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Characterization of interaction of gH and gL glycoproteins of varicella-zoster virus: their processing and trafficking

Lucie Mareová¹

Roman ák¹

Michael Mare²

árka Nmeková¹

Institute of Haematology and Blood Transfusion, Dept of Experimental Virology, Prague 128 20, Czech Republic¹
Institute of Organic Chemistry and Biochemistry, Dept of Protein Biochemistry, Prague 166 10, Czech Republic²

Author for correspondence: Lucie Mareová. Fax +420 2 21977392. e-mail lucie-maresova{at}uiowa.edu

Varicella-zoster virus (VZV) glycoproteins gH and gL were examined in a recombinant vaccinia virus system. Single expression of glycoprotein gL produced two molecular forms: an 18 kDa form and a 19 kDa form differing in size by one endoglycosidase H-sensitive N-linked oligosaccharide. Coexpression of gL and gH resulted in binding of the 18 kDa gL form with the mature form of gH, while the 19 kDa gL form remained uncomplexed. The glycosylation processing of gL was not dependent on gH; however, gL was required for the conversion of precursor gH (97 kDa) to mature gH (118 kDa). Subsequent analyses indicated that gL (18 kDa) was a more completely processed gL (19 kDa). Screening of the culture media revealed that gH and gL were secreted, but only if coexpressed and complexed together. The secreted form of gL was 18 kDa while that of gH was 114 kDa. The fact that secreted gH was smaller than intracytoplasmic gH suggested a proteolytic processing event prior to secretion. The 19 kDa form of gL was never secreted. These findings support a VZV gL recycling pathway between the endoplasmic reticulum and the cis-Golgi apparatus.

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