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pubmed-article:8995697pubmed:abstractTextHerpesviruses 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.lld:pubmed
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pubmed-article:8995697pubmed:articleTitleChaperone functions common to nonhomologous Epstein-Barr virus gL and Varicella-Zoster virus gL proteins.lld:pubmed
pubmed-article:8995697pubmed:affiliationSchool of Biological Sciences, University of Missouri-Kansas City, 64110, USA.lld:pubmed
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