Journal article
Chaperone functions common to nonhomologous Epstein-Barr virus gL and Varicella-Zoster virus gL proteins
Journal of virology, Vol.71(2), pp.1667-1670
02/1997
DOI: 10.1128/jvi.71.2.1667-1670.1997
PMCID: PMC191228
PMID: 8995697
Abstract
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.
Details
- Title: Subtitle
- Chaperone functions common to nonhomologous Epstein-Barr virus gL and Varicella-Zoster virus gL proteins
- Creators
- Qingxue Li - School of Biological Sciences, University of Missouri-Kansas City, 64110, USACharles Grose - School of Biological Sciences, University of Missouri-Kansas City, 64110, USAChantanee Buranathai - School of Biological Sciences, University of Missouri-Kansas City, 64110, USAL M Hutt-Fletcher - School of Biological Sciences, University of Missouri-Kansas City, 64110, USA
- Resource Type
- Journal article
- Publication Details
- Journal of virology, Vol.71(2), pp.1667-1670
- DOI
- 10.1128/jvi.71.2.1667-1670.1997
- PMID
- 8995697
- PMCID
- PMC191228
- ISSN
- 0022-538X
- eISSN
- 1098-5514
- Language
- English
- Date published
- 02/1997
- Academic Unit
- Stead Family Department of Pediatrics; Infectious Disease (Pediatrics)
- Record Identifier
- 9984093225302771
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