D008562:Membrane Glycoproteins; D018832:Molecular Chaperones; D014764:Viral Proteins; C103802:glycoprotein L, Human herpesvirus 4; C094648:glycoprotein gL, varicella-zoster virus